Immunogenic and cell attachment sites of FMDV: further evidence for their location in a single capsid polypeptide.
Chymotrypsin cleaves only one of the four major polypeptides of foot-and-mouth disease virus (FMDV serotype O) in situ. This polypeptide (VP1, mol. wt. 29 X 10(3) was first cleaved into fragments of mol. wt. 20 and 9 X 10(3) and further cleavage could be prevented by the addition of a large excess of bovine serum albumin. The infectivity of the virus particles at this stage was the same as that of the intact virus although the rate of attachment to BHK 21 cells was slower and the immunogenic activity was reduced. If hydrolysis was allowed to continue, VP1 was cleaved into fragments with mol. wt. 18 and less than 9 X 10(3), similar to those obtained with trypsin and the virus particles then had a greatly  reduced infectivity and a lower immunogenicity. Treatment of strains from five other serotypes of the virus with the two enzymes cleaved only VP1 in each instance and there was a corresponding loss of infectivity. The results are discussed in relation to the location and biological activity of the virus polypeptides.
D000818:Animals; D000914:Antibodies, Viral / Q000096:biosynthesis; D005537:Aphthovirus / Q000254:growth & development / Q000276:immunology* / Q000378:metabolism; D001666:Binding Sites, Antibody; D002213:Capsid / Q000276:immunology*; D002460:Cell Line; D002918:Chymotrypsin / Q000378:metabolism; D006168:Guinea Pigs; D006868:Hydrolysis; D008970:Molecular Weight; D009500:Neutralization Tests; D010455:Peptides / Q000276:immunology* / Q000378:metabolism; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism; D014764:Viral Proteins / Q000276:immunology* / Q000378:metabolism
D000914:Antibodies, Viral; D010455:Peptides; D014764:Viral Proteins; D014107:Tosyllysine Chloromethyl Ketone; D014108:Tosylphenylalanyl Chloromethyl Ketone; D002918:Chymotrypsin; D014357:Trypsin