title: N-terminal amino acid sequences in the major capsid proteins of foot-and-mouth disease virus types A, O, and C.
abstract: Sequences of amino acids at the N-termini of virus proteins VP1, VP2, and VP3 were determined for foot-and-mouth disease virus types A12 strain 119, O1Brugge and C3Resende. In the polyacrylamide gel electrophoresis system used to purify the proteins, VP3 migrated faster than VP1 or VP2; and in the virion, VP3 could be cleaved by trypsin into VP3a and VP3b. The N-terminal amino acids for each of the virus types were glycine in VP1, aspartic acid in VP2, and threonine in VP3. No divergences in sequence across the virus types were indicated until at least the fourth position in VP1, and the third in VP3. For virus types A12, O1 and C3, the sequences were, respectively: for VP1 (Gly-ile-phe,pro,val---), (Gly,ile,phe---) and Gly-ile-phe,ala---); for VP2 (Asp,X,met---), (Asp---) and Asp-leu---); and for VP3 (Thr-thr-ala-thr---), (Thr-thr-ser---) and (Thr-thr---). Unresolved mixtures of VP3a and VP3b, from either A12 or O1 viruses, appeared to have the N-terminal amino acids threonine, which is presumed to be the same threonine as in uncleaved VP3 and serine, which is generated by the tryptic cleavage.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D005537:Aphthovirus / Q000032:analysis*; D001216:Asparagine / Q000032:analysis; D001224:Aspartic Acid / Q000032:analysis; D003619:Dansyl Compounds; D005998:Glycine / Q000032:analysis; D007931:Leucyl Aminopeptidase; D012694:Serine / Q000032:analysis; D012703:Serotyping; D013912:Threonine / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis*
chemical_list: D000596:Amino Acids; D003619:Dansyl Compounds; D014764:Viral Proteins; D013912:Threonine; D001224:Aspartic Acid; D012694:Serine; D001216:Asparagine; D007931:Leucyl Aminopeptidase; D005998:Glycine