Gradient SDS-polyacrylamide gel electrophoresis (PAGE) and proteolytic digestions were utilized to examine the virion proteins of two isolates of wild-type vesicular stomatitis virus (WT-VSV), WT from the American Type Culture Collection and WT from Glasgow, as well as temperature-sensitive () mutant G31 and a central nervous system (CNS) isolate of G31 designated G31BP. The WT M protein differed in electrophoretic mobility and in its tryptic or chymotryptic peptide maps from the I-labelled M proteins in WT, G31 or G31BP. The M protein in the latter three viruses appeared identical using either tryptic or chymotryptic digestion procedures; however, limited digestion with V8 protease revealed a difference between the M protein of G31 and both WT and G31BP M proteins. The L, NS and G proteins all had identical tryptic and chymotryptic peptide maps in WT, G31 and G31BP virions. The N protein, however, was demonstrated to be distinctly different in the WT virion when compared with the G31 (or G31BP) virion by its tryptic peptide map. In addition, limited proteolytic digestion of the I-labelled N proteins revealed a different peptide structure in G31BP compared to N proteins of G31 or WT. The altered N protein in the CNS isolate, G31BP, is discussed in terms of its altered phenotype of labile viral RNA, and its potential role in the unique CNS disease associated with this virus.


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