Polypeptides of ‘trypsin-resistant’ (TR) variants of foot-and-mouth disease virus type O (BFS 1860) were analysed by electrofocusing and two-dimensional gel electrophoresis. In contrast to parent O virus, trypsin treatment of these variants did not reduce their infectivity and their ability to attach to susceptible cells, although VP was cleaved as in the parent virus. In OTR, one of the cloned isolates, an additional polypeptide (VP) with a mol. wt. approx. 31 × 10 (31K), was found which resembled VP (28K) in being positively charged and cleaved by trypsinization of the virus into a neutral 18K polypeptide (P18) and a strongly basic fragment (pI > 10) with a mol. wt. of approx. 6K (P6). These findings substantiate the hypothesis that VP is an elongated VP. While P18 fragments of both trypsin-treated parent virus and OTR progeny viruses focused at identical (neutral) pH. P6 fragments of trypsinized OTR variants (including OTR) were even more positively charged than P6 of parent virus. This difference in charge of the P6 polypeptide may be responsible for the retained cell attachment ability of trypsinized OTR viruses. The data are discussed with respect to the known amino acid sequence of VP of the closely related O Kaufbeuren.


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