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

<p style="text-align: justify;">Potatoes are considered to be a staple food constituting up to 37% of the total average vegetable intake. The genetic modification present in transgenic potato lines RBMT15-101, SEMT15&ndash;02 and SEMT15&ndash;15 will not result in any change in the consumption pattern for potatoes. Due to their protection from CPB damage resistance and to infection by PVY, these potato lines may replace some existing commercial potato cultivars in all potato product applications. Hence, they will provide an alternate or additional choice to consumers and food manufacturers.</p>

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

<p style="text-align: justify;">The analysis of macro- and micronutrients from transgenic potato lines revealed only small differences with the respective values from non-transgenic controls and in each case the level was within the normal range of variation reported for commercial potatoes. It was concluded that the consumption of products from CPB-resistant potatoes has no significant impact on the nutritional quality of the Canadian and American food supply.</p>

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

<p style="text-align: justify;">The glycoalkaloids, solanine and chaconine, are naturally occurring toxicants found in potato tubers, particularly in green tubers that have been exposed to sunlight. Analyses of total glycoalkaloid (TGA) levels in each of the transgenic lines demonstrated that in each case the level was below the administrative guideline of 20 mg/100g fresh weight that has previously been established for TGA in potato.</p>

<p style="text-align: justify;">The amino acid sequence of the Cry3A protein expressed in these potatoes is closely related to the sequence of the same proteins that are present in strains of <i>B. thuringiensis</i> that have been used for over 30 years as commercial organic microbial insecticides. An analysis of the amino acid sequences of the inserted Cry3A and PVY CP did not show homologies with known mammalian protein toxins and they were not judged to have any potential for human toxicity. The history of known safe consumption of PVY CP from virus-infected plant products provides additional evidence of lack of toxicity.</p>

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

<p style="text-align: justify;">The Cry3A protein and PVY CP do not possess characteristics typical of known protein allergens. There were no regions of homology when the deduced amino acid sequences of these introduced proteins were compared to the amino acid sequences of known protein allergens. Unlike known protein allergens, the Cry3A protein was rapidly degraded by acid and/or enzymatic hydrolysis when exposed to simulated gastric or intestinal fluids. The Cry3A protein and PVY CP are extremely unlikely to be allergenic.</p>
