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

<p style="text-align: justify;">The MON80100 line of transgenic maize is not a sweet maize, but rather, a field maize intended mainly for use in animal feed. However, some human food uses are relevant for field maize. The MON80100 maize hybrids would be either dry or wet-milled into various processed maize products. The genetic modification of MON80100 maize will not result in any change in the consumption pattern for this product. Consequently, dietary exposure to this product is 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 analysis of nutrients from transgenic MON80100 maize and non-transgenic maize did not reveal any significant differences in the levels of protein, fat, fibre and starch. Similarly, the levels of micronutrients including calcium, phosphorus, potassium and magnesium were within the established ranges for maize. Feeding trials with rats, catfish and quail in which raw or processed maize meal from transgenic MON80100 was incorporated into the diet, did not reveal any significant differences in weight gain, food consumption or gross pathology between test and control subjects. The consumption of products from MON80100 will have no significant impact on the nutritional quality of the food supply.</p>

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

<p style="text-align: justify;">The trypsin-resistant Cry1Ab protein core expressed in insect-protected MON80100 was identical to the same form of the protein contained in microbial <i>Bt</i> spray formulations that have been safely used in agriculture for more than 40 years. The low potential for toxicity of plant expressed Cry1Ab protein, and CP4 EPSPS and glyphosate oxidoreductase enzymes was demonstrated by a lack of sequence homologies with known mammalian protein toxins.</p>

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

<p style="text-align: justify;">The Cry1Ab protein, CP4 EPSPS and glyphosate oxidoreductase enzymes do not possess characteristics typical of known protein allergens. There were no regions of homology when the sequences of three introduced proteins were compared to the amino acid sequences of known protein allergens. Unlike known protein allergens, these proteins were rapidly degraded by acid and/or enzymatic hydrolysis when exposed to simulated gastric or intestinal fluids.</p>
