Purified foot-and-mouth disease virus (FMDV) of type OK was treated with several endopeptidases of differing specificity. The immunizing protein VP was cleaved into two detectable fragments by all enzymes except for glutamic acid-specific V8 protease. The longest fragments were generated by mouse submaxillary gland protease and the shortest by trypsin treatment of the intact virion. Several fragments, including the peptides resulting from the cyanogen bromide (CNBr) cleavage of the isolated protein VP, were characterized in terms of their molecular weights, N- and C-terminal amino acids, and ability to induce virus-specific antibodies. The order of the fragments along the protein was determined, and then located on the amino acid sequence of the protein. Two enzyme-sensitive areas of the protein were found on the surface of the virion: between sequence positions 138 and 154 and between portion 200 and the C terminus. Peptides containing these sections were able to induce neutralizing antibodies against the homologous FMDV. When the virus was treated with trypsin or with chymotrypsin, several amino acids between the detectable fragments were lost and the infectivity of the virus was reduced. The infectivity was retained, however, when the enzyme treatment resulted in cleavage of protein with no loss of amino acids or only the cutting away of the C-terminal section. These results suggest that the property of cell attachment is restricted to small regions of the surface of the virus particle.


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