Shedding of vesicular stomatitis virus soluble glycoprotein by removal of carboxy-terminal peptide

Author:

Irving R A,Ghosh H P

Abstract

A comparison of partial NH2-terminal sequences of vesicular stomatitis viral glycoprotein G (molecular weight, 69,000) and the soluble extracellular glycoprotein antigen Gs (molecular weight, 57,000) shows that both of the sequences are identical. Tryptic fingerprint analyses show that Gs lacks the carboxy-terminal region containing the membrane-anchoring hydrophobic domain of G. These results suggest that Gs is formed by cleavage in the carboxy-terminal region of G.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference15 articles.

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3. Synthesis and assembly of membrane glycoproteins. Membrane anchoring COOH-terminal domain of vesicular stomatitis virus envelope glycoprotein G contains fatty acids;Capone J.;J. Biol. Chem.,1982

4. Partial structure analysis of the oligosaccharide moieties of the vesicular stomatitis virus glycoprotein by sequential chemical and enzymatic degradation;Etchison J. R.;Virology,1977

5. Synthesis and assembly of membrane glycoproteins: presence of leader peptide in nonglycosylated precursor of membrane glycoprotein of vesicular stomatitis virus;Irving R. A.;Proc. Natl. Acad. Sci. U.S.A.,1979

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