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The Positively Charged Structural Virus Protein (VP₁) of Foot-and-Mouth Disease Virus (Type O₁) Contains a Highly Basic Part which may be Involved in Early Virus-Cell Interaction

Central Veterinary Institute Virology Department, Houtribweg 39 8221 RA Lelystad, The Netherlands

Polypeptides of ‘trypsin-resistant’ (TR) variants of foot-and-mouth disease virus type O₁ (BFS 1860) were analysed by electrofocusing and two-dimensional gel electrophoresis. In contrast to parent O₁ virus, trypsin treatment of these variants did not reduce their infectivity and their ability to attach to susceptible cells, although VP₁ was cleaved as in the parent virus. In OTR₁, one of the cloned isolates, an additional polypeptide (VP_A) with a mol. wt. approx. 31 x 10³ (31K), was found which resembled VP₁ (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_A is an elongated VP₁. 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 OTR₁) 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 VP₁ of the closely related O₁ Kaufbeuren.

Keywords: FMDV, trypsin resistance, cell attachment, elongated VP₁

Received 20 January 1982; accepted 10 May 1982.