Alterations in Peptide Structure of Vesicular Stomatitis Virus Mutant and its Central Nervous System Isolate

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Abstract
Gradient SDS[sodium dodecyl sulfate]-polyacrylamide gel electrophoresis (PAGE) and proteolytic digestions were used to examine the virion proteins of 2 isolates of wild-type vesicular stomatitis virus (WT-VSV), WTATCC from the American Type Culture Collection and WTGL from Glasgow [Scotland, UK], as well as temperature-sensitive (ts) mutant ts G31 and a [mouse] CNS isolate of ts G31 designated ts G31BP. The WTATCC M protein differed in electrophoretic mobility and in its tryptic or chymotryptic peptide maps from the 125I-labeled M proteins in WTGL, ts G31 or ts G31BP. The M protein in the latter 3 viruses appeared identical using tryptic or chymotryptic digestion procedures; limited digestion with V8 protease revealed a difference between the M protein of ts G31 and WTGL and ts G31BP M proteins. The L, NS and G proteins all had identical tryptic and chymotryptic peptide maps in WTGL, ts G31 and ts G31BP virions. The N protein was distinctly different in the WTGL virion when compared with the ts G31 (or ts G31BP) virion by its tryptic peptide map. Limited proteolytic digestion of the 125I-labeled N proteins revealed a different peptide structure in ts G31BP compared to N proteins of ts G31 or WTGL. The altered N protein in the CNS isolate, ts G31BP, is discussed in terms of its altered in vivo phenotype of labile viral RNA and its potential role in the unique CNS disease associated with this virus.

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