abstract
- Two polypeptides associated with the envelope of vesicular stomatitis virus are obtained by exhaustive proteolytic digestion of the virion. Analysis of the tryptic peptides and determination of the partial amino acid sequence show that the larger membrane-anchoring peptide is derived from the hydrophobic COOH terminus of the viral transmembrane glycoprotein G. The smaller peptide is, however, derived from the nonglycosylated matrix protein M. Analysis of the membrane-anchoring peptide fragments obtained from virus labeled with [3H]palmitic acid shows that the larger peptide fragment contained all the fatty acid present in G, suggesting that the fatty acids in conjunction with the hydrophobic domain may be involved in the binding of G protein to the membrane.