The genetically modified maize MON-89Ø34-3, as described in the application, expresses the Cry1A.105 and Cry2Ab2 proteins which provide protection to certain lepidopteran pests.

 

Please see the EU relevant links below.

Event specific real-time quantitative PCR based method for genetically modified maize MON-89Ø34-3. - Validated by the Community reference laboratory established under Regulation (EC) No 1829/2003. Please see the EU relevant links below.

• Inheritance studies conducted indicated that Mendelian segregation exists, • New expression proteins are found in low levels of grain, • It is substantially and nutritionally equivalent to its non-transgenic counterpart, • No evidence of any similarity or homology with toxic proteins was found, • The studies presented to evaluate the potential allergenicity show that no allergenic substances are expressed, It is concluded that the corn event MON89034 is similar to its conventional counterpart, therefore, it is as safe and no less nutritious than conventional commercial corn hybrids. http://www.senasa.gob.ar/sites/default/files/ARBOL_SENASA/INFORMACION/6_7_y_8_-mon89034xmon88017_espanol.pdf

MON 89034 corn is protected against a range of lepidopteran insect larvae including
European corn borer, Asian corn borer, southwestern corn borer, sugarcane borer, fall
armyworm and corn earworm.
Protection is achieved through expression in the plant of two insecticidal Cry proteins,
Cry1A.105 and Cry2Ab2, derived from Bacillus thuringiensis, a common soil bacterium.
Cry1A.105, encoded by the cry1A.105 gene, is a chimeric protein made up of different
functional domains derived from three wild-type Cry proteins from B. thuringiensis
subspecies kurstaki and aizawai. The Cry2Ab2 protein is encoded by the cry2Ab2 gene
derived from B. thuringiensis subspecies kurstaki.
The Cry proteins exert their effect on the host insect by causing lysis of midgut epithelial cells, which leads to gut paralysis, cessation of feeding and eventual death of the insect. The lysis of the midgut epithelial cells is mediated by the binding of the activated Cry protein to specialised receptors on these cells.
Hybrid corn lines containing the MON 89034 transformation event are intended for
cultivation in North America and are not intended to be grown in either Australia or New Zealand. Food from MON 89034 corn will therefore be entering the Australian and New Zealand food supply as imported, largely processed food products.

commercial release of genetically modified corn resistant to insects of the order Lepidoptera MON 89034

The insect resistant MON 89034 corn was generated by transformation of hybrid LH172, mediated by Agrobacterium tumefaciens sp. with plasmid PV-ZMIR245 containing genes cr1A.105 and cry2Ab2. Proteins Cry1a.105 and Cry2Ab2 are codified by such genes, which are well known and characterized as insecticide proteins derived from soil bacterium Bacillus thuringiensis. Characterization of DNA inserted in MON 89034 corn was conducted through laboratory analyses showing that MON 89034 corn contains one single functional copy of genes cr1A.105 and cry2Ab2 inserted in its genome. Currently, the general mechanism of the Cry protein insecticide activity is well understood and Cry proteins comprehend different functional domains with highly conserved regions. Several field experiments for assaying agronomic and phenotypic characteristics of MON 89034 – contrasting with the control conventional corn of the same phenotype – were conducted during the 2007/2008 harvest in four representative locations of corn culture in Brazil: Cachoeira Dourada, State of Minas Gerais; Sorriso, State of Mato Grosso do Sul; Rolândia, State of Paraná; and Não-Me-Toques, State of Rio Grande do Sul. Phenotypic and agronomic characteristics of MON 89034 corn were assayed regarding its ecologic impact and potential as an invading plant. The studies covered several parameters, including: characteristics of plant growth and development, seed germination, pollen characteristics and observations for each plant-insect, plant-disease and plant-abiotic stress interaction. The results indicated that the MON 89034 corn has no characteristics that could pose risk as an invading plant or increase ecological risk when compared with conventional corn. Data on ecological interactions indicate that MON 89034 corn fails to grant greater susceptibility or tolerance to specific diseases, insects (except target-insects) and abiotic stress. The data ratify the idea that MON 89034 corn poses no risk of becoming an invading plant or of generating significant ecological impact when compared with conventional corn. Adverse effects in human and animal alimentary chain resulting from ingestion of MON 89034 corn and its derivatives are not expected based on an assay of alimentary safety of MON 89034 corn and its expressed proteins Cry1A.105 and Cry2Ab2. Allergic reactions to Cry proteins were not confirmed in application of microbial products derived from Bacillus thuringiensis for over four decades of use. Dietary safety of proteins Cry1A.105 and Cry2Ab2 present in food and rations derived from MON 89034 corn was assessed for risks posed to humans and animals and it was demonstrated that both proteins fail to show acute toxicity and do not cause adverse effect, even in high doses. Proteins Cry1A.105 and Cry2Ab2 are rapidly digested in simulated gastric juices, where 95% to 99% of proteins were digested in simulated gastric juices in a time not exceeding thirty seconds. Therefore the proteins, which are rapidly digested in the gastrointestinal tract of mammals, have negligible probability to cause allergies when consumed. Proteins Cry1A.105 and Cry2Ab2 do not share any similarity with amino acid sequences of known allergens or toxic proteins that may cause adverse effects in mammals. Dietary products and rations containing, or manufactured with, MON 89034 corn are as safe for human and animal consumption as the food manufactured with conventional corn. Potential adverse effects of MON 89034 corn to animal health were assayed in studies with mammals and birds, and the results corroborated the dietary safety of MON 89034 corn and proteins Cry1A.105 and Cry2Ab2 contained on this corn. Horizontal gene flow between MON 89034 corn and other species, even very closely related ones, have practically no probability of happening, since feral species related to corn do not occur in Brazil. Coexistence among corn cultivars (either improved or creole) and transgenic corn cultivars is possible from the agronomic viewpoint, and therefore the provisions of CTNBio Ruling Resolution nº4 shall be followed. Thus, analyses of the data supplied by applicant, as well as analysis of independent scientific literature, lead to a conclusion that proteins Cry1A.105 and Cry2Ab2 are innocuous and that MON 89034 corn is not potentially a cause of significant degradation of the environment; or of risks to human and animal health. These are the underlying reasons for the absence of restrictions to the use of MON 89034 corn and its derivatives. TECHNICAL OPINION I. GMO Identification GMO designation: MON 89034 corn. Applicant: Monsanto do Brasil Ltda. Species: Zea Mays L. Inserted characteristics: Resistance to insects. Method of insertion: MON 89034 corn, rated as Risk Class I, was produced though the methodology of transformation mediated by Agrobacterium tumefaciens sp. with plasmid PV-ZMIR245. Prospective use: Free registration, use, essays, tests, sowing, transport, storage, marketing, consumption, import, release into the environment and discarding. II. General Information Corn, (Zea mays L.) belongs to the Maydeae tribe, which belongs to subfamily Panicoideae of the Gramineae family. The Maydeae tribe includes genera Zea and Tripsacum in the Western Hemisphere and Coix, Polytoca, Chionachne, Schlerachne and Trilogachne in Asia. The Zea genus includes two sections: Luxiriantes and Zea. Corn (Zea Mays L.) is a separate species within subgenus Zea, together with three subspecies. Another genus included in the Maydeae tribe is the Tripsacum. Tripsacum includes sixteen species featuring a basic number of 18 chromosomes (n = 18), and the different Tripsacum species include multiples of 18 chromosomes within the interval of 2n = 36 to 2n = 108. Corn has a history of over eight thousand years in the Americas and is cultivated since the Pre-Columbian era. Among higher plants, corn is one of the best scientifically characterized and is currently the cultivated species that reached the highest degree of domestication and is unable to survive in nature but when cultivated by man(1). There are currently over 300 identified varieties of corn and, within each such variety there are thousands of cultivars. Corn is one of the most important food sources worldwide and used as input for a variety of food products, rations and industrial products. Brazil is the third largest world producer of corn, with a yield of about 35 million tons in 2005, following the United States of America (282 million tons) and China (139 million tons)(2). Corn is the second most planted culture in Brazil and is cultivated basically in two harvests practically all over the Brazilian territory. Regarding production, corn is second in a list of the largest Brazilian cultures, second only to soybeans(3). Brazil is a large world producer of corn, but it has also a significant consumption of this grain. National consumption is so high that an absence of the second crop would cause the need to import corn to meet national demand. Insect infestation in the tropics is higher than in temperate regions, where damages are higher. Among corn pests, importance of the fall armyworm (Spodoptera frugiperda) shall be underlined. Cruz et al.(4) estimated that the losses in Brazil caused by infestations of Spodoptera frugiperda reached 400 million Dollars each year. From 1999, occurrence of Spodoptera frugiperda increased and therefore, losses soared. Other species of the Lepidoptera order are important pests in the culture of corn, such as the corn earworm (Helicoverpa Zea) and stalk borer (Diatraea Saccharalis). Estimates are that the three species may damage up to 34% of corn production. The main controlling measure for insects in corn farming in Brazil has been the use of insecticides. In some of Brazilian Center-Western areas, for instance, tenths of insecticide spraying are needed for a single cycle of culture. Another measure to control pests would be the use of resistant cultivars. However, obtaining insect resistant corn cultivars by means of classic genetic improvement has not been as successful as desired. For Spodoptera frugiperda, several attempts have been made, with limited success(5). MON 89034 corn produces proteins Cry1A.105 and Cry2Ab2, derived from Bacillus thuringiensis, that are active against important pest lepidopterans in this culture. Compared with the corn containing the single event MON 810, MON 89034 corn controls a wider range of pests. MON 89034 corn provides efficient control against fall armyworm (Spodoptera frugiperda) over the whole harvest. Besides, MON 89034 corn gives significantly higher protection against damages caused by cotton bollworm (Helicoverpa Zea) when compared to genetically modified corn containing just one protein, and a high control of Ostrinia insects, such as European corn borer and Asian corn borer, and of Diatraea insects, such as stalk worm. The main corn pests in Brazil that are targets for corn containing event MON 89034 will be the fall armyworm, corn earworm and stalkworm. Brazil is held the world third larger consumer of agricultural pesticides, where currently there are 142 registered corn pesticides and, out of them, 107 have caterpillars as targets. There are several records of resistance for the constant and indiscriminate use of insecticides in corn culture in Brazil. Besides, one of the important factors affecting Brazilian farmers’ health is the use of agricultural pesticides, responsible for intoxicating a million individuals each year(6). III. Description of the GMO and Proteins Expressed MON 89034 corn was produced through the methodology of genetic transformation mediated by Agrobacterium tumefaciens, using the binary plasmid PV-ZMIR245. The plasmid consists of two separate T-DNA regions, each of them involved by the right and left border regions of the Ti plasmid(7). One T-DNA (T DNA I) contains genes cr1A.105 and cry2Ab2, while the other T-DNA (T DNA II) contains gene nptII, which grants resistance to the kanamycin antibiotic and was used in the initial process of selecting the transformed cells. Expression of genes cr1A.105 and cry2Ab2 is regulated by promoters e35S and FMV, respectively. The coding sequence of gene cr1A.105 produces protein Cry1A.105 that features insecticide action on corn farming pest lepidopterans. Protein Cry1A.105 is a modified Cry1A protein derived from Bacillus thuringiensis, that is 90.0%, 93.6% and 76.7% equivalent to proteins Cry1Ab, Cry1Ac and Cry1F, respectively. Gene cr2Ab2 coding sequence produces protein Cry2Ab2, a member of the Cry2Ab class of proteins with which has over 95% of the amino acid sequence in common(8,9). This is a variant of wild protein Cry2Ab2 isolated from Bacillus thuringiensis subspecies kurstaki. Bacillus thuringiensis, the donor organism of genes cr1A.105 and cry2Ab2, is a spore-forming gram-positive bacterium, naturally found in the soil. The bacterium produces proteins in the form of crystal or inclusion bodies that are selectively toxic for certain orders of pest insects. The technology has been used since 1958 to produce microbial formulations that are active as insecticides(10). This history or safe use shows that there is not harm associated to the use of Bacillus thuringiensis and to presence of Cry proteins in foodstuffs and rations, facts that have been corroborated by the lack of adverse effects for mammals in studies conducted with these products. The conclusion is supported by a revision on the history of safe use of Bacillus thuringiensis in agriculture(11). There are no known adverse effects to human beings that have been recorded over this long period of use of Bacillus thuringiensis microbial formulations(10). Betz et al(12) demonstrated the safety of several Cry proteins – expressed in genetically modified plants – for humans, animals and the environment. Gene nptII codifies enzyme neomycin phosphotransferase II (NPTII) that inactivates certain aminoglycosidic antibiotics such as kanamycin, neomycin and puromycin. The coding sequence of gene nptII derives from prokaryotic transposon Tn5(11). Enzime NPTII uses adenosine-triphosphate (ATP) to phosphorylate and inactivate aminoglycosidic antibiotics, which prevents the latter from injuring cells expressing NPTII when they are cultivated in a means that contain such selective agents. The only purpose of inserting gene nptII in MON 89034 corn was, therefore, selecting transformed cells containing genes cr1A.105 and cry2Ab2. Classic genetic improvement techniques were used to isolate plants that contained just the genes of interest cr1A.105 and cry2Ab2, and were devoid of gene nptII (T-DNA II), therefore producing plants free from the selection marker and containing just the characteristic of resistance to certain pest lepidopterans(14). Characterization of DNA inserted in MON 89034 corn took place through analyses of Southern blot, polymerase chain reaction (PCR) and DNA sequencing. Results show that MON 89034 corn contains a single functional copy of genes cr1A.105 and cry2Ab2 and that the complete insert contains: (1) The coding sequence of gene cr1A.105, whose transcription is controlled by the modified promoter e35S, the untranslated leading sequence Cab 5’ of the protein that bonds to wheat a/b chlorophyll, the introns of the rice actin gene (Ract1) and the termination transcription and polyadenylation sequence derived from the untranslated 3’ region of wheat (Hsp17) protein Hsp17.3 coding region; and (2) gene cry2Ab2 coding sequence whose transcription is controlled by figwort mosaic virus (FMV) promoter 35S, the first intron of protein Hsp70 gene (Hsp70), the DNA region containing the sequence of the transit peptide for the chloroplast of the smaller subunit of corn 1,5-biphosphate carboxylase ribulose and the first intron (SSU-CTP) and termination transcription and polyadenylation sequence derived from termination sequence 3’ of nopalyne synthase (nos 3’) of Agrobacterium tumefaciens. This T-DNA (T-DNA I) was inserted in the corn genome and resulted in the synthesis of Cry1A.105 and Cry2Ab2 proteins through expression of genes cr1A.105 and cry2Ab2. The transit peptide for chloroplast (CTP) is present do direct protein Cry2Ab2 to the corn plasmids. Analyses of PCR, sequencing of introduced and genomic DNA adjacent to the MON 89034 corn insert confirmed the organization of genetic elements within the genome. Results from sequencing amplified DNA fragments confirmed that the DNA sequence inserted in MON 89034 corn corresponds to the sequences that are present in plasmid PV-ZMIR245. However, promoter e35S that regulates gene cr1A.105 expression was modified by substitution of the right border present in plasmid PV-ZMIR245 by the left border sequence of MON 89034 corn. Protein Cry1A.105 consists of 1,177 amino acids with a molecular weight (MW) of 133 kDa, is a chimeric protein formed by domains I and II of proteins Cry1Ab or Cry1Ac1, a substantial portion of protein cry1F domain III and the C-terminal domain of protein Cry1aAc. The design strategy of protein Cry1A.105 used the change of domains to reach high levels of homology in several domains of protein Cry1A.105 with the respective domains in proteins Cry1Ab, Cry1Ac and Cry1F. Domains I and II of proteins Cry1A.105 are 100% identical to domains I and II of proteins Cry1Ab and Cry1Ac in amino acid sequences. Domain III of protein Cry1A.105 is 99% identical to domain III of protein Cry1F in amino acid sequence. The C-terminal portion is 100% homologous to the C-terminal portion of protein Cry1Ac. On average, sequence identity of protein Cry1A.105 with proteins Cry1Ac, Cry1Ab and CryF is 93.6%, 90.0% and 76.7%, respectively. According to the accepted phylogram for Cry proteins of Bacillus thuringiensis(8,9), protein Cry1A.105 may be grouped with proteins Cry1Ac and Cry1Ab due to their high degree of homology(15). Domain interchange is a well known mechanism that occurs in nature and increases the diversity of proteins Cry(16,17,18). The interchange, coupled with modern molecular biology tools, has been used to change functional domains of proteins Cry1 and develop commercial microbial biopesticides with greater specificity to pest lepidopterans. Microbial pesticides with the chimeric protein Cry1Ac/Cry1F have been used to control pest lepidopterans since 1997(19,20), and cotton expressing the chimeric protein containing domains of Cry1F, Cry1C and Cry1Ab also has been marketed(21). The general mechanism of Cry protein insecticide activity is well understood(22,23,24). The proteins encompass several functional domains possessing highly conserved regions among different classes. For instance, proteins Cry1A sequence of amino acids is highly conserved in domains I, II, and III. These functional domains determine the Cry proteins activity and specificity. Domain I is involved in inserting the membrane and formatting of pores. Domain II is involved in recognition and bonding to the specific receptor. Domain III keeps the structural integrity of the protein molecule(25) and contributes also to its specificity(16,26). C-terminal domain relates to crystal formation, which has no direct contribution to the protein activity(16). C-terminal domain is cut once within the insect guts or by certain in vitro proteases. Only insects possessing specific receptors are affected and there is no record of toxicity on other species that are devoid of such receptors(8,9). As in other proteins Cry1A, Cry1A.105 is active against important lepidopteran pests. The range of activities includes corn borers of genus Ostrinia (such as the European corn borer of 1 Cry1Ab and Cry1Ac share 100% of the amino acid sequence in domains I and II corn and the Asian corn borer) and Diatraea (corn stalk worm), fall armyworm (Spodoptera frugiperda sp.), cotton bollworm (Helicoverpa Zea) and black cutworm (Agrotis ipsilon). Protein cr1A.105 was purified from kernels of MON 89034 cotton and a recombinant lineage of Escherichia coli through fermentation. A panel of analytic tests was used to identify, characterize and compare protein cr1A.105 produced in the MON 89034 corn plant and the protein produced in Escherichia coli. Analysis of the purified and characterized cr1A.105 protein isolated in MON 89034 corn demonstrated its equivalence between the protein produced in the plant and the protein produced in Escherichia coli. Electrophoresis results in SDS-PAGE demonstrated that protein cr1A.105 produced in MON 89034 corn compared with protein produced in Escherichia coli indicate that both have equivalent molecular weight. The Western blot test showed that electrophoretic mobility and immunoreactivity of MON 89034 corn-produced Cry1A.105 protein are equivalent to that of Escherichia coli-produced protein. Mapping of the tryptic peptide by MALDI-TOF MS resulted in masses of peptides consistent with the expected tryptic peptides generated in silico based on the loci foreseen of trypsin breaking in cr1A.105 sequences. Besides, the two proteins were equivalent for functional activity and absence of glycosylation. Protein Cry2Ab2 produced in MON 89034 corn derives from Bacillus thuringiensis subspecies kurstaki and its amino acid sequence differs from that of the wild protein by a single amino acid. Protein Cry2Ab2 has 88% of identity in amino acid sequence with protein Cry2Aa that is present in commercial microbial products used to the control of pests. Proteins Cry2Ab2 produced in MON 89034 corn and in genetically modified cotton containing event MON 15985(27) share identical amino acid sequence. Protein Cry2Ab2 produced in MON 89034 corn is a variation of wild Cry2Ab2 of Bacillus thuringiensis. Its accumulation in MON 89034 corn is targeted to the chloroplast through the use of a transit peptide to the chloroplast (CTP) in the expression cassette. CTPs facilitate intracellular transport of proteins from the cytoplasm to plastids(28) and are typically eliminated from the mature protein once they are in the chloroplasts, where they are rapidly degraded. In order to enable accumulation of Cry2Ab2 in MON 89034 corn plastids, the DNA sequence that codes the CTP region of the smaller subunit of corn ribulose 1.5-biphosphate carboxylase was fused with the cry2Ab2 gene coding sequence. Protein Cry2Ab2 isolated from MON 89034 corn was purified, characterized, and the result was an equivalence between the plant produced protein and the protein produced in Escherichia coli. SDS-PAGE demonstrated that protein Cry2Ab2 produced in MON 89034 corn migrated in gel with protein produced in Escherichia coli, indicating that the proteins from the two sources have equivalent molecular weight. Western blot analysis showed that protein Cry2Ab2 electrophoretic mobility and immunoreactivity produced in MON 89034 corn are equivalent to that of the protein produced in Escherichia coli. The N-terminal of Cry2Ab2 protein in MON 89034 corn was blocked but mapping analysis by MALDI-TOF MS revealed masses of peptides consistent with tryptic peptides expected in loci foreseen for breaking by trypsin in Cry2Ab2 sequences, confirming the identity of the protein. Besides, the two proteins were equivalent in terms of functional activity and absence of glycosylation. The whole set of data supplied a detailed characterization of Cry2Ab2 protein isolated in MON 89034 corn and established its equivalence with the protein produced in Escherichia coli used in biosafety studies. IV. Aspects Related to Human and Animal Health A ninety day study with rats was conducted to assay potential adverse effects from MON 89034 corn to human and animal health(29). In the study, kernels of MON 89034 corn were fed to rats during ninety days. Results showed that there were no deaths or clinic observations related to the treatments, as well as changes in the parameters assayed: corporal weight; food consumption; hematology; serum chemistry; and urine tests. Besides, no changes in weight of organs were recorded that could have been attached to the administration of MON 89034 corn in the sample diet, nor macro or microscopic change associated to the treatment. Finally, the results enable the conclusion that the study with rats fed with MON 89034 corn kernels for ninety consecutive days failed to reveal adverse effects to growth and health of rats. This result corroborates the remaining conclusions on alimentary safety of MON 89034 corn and on proteins Cry1A.105 and Cry2Ab2 expressed in the plant. In addition, a forty-two day study was conducted to compare the nutritional value of MON 89034 corn kernels with the control conventional H1325023 and four commercial corn references when fed to fast-growing broiler chicken. Based on the study results, a conclusion was reached that the diet containing MON 89034 corn was as healthy as the control and commercial reference diet, considering the ability to promote fast growth in birds(30). A conclusion from the experiments was that weight measurements of the frozen carcass, fatty tissues, chest, thigh, drumsticks and wings were similar to the birds submitted to the different treatments. Similarly, there were no record of difference for humidity, proteins and fat rates in bird’s chest and drumsticks meat. Comparison were conducted between birds fed with the diet containing MON 89034 corn and birds fed on the control corn and the references failed to show differences regarding the parameters of performance, carcass and meat quality. Therefore, no differences were recorded in parameters measured in birds fed with MON 89034 when contrasted to birds fed with the control corn. One contributing factor to greater potential allergic oral sensitization to proteins is its stability for gastrointestinal digestion. Protein allergens tend to be stable to peptic and acid conditions of the digestive tract when they reach and pass through the intestinal mucosa to induce an allergic response(31,32,33,34). Rapidly digested proteins are highly correlated to significant decrease in the potential to cause allergic sensitization or reaction when consumed by humans. One aspect of this study includes analysis of protein in an essay with Simulated Gastric Fluid – SGF containing pepsin. The relation between digestibility in SGF and potential allergenicity was previously reported for a group of allergenic and non-allergenic proteins(31). The pepsin digestion essay was conducted to assess susceptibility of proteins Cry1A.105 and Cry2Ab2 to in vitro digestion in a fluid containing pepsin(35). Additionally to the SGF essay, an in vitro essay in Simulated Intestinal Fluid – SIF was also conducted to assay digestibility of alimentary components(36,37). In vitro susceptibility of Cry1A.105 and Cry2Ab2 proteins to pancreatin was assayed for SIF digestibility according to methods described in the literature(38). Protein Cry1A.105 digestibility was assayed by SDS-PAGE and Western blot. Digestion of protein Cry1A.105 was assayed by visual analysis in stained polycrylamide gel or by visual analysis in developed X-Ray films. Results of this study showed that protein Cry1A.105 was rapidly digested after incubation in SGF. Protein Cry1A.105 was digested below the 30 seconds LOD. Digestibility of Cry2Ab2 in SGF was assayed by SDS-PAGE and Western blot. Protein Cry2Ab2 digestion extension was assayed by visual analysis in stained polycrylamide gel or by visual analysis in developed X-Ray films. One gel or membrane was prepared in separate at the same time to determine the limit of detection (LOD) in each essay. Digestibility of Cry2Ab2 protein in SGF was assayed in SDS polycrylamide gel and the protein was rapidly digested. The results were consistent with reports from other Cry proteins that had its safety verified. The fact that Cry1A.105 protein was promptly digested in simulated gastric fluid makes its activity as an alimentary allergen unlikely. The same way, Cry2Ab2 is promptly digested in simulated gastric fluid and it also unlikely that it may act as an alimentary allergen. Adverse effects were no reported when mice received a total of 2,072 mg/kg of body weight of Cry1A.105 protein or 2,198 mg/kg of body weight of protein Cry2Ab2 in one day. Therefore, potential risks to health caused by acute ingestion in the diet of such proteins through consumption of MON 89034 corn was assayed by the exposure margin calculation based on no-observed effect level (NOEL) of the acute toxicity study with mice and estimates of the 95th percentile of acute exposure in their diet. Ingestion of Cry1A.105 and Cry2Ab2 in the diet of birds, piglings and fattening hogs was estimated using the daily consumption of cotton kernels and the highest levels of Cry1A.105 (7.0 μg/g of dry weight) Cry2Ab2 (2.1 μg/g of dry weight). A margin of exposure (MOE), defined as the ratio of NOEL with daily ingestion in the diet, was calculated for proteins Cry1A.105 and Cry2Ab2 for birds, piglings, young hogs, fattening hogs and dairy cattle. For birds and bovines, MOEs ranged from 1,930 to 13,500 and from 2,160 to 47,600 for proteins Cry1A.105 and Cry2Ab2, respectively. The high values of MOE indicate negligible risk to the health of birds and bovines exposed to rations containing MON 89034 corn in their diet. Ingestion of proteins Cry1A.105 and Cry2Ab2 in the diet of birds, piglings, and fattening hogs was estimated using a daily consumption of corn kernels and the highest levels of proteins Cry1A.105 (7.0 μg/g dry weight) and Cry2Ab2 (2.1 μg/g of dry weight). A margin of exposure (MOE), defined as the ratio of NOEL with daily ingestion in the diet, was calculated for proteins Cry1A.105 and Cry2Ab2 for birds, piglings, fattening hogs and daily cattle. For birds and bovines, MOEs were in the range from 1,930 to 13,500 and 2,160 to 47,600 for proteins Cry1A.105 and Cry2Ab2, respectively. The high values for MOE indicate negligible risk to the health of birds and bovines resulting from exposure to rations containing MON 89034 corn in their diet. Exogenous proteins produced in genetically modified cultures are not structural or functionally related to toxic or pharmacologically active proteins that may cause adverse effects on pregnant animals and their progeny. Besides, the likelihood that proteins expressed in genetically modified cultures resist to digestion in the gastrointestinal tract is minimal, as shown by in vitro studies performed as part of the alimentary safety assessment of such products (in this case, proteins Cry1A.105 and Cry2Ab2 of MON 89034 corn). Therefore, the likelihood that such exogenous proteins are absorbed intact, in amounts sufficient to gain access to the fetal circulation, is negligible. Normally, enzymes do not display evidence of producing toxic effects or being teratogenic to the reproductive system when supplied in food to rodents(39,40,41,42). Security studies conducted with a number of food enzymes produced by fermentation failed to record evidence that the proteins could trigger mutagenic or carcinogenic processes in laboratory animals(43). Some studies showed that food enzymes have no mutagenic nor teratogenic effects in animals and bacteria(44,45,46,47,48,49). Therefore, MON 89034 corn was assayed for its alimentary safety through available and internationally validated protocols, which, coupled with assaying guides for genetically modified cultures produced and/or updated by internationally renowned organizations will keep being used when necessary to secure that biotechnology derived food may be safely consumed(50). V. Environmental Aspects Corn is a monoic, allogamic and annual plant with anemochoric pollination, whereby distances that may be covered by pollen depend on wind patterns, humidity and temperature. Corn pollen disperses freely in areas located near the culture, and is able to reach stily-stigmas of the same or different genotypes and, under adequate conditions, starts germinating to originate the pollinic tube promoting ovule fecundation within an average period of 24 hours. Studies conducted on pollen dispersion demonstrated that pollen may travel long distances, though the major part of it is deposited close to the corn field, with a very low translocation rate, where over 95% of pollen may reach distances within sixty meters from its source. Luna et al.(51) examined the isolation and control distance for pollen and demonstrated that crossed pollination takes place within 200 meters, though no crossed pollination was recorded, under conditions of non-detasseling, for distances no lower than 300 meters from pollen sources. Results indicate that pollen viability is maintained for two hours and that crossed pollination was not recorded at a distance of 300 meters from the pollen source. By comparing concentrations at one meter from the source under low-to-moderate wind, one estimated that about 2% of the pollen are recorded at sixty meters, 1.1% at 200 meters, and 0.75-0.5% at 500 meters from the source. At a distance of ten meters from the source, on average, pollen grains by unit of soil is tenfold lower the pollen recorded at one meter from the border. Therefore, if separation distances established for corn seeds are observed, one expects that pollen transfer to adjacent varieties be minimal, being unlikely the presence of glyphosate-resistant genetic materials. Tesinte (Zea mays subspecies mexicana) and corn are species pollinated by wind, mutually compatible, highly variable and infertile(52,53). Both are genetically compatible and, in some areas of Mexico and Guatemala, cross freely when close to one another or under favorable conditions. Though corn can easily cross with teosinte, the species is not present in Brazil. Natural distribution of teosinte is limited to seasonally dry and sub-tropical zones with summer rains in Mexico and Guatemala and to the Mexican Central Plateau(53,54). With the introduction of genes cr1A.105 and cry2Ab2 one does not expect that the characteristics granted may give any competitive advantage, or greater aggressiveness to MON 89034 corn that would result in an invasive plant. The characteristics of resistance to some lepidopteran pest do not make MON 89034 corn a plant pest or a natural habitat invading plant, since the corn reproductive and development characteristics were not changed. Thus, the only advantage of MON 89034 corn is its resistance to damages caused by some insects of the Lepidoptera Order. The insect-resistant characteristics could even grant an adaptive advantage in the environment. However, this would only happen in a system where insects were agents limiting propagation of the plant, that is to say, if there was a strong pressure for selection by pests(55,56,57). This is not the case for MON 89034 corn, where genes cr1A.105 and cry2Ab2 grant protection only against some species of lepidopteran pests. A number of other insect species could cause impact in the survival of the plant in natural environments and Cry proteins produced in MON 89034 corn do not grant the plant any advantage regarding such non-target pests(56). Insecticide proteins Cry are extremely selective for insects of the Lepidoptera Order(58, 59, 60, 61, 62), with no poisonous effects to insects held as beneficial and non-target insects, among which predators, parasitoids, pollinating and other insects(63,64,65,66). An assay for both, target and non-target insects was conducted in the entomofauna during the 2007/2008 crop in four Monsanto of Brazil Experimental Stations (Cachoeira Dourada, State of Minas Gerais; Sorriso, State of Mato Grosso; Não-Me-Toques, State of Rio Grande do Sul; Rolândia, State of Paraná) located in areas of representative corn culture(67). The results showed that the insect species or families collected and identified in 235 comparisons failed to display a behavioral trend, with no records of increased or diminished insect visitation between plots with MON 89034 corn, control corn, or commercial references corn. Insects found represent species and/or families common to corn culture in different areas where the experiment was conducted. Similarity in visitation recorded in plots with MON 89034, control and commercial reference corn indicate that the introduction of the lepidopteran-resistant characteristics fails to interfere with insect visitation in the culture of corn in Brazil regarding the insects studied. The impact that may be caused, in general, by Cry proteins on non-target insects and soil organisms has been widely studied as part as an assessment of environmental safety of cultures with different events containing proteins Cry. Studies show that the tested terrestrial and soil non-target organisms were not affected by protein Cry1Ab, even though the level of the protein was above the maximum levels that may be verified in case of natural exposure(61,68,69). Additionally, a comparison of Cry proteins produced by Bacillus thuringiensis and the Cry1Ab protein produced by MON 89034 corn demonstrated that they may persist in tropical soils for a longer time due to its bonds to clay particles; however, effects on the soil microbiota were not recorded(70). Papers published in the scientific literature report that presence of Cry proteins do not affect in a significant way the microbiota and animals living in the soil(71,72). Additionally, Cry proteins of three subspecies of Bacillus thuringiensis failed to display microbiocide activity against a variety of bacteria, fungi and algae(73). Based on the experience with domesticated plant, the corn potential to be an invasive species to natural habitats, or to be persistent in a farm environment without human intervention is negligible. Corn plant is known to be a weak competitor, that when is outside cultivation areas has no significant impact in the environment. In assaying phenotypic, agronomic characteristics and ecologic interactions of MON 89034 corn, data were collected under five different categories: (1) germination, dormancy and emergence; (2) vegetative phase; (3) reproductive phase (including pollen characteristics); (4) retention of seeds in the plant; and (5) interactions of the plant with insects, diseases and abiotic stresses. Phenotypic, agronomic and ecologic interactions assays were based on combination of laboratory experiments and field studies conducted by experts in corn production and assay. Additionally, several commercial references were also used to provide a range3 of values common to corn commercial hybrids for each phenotypic, agronomic and ecologic interaction characteristic assayed. Completed the experiments, a conclusion was reached that MON 89034 corn is equivalent to conventional corn regarding its propagation and reproduction structures dispersion ability beyond cultivation areas and mechanisms for dispersion in the air, including that pollen viability of MON 89034 corn is equivalent to that of conventional corn. VI. Restrictions to the Use of the GMO and its Derivatives Studies submitted by applicant demonstrated that there was no significant difference between corn hybrids derived from non-modified lineages and MON 89034 corn regarding agronomic characteristics, reproduction, dissemination and survival ability. All evidence submitted in the proceedings and bibliographic references ratify that the risk level of transgenic variety is equivalent to non-transgenic varieties before soil microbiota, as well as that of other plants and to human and animal health. Thus, farming and consumption of MON 89034 corn are not potentially causes of significant environment degradation and fail to pose any risk to human and animal health. For these reasons, there are no restrictions to the use of MON 89034 corn and its derivatives, except in places mentioned by Law nº 11460, of March 21, 2007. Gene flow to local varieties (so-called creole corns) of open pollination is possible and poses the same risk caused by commercial genotypes available in the market (80% of conventional corn planted in Brazil comes from commercial seeds that underwent genetic improvement). Coexistence between conventional corn (either improved or creole) and transgenic corn cultivars is possible from the agronomic viewpoint(41,42) and shall comply with the provisions of CTNBio Ruling Resolution nº 4. After the years of use in different countries, there is no record of problems for human and animal health that could be attributed to transgenic corns. It shall be stressed that the lack of negative effects from cultivation of transgenic corn plants do not entail that such effects are free from occurring. Zero risk and absolute safety do not exist in a biological world, although there is a mass of reliable scientific information and a safe history of ten years of use that enable us to assert that MON 89034 corn is as safe as conventional corn versions. Therefore, applicant shall conduct post commercial-release monitoring under CTNBio Ruling Resolution nº 3. VII. Consideration on the Particulars of Different Regions of the Country (Information to supervisory agencies) As established by Article 1 of Law nº 11,460, of March 21, 2007 “research and cultivation of genetically modified organisms may not be conducted in indigenous lands and areas of conservation units.” VIII. Conclusion Considering that MON 89034 corn (Zea mays) variety belongs to a well characterized species with a solid safety record for human consumption and that cr1A.105 and cry2Ab2 genes introduced in this variety codify proteins that are ubiquitous in nature and are present in plants, fungi and microorganisms that are part of the alimentary diet of humans and animals; Considering that the insertion of the genotype took place though classical genetic improvement, resulting in insertion of one stable and functional copy of genes cr1A.105 and cry2Ab2 that granted resistance to insects; Considering that data on centesimal composition fail to show significant differences between genetically modified varieties and conventional varieties, suggesting nutritional equivalence between them; Considering that CTNBio granted approval do different corns containing event with protein Cry and that even Whereas: 1. studies showed that, as well as other Cry proteins, Cry1A.105 and Cry2Ab2 proteins are not potential causes of adverse effects at the exposure levels in fields on representative terrestrial beneficial invertebrate species, among them bees (larvae and adults); 2. expression of Cry1A.105 and Cry2Ab2 proteins fails to change the morphology and viability of MON 89034 corn pollen when compared to the pollen of conventional corn; 3. Cry1A.105 and Cry2Ab2 proteins do not share similarities with known allergen amino acid sequences, gliadins, gluteins and toxic proteins that have adverse effects on mammals; 4. laboratory studies with indicator species showed that proteins Cry1A.105 and Cry2Ab2 fail to cause adverse effects on tested non-target organisms; 5. molecular comparative analysis of MON 89034 corn ratified insertion of a single functional copy of genes cr1A.105 and cr1A.105 expression cassettes in a single locus of the corn genome; 6. comparative biochemical studies indicate that Cry1A.105 and Cry2Ab2 proteins have an important difference in their mode of action, namely in the form in which they bond to receptors in lepidopteran insects midgut and therefore the likelihood of crossed resistance between the two proteins is low; 7. the two proteins belong to the Cry family of proteins, derived from Bacillus thuringiensis, an organism that has been commercially used for over forty years in producing microbial insect controlling formulations; 8. the history of safe use and data from a number of studies support the conclusions on safety of MON 89034 corn and proteins Cry1A.105 and Cry2Ab2; 9. agronomic and efficacy assays of MON 89034 corn indicate that the event failed to express any other characteristics besides the expected ones; 10. phenotypic, agronomic and ecologic interaction assays indicate that MON 89034 corn is comparable to conventional corn and carries no higher risk to change into an invading plant. Therefore, considering internationally accepted criteria in the process of analyzing risks in genetically modified raw-material it is possible to conclude that MON 89034 corn is as safe as its conventional equivalent. CTNBio considers the activity free from being a potential cause of significant degradation to the environment, or harm to human and animal health. Restrictions to the use of this GMO and its derivatives are conditioned to the provisions of Law nº 11460, of March 21, 2007, CTNBio Ruling Resolution nº 03, and CTNBio Ruling Resolution nº 04. CTNBio analysis took into consideration opinions of the Commission members; ad hoc consultants; documents delivered to CTNBio Executive Secretary; results of planned releases into the environment; and lectures, texts and debates of the public hearing held on 03.20.2007. Also considered and consulted were applicant’s independent studies and scientific literature conducted by third parties. According to Annex I to Ruling Resolution nº 5, of March 12, 2009, the applicant shall have a term of thirty (30) days from publication of this Technical Opinion to adjust its proposal to the post-commercial release monitoring plan. VIII. Bibliography 1. BAHIA FILHO, A. F. C.; GARCIA, J. C. 2000. Análise de avaliação do mercado brasileiro de sementes de milho In: UDRY C. V.; DUARTE, W. F. (org) Uma história brasileira do milho: o valor de recursos genéticos. Brasilia: Paralelo 15,167-172. 2. FOOD AND AGRICULTURE ORGANIZATION OF THE UNITED NATIONS - FAO. 2007. FAOSTAT. Disponível em http://faostat.fao.org/site/340/default.aspx. 3. Companhia Nacional de Abastecimento – CONAB. 2007 Milho total (1a e 2a safra) Brasil – Série histórica de área plantada: safra 1976-77 a 2006-07. http://www.conab.gov.br/conabweb/download/safra/milhototalseriehist.xls. 4. CRUZ, I.; FIGUEIREDO, M. L. C.; OLIVEIRA, A. C.; VASCONCELOS, C. A. 1999. Damage of Spodoptera frugiperda (Smith) in different maize genotypes cultivated in soil under three levels of aluminium saturation. International Journal of Pest Management 45:293-296. 5. WAQUIL, J. M.; VILLELA, F. M. F.; FOSTER, J. E. 2002. Resistência do milho (Zea mays L.) transgênico (Bt) à lagarta-do-cartucho, Spodoptera frugiperda (Smith) (lepidoptera: Noctuidae). Revista Brasileira de Milho e Sorgo 1 (3): 1-11. 6. ALVES FILHO, J. P. 2001. Agrotóxicos e Agenda 21: sinais e desafios da transição para uma agricultura sustentável. In: II SINTAG Anais. II Simpósio Internacional de Tecnologia de Aplicação de Agrotóxicos: Eficiência, Economia e Preservação da Saúde Humana e do Ambiente. Jundiaí, SP, 17/07/2001 a 20/07/2001. 7. Komari, T. Y.; Hiei Y.; Saito, N.; Murai, and T. Kumashiro. 1996. Vectors carrying two separate T-DNAs for cotrasformation of higher plants mediated by Agrobacterium tumefaciens and segregation of transformants free from selection markers. The Plant J. 10:165-174. 8. Crickmore, N.; D. R. Zeigler; J. Feitelson; E. Schnepf; J. van Rie; D. Lereclus, J. Baum; and D. H. Dean. 1998a. Revision of the nomenclature for the Bacillus thuringiensis pesticidal crystal proteins. Microbiol Mol Biol Rev 62:807-13. 9. Crickmore, N.; D. R. Zeigler; J. Feitelson; E. Schnepf; J. van Rie; D. Lereclus; J. Baum, and D. H. Daen. 1998b. Revision of the nomenclature for the bacillus thuringiensis pesticidal crystal proteins. Microbiology and molecular biology reviews 62:807-813. 10. U.S. EPA. 1998. Bacillus thuringiensis (B.t.) plant-pesticides and resistance management EPA 738-F-98-001. United States Environmental Protection Agency. 11. McClintock, J. T.; C.R. Schaffer; and R.D. Sjobald. 1995. A comparative review of the mammalian toxicity of Bacillus thuringiensis-based pesticides. Pest. Sci. 45:95-105. 12. Betz, F. S., B. G. Hammond, and R. L. Fuchs. 2000. Safety and advantages of Bacillus thuringiensis-protected plants to control insect pests. Reg. Toxicol. and Pharmacol. 32:156-173. 13. Beck, E.; G. Ludwig; E. A. Auerswald; B. Reiss, and H. Schaller. 1982. Nucleotide sequence and exact localization of the neomycin phosphotrasferase gene from trasposon tn5. Gene 19:327-36. 14. Monsanto do Brasil. 2008. Relatório Técnico Liberação Comercial milho MON 89034. 15. Crickmore, N., D. R. Zeigler; E. Schnepf; J. van Rie; D. Lereclus; J. Baum, A. Bravo; and D. H. Dean. 2004. Bacillus thuringiensis toxin nomenclature. http//www.biols.susx.ac.uk/home/neilcrickmore/bt/index.html. 16. De Maagd, R. A.; A. Bravo, and N. Crickmore. 2001. How Bacillus thuringiensis has evolved specific toxins to colonize the insect world. Trends Genet. 17:193-9. 17. De Maagd, R. A.; A. Bravo; C. Berry; N. Crickmore; and H. E. Schnepf. 2003b. Structure, diversity, and evolution of protein toxins from spore-forming entomopathogenic bacteria. Annu. Rev. Genet. 37:409-433. 18. Masson, L.; A. Mazza; S. Sangadala; M. J. Adang; and R. Brusseau. 2002. Polydispersity of Bacillus thuringiensis Cry1 toxins in solution and its effect on receptor binding kinetics. Bichim biophys Acta 1594:266-75. 19. Baum, J.A 1998. Transgenic Bacillus thuringiensis. Phytopotection 79:127-130. 20. Baum, J. A., T. B. Johnson, and B.C. Carlton. 1999. Bacillus thuringiensis. Natural and recombinant bioinsecticide products, p. Pp 189-209, In F. R. Hall and J. J. Menn, eds. Methods in Biotechnology. Pesticides: Use and Delivery, vol. 5. Humana Press, Inc., Totowa, New Jersey. 21. Gama, M. I. C. S. 1998. Identificação de plantas transgênicas por PCR. Manual de transformação genética de plantas. Ed. Brasileiro, A.C.M. and Carneiro, V.T.C. Brasília - EMBRAPA-SPI / EMBRAPA CENARGEN.pp.309. 22. Gill, S.S.; E. A. Cowles, and P. V. Pietrantonio. 1992. The mode of action of Bacillus thuringiensis endotoxins. Ann. Rev. entomol. 37:615-636. 23. Schnepfe, E.; N. Crickmore; J. van Rie; D. Lereclus; J. Baum; J. Feitelson; D. R. Zeigler; and D. H. Dean. 1998. Bacillus thuringiensis and its pesticidal crystal proteins. Microbial. Mol. Biol. Rev. 62:775-806. 24. Zuang, M.; and S.S. Gill. 2003. Mode of action of Bacillus thuringiensis toxins., p. Pp 213-236, In G. Voss and G. Ramos, eds. Chemistry of crop protection, progress and prospects in Science and Regulation. Wiley-VCH, Weinheim, Germany. 25. Li, J.D.; J. Carroll; and D. J. Ellar. 1991. Crystal structure of insecticidal delta-endotoxin from Bacillus thuringiensis at 2.5 a resolution. Nature 353:815-21. 26. De Maagd, R. A. ; M. Weemen-Hendriks; W. Stiekema, and D. Bosch. 2000. Bacillus thuringiensis deltaendotoxin Cry1c domain III can function as a specificity determinant for Spodoptera exigua in different, but not all, Cry1-cry1c hybrids. Appl Environ Microbiol 66:1559-63. 27. Comissão Técnica Nacional de Biossegurança. 2009. Parecer Técnico 1.832/2009. D.O.U 22/05/2009, Seção 01 pág.10. 28. Bruce, B. D. 2000. Chloroplast transit peptide: structure, function and evolution. Trends cell biol. 10:440-447. 29. Kirkpatrick, J. B. 2007. A 90-day feeding study in rats with MON 89034. Monsanto Technical Report MSL0020649. 30. Taylor, M.; G. Hartnell; M. Nemeth; D. Lucas, and S. Davis. 2007. Comparison of broiler performance when fed diets containing grain from second-generation insect-protected and glyphosate-tolerant, conventional control or commercial reference corn. Poultry Science 86:1972-1979. 31. Astwood, J.; J. J. Leach; and R. L. Fuchs. 1996. Stability of food allergens to digestion in vitro. Nature Biotechnology 14:1269-1273. 32. Astwood, J.D.; and R. L. Fuchs. 1996a. Allergenicity of foods derived from transgenic plants. Monogr Allergy 32:105-20. 33. Fuchs, R. L.; and J. D. Astwood. 1996. Allergenicity assessment of foods derived from genetically modified plants. Food technology 50:83-88. 34. Metcalfe, D. J.; Astwood T. R.; S. H.; T.M. L.; and F. R. 1996. Assessment of the allergenic potential of foods derived from genetically engineered crop plants. Critical Reviews in Food Science and Nutrition 36:165-186. 35. Thomas, K.; M. Aalbers; G. A. Bannon; M. Bartels; R.J. Dearman; D. J. Esdaile; T.J. Fu; C. M. Glatt; N. Hadfield; C. Hatzos; S. L. Hefle; J.R. Heylings; R. E. Goodman; B. Hhenry; c. Herouet; M. Holsapple; G. S. Ladics; T. D. Landry; S. C. Macintosh; E. A. Rice; L. S. Privalle; H. Y. Steiner; R. Teshima; R. van Ree; M. Woolhiser; and J. Zawodny. 2004. A multi-laboratory evaluation of common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Regul.t Toxicol. Pharmacol.39:87-98. 36. Okunuki, H.; Techima, R.; Shigeta, T.; Sakushima; J.; Akiyama, H.; Yukihiro, G.; Toyoda, M.; and Sawada, J. J. 2002. Increased digestibility of two products in genetically modified food (CP4-EPSPS and Cry1ab) after preheating. Food Hyg. Soc. Japan 43:68-73. 37. Yagami, T.; Hashima Y.; Nakamura, A.; Hiroyuki, O.; and Ikesawa, Z. 2000. Digestibility of allergens extracted from natural rubber latex and vegetable foods. J. Allergy Clin. Immunol.106:52-762. 38. Pharmacopeia, U.S. 1995. The National Formulary Mark Printing Co., Easton, PA. (ed) 2000. Proceedings of the 6th International feed production conference, Piacenza, Italy. 39. Ashby, R.; R. K. Hjortkjaer; M. Stavnsbjerg; H .Gurtler; P. B. Pedersen; J. Bootman; G. Hodson-Walker; J. M. Tesh; C.R. Willoughby; H. West; and J.P. Finn. 1987. Safety evaluation of Streptomyces murinus glucose isomerase. Toxicol. Lett. 36:23-35. 40. Flood, M.T.; and M. Kondo. 2004. Toxicity evaluation of a ƒÒ-galactosidase preparation produced by Penicillium multicolor. Regul. Toxicol. Pharmacol. 40:281. 41. Greenough, R. J.; and D. J. Everett. 1991. Safety evaluation of alkaline cellulose. Food Chem. Toxicol. 29:781. 42. Hjortkjaer, R.K. 1993. Safety evaluation of esperase. Food Chem. Toxicol. 31:999. 43. Pariza, M. W.; and E. M. Foster. 1983. Determining the safety of enzymes used in food processing. J. Food Protection 46:453-468. 44. Bergmam, A.; and A. Broadmeadow. 1997. An overview of the safety evaluation of the Thermomyces lanuginosus xylanase enzyme (SP 628) and the Aspergillus aculeatus xylanase enzyme (SP 578). Food additives and contaminants 14:389-398. 45. Dean, S. 1997. Industrial genotoxicology group (IGG): The use of historical data in data interpretation and genotoxicity testing of biotechnology products, Royal Society of Medicine, London, UK, December 1995. Mutagenesis 12:49-50. 46. Kondo, M.; T. Ogawa; Y. Matsubara; A. Mizutani; S. Murata and M. Kitagawa. 1994. Safety evaluation of lipase G from Penicillium camembertii. Fd. Chem. Toxic. 32:685-696. 47. Mackenzie, K. M.; S. R. W. Petsel; R. H. Weltman; and N. M. Zeman. 1989a. Subchronic toxicity studies in dogs and in utero rats fed diets containing Bacillus stearothermophilus alpha-amylase from a natural or recombinat DNA host. Fd. Chem. Toxic. 27:599-606. 48. Mackenzie, K. M.; S. R. W. Petsel; R. H. Weltman; and N.W. Zeman. 1989b. Subchronic toxicity studies in dogs and in utero – exposed rats fed diets containing Bacillus megaterium amylase derived from a recombinant DNA organism. Fd. Chem. Toxic. 27:301-305. 49. Stavnsbjeg, M.; R. K. Hjorkjaer; V. Bille-Hansen; B. F. Jensen; R.J. Greenough; M. McConville; M. Holmstroem, and K. P. Hazelden. 1986. Toxicologic safety evaluation of a Bacillus acidopullulyticus pullulanase. J. Food Protect. 49. 50. Hammond, B. and A. Cockburn. 2008. The safety assessment of proteins introduced into crops developed through agricultural biotechnology: a consolidated approach to meet current and future needs. In: Hammond, B. (2008) Food Safety of Proteins in Agricultural Biotechnology, CRC Press, Taylor and Francis Group, LLC.:259-288. 51. LUNA, S. V.; FIGUEROA, J. M.; BALTAZAR, M. B.; GOMEZ, L. R.; TOWNSEND, R.; and SCHOPER, J. B. 2001. Maize pollen longevity and distance isolation requirements for effective pollen control. Crop Sci. 41:1551-1557. 52. Wilkes, G. 1989. Maize: domestication, racial evolution, and spread. Foraging and farming - the evolution of plant exploration: 440-455. 53. Wilkes, H.G. 1972. Maize and its wild relatives. Science 177:1071-1077. 54. Gonzalez, J.; and J. Corral. 1997. Teosinte distribution in Mexico. Proceedings of a forum: gene flow among maize landraces, improved maize, varieties and teosinte: implications for transgenic maize:18-39. 55. Borém, A . 2001. Escape gênico & transgênicos. Viçosa, UFV:206 p. 56. Glover, J. 2002. Gene flow study: implications for GM crop release in Australia. Bureau of rural Sciences, Canberra, Australia http://www.affa.gov.au/brs : 71p. 57. Nilsen, K. M.; J. D. van Elsas; and K. Smalla. 2000b. Safety issues in antibiotic resistance marker genes in transgenic crops. Proc. of the 6th International Feed production Conference:146-162. 58. MENDELSOHN, M.; KOUGH, J.; VAITUZIS, Z.; MATTEWS, K. Are Bt crops safe? Nature Biotechnology, v.21, n. 9, p. 1003-1009, 2003. 59. DULMAGE, H. T. Microbial control of pests and plant diseases 1970 – 1980. In: BURGES, H. D. (ed). London: Academic Press, 1981. p. 1993-222. 60. KLAUSNER, A. Microbial insect control. Bio/technology, v.2, p. 408-419, 1984. 61. ARONSON, A. I. BACKMAN, W.; DUNN, P. Bacillus thuringiensis and related insect pathogens. Microbiol. rev., v. 50, p. 1-24,1986. 62. MACINTOSH, S. C.; STONE, T. B.; SIMS, S. R.; HUNST, P.; GREENPLATE, J. T.; MARRONE, P. G.; PERLAK, F. J.; FISCHHOFF, D.A.; FUCHS, R. L. Specificity and efficacy of purified Bacillus thuringiensis proteins against agronomically important insects. J.Insect Path., v. 56, p. 258-266, 1990. 63. WHITELEY, H. R.; SCHNEPF, H. E. The molecular biology of parasporal crystal body formation in Bacillus thuringiensis. Ann. Rev. Microbiol., v.40, p. 549-576, 1986. 64. CANTWELL, G. E.; LEHNERT, T.; FOWLER, J. Are biological insecticides harmful to the honey bee. Am. Bee J., v. 112, p. 294-296, 1972. 65. KRING, A.; LANGENBRUCH, G. A. Susceptibility of arthropod species to Bacillus thuringiensis. In: Microbial Control of Pests and plant Diseases. BURGES, H. D. (Ed). London: Academic Press, 1981. p. 837-896. 66. FLEXNER, J. L.; LIGHTHART, B.; CROFT, B. A. The effects of microbial pesticides on non-target beneficial arthropods. Agric. Ecosys. Environ., v. 16, p. 203-254,1986. 67. Oliveira, W. 2008a. Agronomic and phenotypic evaluation of corn MON 89034 in Brazil field trials during 2007/2008 season. Monsanto Technical Report MSL-013. 68. FERNANDES, O. D. Efeito do milho geneticamente modificado (MON 810) em Spodoptera frugiperda (J. E. Smith,1797) e no parasitóide de ovos Trichogramma spp. 164 f. Tese (Doutorado em Entomologia), Departamento Entomologia, ESALQ, Universidade de São Paulo, Piracicaba, 2003. 69. SIMS, S. R. Bacillus thuringiensis var. kurstaki (Cry1Ac) protein expressed in transgenic cotton: effects on beneficial and other non-target insects. Southwestern Entomol., v. 20, p. 493-500, 1995. 70. SANDERS, P. R.; LEE, T. C.; GROTH, M. E.; ASTWOOD, J. D.; FUCHS, R. L. Safety assessment of insect-protected corn. In: THOMAS, J. A. Biotechnology and Safety Assessment. 2 ed. Taylor and Francis, 1998. p. 241-256. 71. MUCHAONYERWA, P.; WALADDE, S.; NYAMUGAFATAR, P.; MPEPEREKI, S.; and RISTORI, G. G. Persistence and impact on microorganisms of Bacillus thuringiensis proteins in some Zimbabwean soils. Plant and soil, v. 266, p. 41-46, 2004. 72. STOTZKY,G. Clays and humic acids affect the persistence and biological activity of insecticidal proteins from Bacillus thuringiensis in soil. In: Developments in Soil Science 28B (Soil Mineral - Organic Matter Microorganism Interactions and Ecosystem Health), p: 1-16, 2002. 73. STOTZKY, G. Persistence and biological activity in soil of the insecticidal proteins from Bacillus thuringiensis, especially from transgenic plants. Plant and Soil, v. 266, p. 77-89, 2004.

molecular traditional methods

Genetically modified MON 89034 corn was developed using recombinant DNA techniques to introduce two Bacillus thuringiensis (Bt) derived novel genes: the cry1A.105 sequences encoding Cry1A.105, a synthetic chimeric protein; and the cry2Ab2 gene encoding the Cry2Ab2 protein. The Cry1A.105 protein is a chimeric protein comprised of various domains from Cry1Ac, Cry1Ab, and Cry1F. The Cry2Ab2 protein as expressed in MON 89034 corn differs by a single amino acid from the wild type protein equivalent. All cry sequences are originally derived from Bt subsp. kurstaki with the exception of domain III sequences for cry1F, which are originally derived from Bt subsp. aizawai

The safety assessment performed by Food Directorate evaluators was conducted according to Health Canada's Guidelines for the Safety Assessment of Novel Foods. The assessment considered: how corn event MON 89034 was developed; how the composition and nutritional quality of corn grain derived from plants containing this event compare to non-modified corn; and what the potential is for food products derived from plants containing this event to be toxic or cause allergic reactions.

The Food Directorate has a legislated responsibility for pre-market assessment of novel foods and novel food ingredients as detailed in Division 28 of Part B of the Food and Drug Regulations (Novel Foods). Foods derived from corn lines containing event MON 89034 are considered novel foods under the following part of the definition of novel foods: "c) a food that is derived from a plant, animal or microorganism that has been genetically modified such that

i.the plant, animal or microorganism exhibits characteristics that were not previously observed in that plant, animal or microorganism".

Please see decision document weblinks

Based on the risk assessment, it can be concluded that the event shows the same risks as its conventional counterpart. Therefore the National Technical Biosafety Committee for GMO use exclusively in Health and human consumption (CTNSalud) recommends its authorization.

Based on the risk assessment, it can be concluded that the event shows the same risks as its conventional counterpart. Therefore, the National Technical Committee for GMO use exclusively in health and human consumption (CTNSalud) recommends its authorization.

Bayer West-Central Africa S.A. has applied requesting for authorisation of genetically modified maize (Zea mays) event MON 89034 with the OECD unique identifier MON-89Ø34-3 for direct use as food, feed or for processing in Ghana.

 

The Maize Event MON89034 expresses the genes Cry1A.105 and Cry2Ab2 which encodes Cry1A.105 and Cry2Ab2 proteins that confer protection against certain lepidopteran pests such as European corn borer, fall armyworm, black cutworm, and the corn earworm. This Maize Event has been reviewed and approved for diverse uses (e.g., food, feed or for processing and/or cultivation) in several countries. 

The Board of the NBA considered the recommendations from the Technical Advisory Committee (TAC) following the Committee's thorough evaluation of the application submitted by the applicant using information available on: i. the Biosafbty Clearing House (BCH), which is a mechanism set up by the Carlagena Protocol on Biosafety to facilitate the exchange of infbrmation on Living Modified Organisms (LMOs) and assist the Parties to better comply with their obligations under the Protocol and to which Ghana is a Party, ii. the Organisation for Economic Co-operation and Development (OECD) Biotrack Product Database, iii. the Food and Agriculture Organisation of the United Nations (FAO) genetically modified foods platform. The following considerations were evaluated: ./ development of the modified Maize Event GA2l, including the molecular biology data that characterizes the genetic change; ,/ proximate analyses; major constituents (fats, proteins, carbohydrates) and minor constituents (minerals and vitamins); ,/ composition of, and nutritional information (including anti-nutrients) on the GM maize compared to its conventional counterpart; '/ the potential for causing allergic reactions; ,/ microbiological and chemical safety of the event; '/ the potential for production of new toxins in the event; and, ,/ the potential for any unintended or secondary effects;

Please refer to the uploaded document.

Competent National Authority: Ministry of Agriculture-Jehad, Agricultural Research, Education and Extension Organization (AREEO). Risk Assessment file is uploaded. https://bch.cbd.int/en/database/RA/BCH-RA-IR-114186/2

Please refer to the links below.

Please refer to the uploaded document.

Authorization by COFEPRIS: 58

The genetically modified maize MON-89Ø34-3, as described in the application, expresses the Cry1A.105 and Cry2Ab2 proteins which provide protection to certain lepidopteran pests.

UI OECD: MON-89Ø34-3 During the risk assessment of this GMO based on existing knowledge to date, no toxic or allergic effects neither substantial nutritional changes are observed. The event is as safe as its conventional counterpart. For more detail please find attached the risk assessment summary in this page.

FSANZ has completed a comprehensive safety assessment of food derived from insect protected corn line MON 89034, as required under Standard 1.5.2. The assessment included consideration of (i) the genetic modification to the plant; (ii) the potential toxicity and allergenicity of the novel proteins; and (iii) the composition of MON 89034 corn compared with that of conventional corn varieties. No public health and safety concerns were identified as a result of the safety assessment. On the basis of the available evidence, including detailed studies provided by the Applicant, food derived from insect-protected corn line MON 89034 is considered as safe and wholesome as food derived from other commercial corn varieties.

The food and feed safety assessment was performed following the CODEX Guidelines. The Commercial Release Opinion of the National Commission for Agricultural and Forestry Biosafety (CONBIO), in its substantial part states: "...Recommends technically: (1) The commercial release of the event MON89034 (2) In case of detection of an unexpected effect, the company is obliged to inform CONBIO".

Monsanto has developed a biotechnology derived product corn MON 89034 through Agrobacterium mediated transformation to express the Bacillus thuringiensis insecticidal proteins Cry1A.105 and Cry2Ab2 using the plasmid vector PV-ZMIR245, which is a binary vector containing two separate transfer DNA’s (2T-DNA). The first T-DNA, designated as T-DNA I, contains the cry1A.105 and the cry2Ab2 expression cassettes. The second T-DNA designated as T-DNA II contains the nptII (neomycin phosphotransferase II) expression cassette, as a selectable marker. Traditional breeding was used to isolate those plants only contained the cry1A.105 and cry2Ab2 expression cassettes (T-DNA I) and did not contain the nptII expression cassette (T DNA II), thereby, producing marker-free corn MON 89034. The introduction of the second generation product MON 89034 is expected to provide enhanced benefits for the control of lepidopteran insects pests such as Ostrinia furnacalis (ACB) and Spodoptera frugiperda (FAW) and Helicoverpa zea (CEW) compared to existing products.

Monsanto Philippines, has filed an application with attached technical dossiers to the Bureau of Plant Industry (BPI) for a biosafety permit for direct use as food, feed and for processing under Administrative Order (AO) No. 8 Part 5 for Corn MON 89034, a second generation product, which has been genetically modified for insect resistance. Corn MON 89034 has been evaluated according to BPI’s safety assessment by concerned agencies of the Department of Agriculture, such as [Bureau of Animal Industry (BAI), Bureau of Agriculture, Fisheries and Product Standards (BAFPS), and a Scientific and Technical Review Panel (STRP) members]. The process involves an intensive analysis of the nature of the genetic modification together with the consideration of safety assessment paradigm which includes molecular characterization, protein characterization, and food/feed composition. The petitioner/applicant published the said application in two widely circulated newspapers for public comment/review. During the 30-day comment period, BPI had not received comments on the said application. The STRP and agencies’ assessment and review of results of evaluation by the BPI Biotech Core Team completed the approval process.

Toxicological Assessment For the digestibility study using simulated gastric fluid (SGF) that contained the enzyme pepsin, the Cry1A.105 was digested within 30 seconds. There were no proteolytic fragments observed in the SDSPAGE gel, except for a very faint band of ~4.5 kDa band visible in the first 20 min of digestion but was not visible after 30 min of digestion. This band is unlikely to pose a health risk because of its small size. Western Blot analysis also demonstrated that the Cry 1A.105 was digested below the limit of detection (LOD) of 1 ng within 30 seconds in SGF (see Figure VI.16 of the reference document FDA BNF 00105). On the other hand, in simulated intestinal fluid (SIF) that contained pancreatin, the digestion of Cry1A.105 was assessed by Western blotting (with LOD of 0.1 ng). The full length protein of was digested below the LOD within five minutes. Fragments of 60, 32 and 30 kDa were visible up to 24 h of digestion (Figure VI.17 of the reference document FDA BNF 00105). The 60 kDa fragment was said to be representative of the tryptic core portion Cry1A.105. This is consistent with other Cry proteins with demonstrated safety. The estimated T50 result in SGF is <30 seconds and the estimated T50 in SIF is <5 minutes. In addition, the effect of heat treatment on the immunologically detectable levels of the Cry1A.105 protein in corn grain from MON 89034 was evaluated using the Western blot method and image analysis of blot films. The amount of immunodetectable Cry1A.105 protein present in buffer extracts of MON 89034 after heating was below the lower limit of detection, or had decreased considerably relative to their original values. These results clearly demonstrate that the heating of ground corn grain, in a manner similar to the conditions employed for commercial processing, results in the loss of immunodetectable Cry1A.105 protein. Bioinformatics analyses were performed to assess the potential for toxicity of the Cry1A.105 by amino acid sequence alignment to sequences in the TOXIN5 and ALLPEPTIDES databases. The FASTA algorithm was employed to identify structural and sequence similarities where proteins sharing a high degree of similarity are often homologous in function as well. From comparisons with the TOXIN5 database, the results showed significant sequence similarity to Bac. thuringiensis pesticidal crystal protein Cry1Ac (92% identity in 1,182 amino acid residues, E score=0). This was expected because Cry1A.105 has a significant portion similar to Cry1Ac. This protein and Cry1A.105 did not share any match with other proteins that are known as toxic to human beings and animals. From the ALLPEPTIDES database, there was again a 92.1% identity to Cry1A over 1,177 amino acid with E score =0. Other matches with significant E scores were to Cry homologues and the hypothetical amino acid sequence JMP 134 from Ralstonia eutropha. According to the reference document, there are no indications for any adverse biological activity of the Cry protein homologues or the hypothetical protein from the JMP 134 sequences to non-target species. Further, an acute oral toxicity assessment was conducted to evaluate potential adverse clinical signs or detrimental effects on mice exposed to E. coli-produced Cry1A.105 protein. Cry1A.105 protein was administered by oral gavage (as two doses about 4 hours apart) to 10 male and 10 female CD-1 mice at a total dose level of 2072 mg/kg body weight. There were no treatment-related effects on survival, clinical observations, body weight gain, food consumption or gross pathology. Therefore, the No Observable Adverse Effect Levels (NOAEL) for Cry1A.105 was considered to be 2072 mg/kg body weight, the highest dose tested. Lastly, E. coli-produced Cry1A.105 protein was used as the test protein. An acute oral toxicity study conducted with The E. coli-produced Cry1A.105 protein was shown to be equivalent to the plantproduced Cry1A.105 present in MON 89034. Meanwhile, in SGF with pepsin, the full length Cry2Ab2 (65 kDa) produced in E.coli was rapidly degraded within 30 seconds. At least 99.4 % and 99.0% of the original amount of protein was digested as shown in the SDS-PAGE gel and by Western Blotting, respectively. No other stable fragments were visible at any time point (0.5-60 min). Therefore, the T50 can be considered to be <30 seconds. While, In SIF with a mixture of pancreatin as enzyme, the full length Cry2Ab2 produced in E.coli was digested within 15 min to at least 97.5% of the original amount. Western Blot analysis showed bands of 60, 55, 50, 40, 12 and 10 kDa were observed. The 60 kDa band was not detectable after 1 h of incubation in SIF. The 55 kDa band was undetected at 24 h incubation time point. The 50 kDa band was still present after 24 h incubation in SIF. The 40 kDa band disappeared after 12 h of incubation in SIF. The 12 kDa band was undetectable after 1 h incubation in SIF. New bands of <50 kDa were detected beginning at 4 h incubation time point. These represented the fragments of Cry2Ab2 produced during incubation and were undetected at the 24 h incubation time point as shown in Figure 1 of the reference document Thorp and Goley. The estimated T50 for Cry2Ab2 in SIF is <15 minutes. Immunologically detectable Cry2Ab2 extracted in CAPS and NLS buffers from MON 89034 powdered grains that were obtained after heating at 204oC for 20 min, was measured to be below the lower limit of detection of the Western Blot analysis. The reduction in the original amount of protein was reported to be 77% and 70% in CAPS and NLS buffers, respectively. The T50 result cannot be accurately determined. However, the Cry2Ab2 was established to be inactivated by heating, as used in common commercial corn processing methods. Further, using the FASTA sequence alignment tool, a comparison of the Cry2Ab2 protein sequence was performed with the toxin (TOXIN5) and public domain (ALLPEPTIDES) database sequences. The highest similarity observed was to pesticidal crystal protein Cry2Ab, demonstrating 100% identity over 632 amino acids with an E-score of zero. All remaining alignments with significant E-scores were to Cry protein homologues derived from B. thuringiensis, Paenibacillus popilliae or Paenibacillus lentimorbus. Based on these data, the Cry2Ab2 protein does not share structural congruence with any proteins that may cause adverse effects in humans and animals. An acute oral toxicity assessment was also conducted to evaluate potential adverse clinical signs or detrimental effects on mice exposed to E. coli-produced Cry2Ab2 protein. Cry2Ab2 protein was administered by oral gavage (as two doses about 4 hours apart) to 10 male and 10 female CD-1 mice at a total dose level of 2198 mg/kg body weight. There were no treatment-related effects on survival, clinical observations, body weight gain, food consumption or gross pathology. The NOAEL for Cry2Ab2 was considered to be 2198 mg/kg body weight, the highest dose tested. The source for the Cry2Ab2 used in the acute oral toxicity study in mice was Cry2Ab2 produced in recombinant E.coli. The plantproduced and E.coli-produced Cry2Ab2 have been established to be equivalent in form and function through a battery of physico-chemical and biochemical tests (molecular weight analysis; N-terminal sequence analysis; MALDI-TOF analysis of tryptic peptides; lack of glycosylation; protein stability test) as well as performance in insect bioassays. K. Allergenicity Assessment Bioinformatics analyses were performed to assess the potential for allergenicity of the Cry1A.105 by amino acid sequence alignment to sequences in the allergen AD6 database. The FASTA algorithm was employed to identify sequence similarities and no relevant matches were found. Using the algorithm ALLERGENSEARCH for alignment of eight contiguous amino acid residues, again there was no matches found in the AD6 sequences. The Cry2Ab2 sequence was also compared to the allergen AD6 database sequences using the FASTA algorithm. There was no relevant similarity based on amino acid sequences with known allergens. Using an eight amino acid sliding window for the algorithm ALLERGENSEARCH, there were no immunologically relevant sequences when the Cry2Ab2 sequence was compared to the sequences available in the AD6 database. The analyses demonstrated that Cry1A.105 and Cry2AB2 have no amino acid sequence similarities to known allergens, gliadins and glutelins. The Cry1A.105 protein produced from the plant and that produced in E.coli migrated at 130 kDa in gels and are both non-glycosylated. The Cry1A.105 therefore is not within the 10-70 kDa molecular weight range. Meanwhile, molecular weight of the intact plant-produced Cry2Ab2 migrated in the same manner on the gel as the E.coli-produced Cry2Ab2 at 61.3 kDa. This size is well within the 10-70 kDa range. The Cry1A.105 present in MON 89034 grain was calculated to be 0.0047% of total protein whereas for Cry2Ab2, it was calculated to be 0.001% of total protein. L. Nutritional Data The over-all (combined sites) analyses of proximate amounts of ash, carbohydrates, moisture, protein and total fat from grains and forage of MON 89034 were comparable to grain and forage obtained from the non-transgenic isoline (control). There were significant differences in the amount of carbohydrate in MON 89034 grain as compared to the non-transgenic control at two sites, namely, Site IA and Site OH with values lower and higher than in the control, respectively. For forage, there were differences between those derived from MON89034 forage with those from the non-transgenic control in the amounts of moisture, ash and carbohydrates in only one site each. However, the said discrepancies were within the range of the respective parameters in the commercial reference varieties. Taken together, the proximate composition of grain and forage from MON 89034 were substantially the same as in the non-transgenic corn lines. As for key nutrient combined-site analyses, statistical differences between MON 89034 and control corn were observed for phosphorus in forage, and 18:0 stearic and 20:0 arachidic acids in grain. The differences observed are generally small (3.4 – 19.2%), considering the range of natural variability, and the mean levels and ranges of MON 89034 are well within the 99% tolerance intervals for commercial corn. The mean levels and ranges of phosphorus in forage, and 18:0 stearic and 20:0 arachidic acids in grain, were also within the ranges in the International Life Sciences Institute Crop Composition Database (ILSI-CCD), as well as within published literature ranges. Therefore, it is concluded that MON 89034 and control corn are compositionally equivalent based on analyses of the combined-site data. The data for anti-nutrients and secondary metabolites were obtained from the summary of combined sites analyses. The value for the anti-nutrient phytic acid was very slightly higher in the transgenic MON 89034 grain than in the non-transgenic control isoline. However, the difference was not statistically significant. The data for raffinose was not included because the values was found to below the limit of quantitation and were then excluded for further statistical analysis. Statistical difference between the amount of p-coumaric acid in MON 89034 grain with that from the non-transgenic isoline was identified in only one site (Site OH). But the value was within the range derived from the commercial reference varieties. Ferulic acid was present in comparable amounts in the transgenic and non-transgenic control corn lines. Therefore, the contents of phytic acid and secondary metabolites in grain form MON 89034 can be considered substantially equivalent to those in the nontransgenic isoline.

Please see the link below(in Korean).

Peer review of the data submitted by the applicant and the results of complex medical and biological studies of transgenic maize line MON89034 tolerant to lepidopteran pests, attest to the absence of any toxic, reprotoxic, genotoxic, or allergenic effects of this maize line. By biochemical composition, transgenic maize line MON89034 was identical to conventional maize. GM maize line MON89034 tolerant to lepidopteran pests has been registered for food use, listed in the State Register, and licensed for use in the territory of the Russian Federation, import into the territory of the Russian Federation, and placing on the market without restrictions.

The genetic modification in corn line MON 89034 (MON-89034-3) involves the introduction of the cry1A.105 and cry2Ab2 genes derived from B. thuringiensis subspecies kurstaki and aizawai. These genes encode the Cry1A.105 and Cry2Ab2 insecticidal proteins which are selectively toxic to a range of lepidopteran insect larvae. Molecular analyses indicate that one copy of each of the cry1A.105 and cry2Ab2 genes have been inserted at a single site in the plant genome and are stably inherited from one generation to the next. Both proteins Cry1A.105 and Cry2Ab2 are unlikely to be toxic or allergenic in humans. Food from MON 89034 corn is compositionally equivalent to food from conventional corn varieties. Food derived from corn line MON 89034 is as safe as food from the conventional counterpart.

Commodity : Corn / Maize (Zea mays L. )

Maize event MON89034 has been genetically modified to expresses two Bt-toxins (Cry1A.105 and Cry2Ab2 proteins) which provide protection to certain lepidopteran pests.

Application for food safety assessment.

The food safety assessment performed by the National Center for Genetic Engineering and Biotechnology (BIOTEC) as advisory and technical arm of Thai FDA. BIOTEC conduct food safety assessment according to codex guideline and based on the safety data and information provided by the applicant (as specified in Annex 2 attached to Notification of the Ministry of Public Health No.431). According to the existing scientific data and information available during the safety assessment, it is concluded that the maize event MON 89034 is substantial equivalent to its conventional counterpart in the aspects of morphology, nutrition, allergenicity and toxicity.

Commodity : Corn / Maize (Zea mays L. )

Maize event MON88017 has been genetically modified to expresses Bt-toxin (Cry3Bb1 protein) which provide protection to certain coleopteran pests and CP4 EPSPS protein which confers tolerance to glyphosate herbicide.

Application for food safety assessment

The food safety assessment performed by the National Center for Genetic Engineering and Biotechnology (BIOTEC) as advisory and technical arm of Thai FDA. BIOTEC conduct food safety assessment according to codex guideline and based on the safety data and information provided by the applicant (as specified in Annex 2 attached to Notification of the Ministry of Public Health No.431). According to the existing scientific data and information available during the safety assessment, it is concluded that the maize event MON88017 is substantially equivalent to its conventional counterpart in terms of morphology, nutrition, toxicity and allergenicity.

Commodity:Corn / Maize (Zea mays L.)

Maize event MON89034 has been genetically modified to expresses two Bt-toxins (Cry1A.105 and Cry2Ab2 proteins) which provide protection to certain lepidopteran pests.

Application for food safety assessment.

The food safety assessment performed by the National Center for Genetic Engineering and Biotechnology (BIOTEC) as advisory and technical arm of Thai FDA. BIOTEC conduct food safety assessment according to codex guideline and based on the safety data and information provided by the applicant (as specified in Annex 2 attached to Notification of the Ministry of Public Health No.431). According to the existing scientific data and information available during the safety assessment, it is concluded that the maize event MON 89034 is substantial equivalent to its conventional counterpart in the aspects of morphology, nutrition, allergenicity and toxicity.

Commodity: Corn / Maize (Zea mays L.)

 

Maize event MON88017 has been genetically modified to expresses Bt-toxin (Cry3Bb1 protein) which provide protection to certain coleopteran pests and CP4 EPSPS protein which confers tolerance to glyphosate herbicide.

Application for food safety assessment

 

The food safety assessment performed by the National Center for Genetic Engineering and Biotechnology (BIOTEC) as advisory and technical arm of Thai FDA. BIOTEC conduct food safety assessment according to codex guideline and based on the safety data and information provided by the applicant (as specified in Annex 2 attached to Notification of the Ministry of Public Health No.431). According to the existing scientific data and information available during the safety assessment, it is concluded that the maize event MON88017 is substantially equivalent to its conventional counterpart in terms of morphology, nutrition, toxicity and allergenicity.

 

Application for direct use as feed

 

Turkish Biosafety Law, entered in force in 2010, diverges from EU legislations in some points
 such as food and feed use require different separate applications, risk assessments and approvals.
  Addition, our Law forsees prision sentences in some circumtances of Law violation and joint
 reponsibilities for the violation. Therefore, GM product owners avoid to make application for approval
and non product developer have made application till now. Instead, some Turkish assosiations
 such as poultry producers assosiations, animal feed assosiations have applied to get approval
for import of GM products for their members. Thus, name of product applicants are not product
developers for our country.

 

Turkish Feed Manufacturer's Association
Turkish Poultry Meat Producers and Breeders Association
Turkish Egg Producers Association

 

After the evaluation of reports released by Scientific Risk Assessment Committee and Socio- economic Assessment Committee and also by considering public opinion, Biosafety Board has approved the use of genetically modified maize MON89034 and products thereof for animal feed.

Please see EPA BRAD and FDA Consultation. Please see EPA Residue Tolerance Exemptions for Cry1A.105 and Cry2Ab2.