<p style="text-align: justify;"><b>Dietary Exposure</b></p>

<p style="text-align: justify;">MON809 maize was intended mainly for use in animal feed. The major human food uses for maize are extensively processed starch and oil fractions prepared by wet or dry milling procedures and products include corn syrup and corn oil, neither containing protein. The potential human exposure to the modified protein from whole grain corn in the diet was considered to be very low due both to its low abundance in the protein fraction of the grain and to the proportionately low percentage of protein in the kernel, compared with the major starch component. Overall, the dietary exposure of consumers in the United States and Canada to insect resistant hybrids of MON809 maize was anticipated to be the same as for other lines of commercially available field maize.</p>

<p style="text-align: justify;"><b>Nutritional Data</b></p>

<p style="text-align: justify;">The nutritional quality of grain from MON809 maize was similar to that of grain from an equivalent non-transgenic line and to grain currently available in commerce. Grain was subjected to proximate analysis (<i>e.g.</i>, ash, moisture content, crude protein, crude fat), amino acid and fatty acid composition. Some minor differences were observed between MON809 and an equivalent non-transgenic line, but the levels were within the range of variation normally observed in the commercial grain supply and were attributed to variations in the plant genotypes rather than to the presence of the introduced genes.</p>

<p style="text-align: justify;"><b>Toxicity</b></p>

<p style="text-align: justify;">Data were submitted that demonstrated that the active Cry1Ab protein product of the inserted <i>cry1Ab</i> gene was equivalent to the protein contained in microbial <i>Bt</i> spray formulations that have been safely used in agriculture for more than 40 years. Studies on the Cry1Ab protein expressed in plants and the resulting proteolytic fragments were compared to the bacterial proteins and shown to be of similar molecular weight, amino acid sequence, immunological reactivity and trypsin resistance. The protein was not glycosylated and showed similar bioactivity and host range specificity to the native protein. The Cry1Ab and CP4 EPSPS proteins should pose no risks for consumption of products produced from insect resistant maize. The introduced proteins were compared to databases of known protein toxins and neither showed any significant amino acid sequence similarity to known protein toxins. Neither protein was toxic when fed to mice.</p>

<p style="text-align: justify;"><b>Allergenicity</b></p>

<p style="text-align: justify;">The Cry1Ab and CP4 EPSPS proteins are extremely unlikely to be allergens. The deduced amino acid sequences of the introduced proteins were compared to sequences of known allergens contained in the public domain databases GenBank, EMBL, Pir and SwissProt. No significant sequence homologies were detected. Neither the Cry1Ab and CP4 EPSPS protein originated from an allergenic source, or were structurally similar to known allergens. EPSPS is ubiquitous in bacteria, plants and animals and no toxic or allergenic effects have ever been reported. In addition, the potential for allergenicity was assessed based upon the characteristics of known food allergens (stability to digestion, stability to processing, abundance in foods). Protein allergens are normally resistant to digestion unlike the Cry1Ab protein that was shown to degrade readily in simulated gastric fluid. Similarly, data were presented showing that the CP4 EPSPS enzyme was rapidly inactivated by heat and by digestion in simulated mammalian gastric fluid.</p>

<p style="text-align: justify;">Maize products are an important alternative to wheat flour for individuals afflicted with coeliac disease, an immune mediated food intolerance for which wheat gliadins have been implicated as the causal agent. In light of the importance of corn products to these individuals, a sequence similarity search was conducted and no amino acid sequence homologies between the Cry1Ab protein and gliadins were detected.</p>
