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PMID: 430608 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Structure of the murine leukemia virus envelope glycoprotein precursor.

Journal of virology ·Vol. 29 ·No. 2 ·1979-02-00 ·Pages 735-43

Witte ON, Wirth DF

Abstract

The glycosylated env gene precurosr (Pr80env) of Moloney murine leukemia virus has been isolated by selective immunoprecipitation. Use of the drug tunicamycin to inhibit nascent glycosylation or specific cleavage with endoglycosidase H demonstrated that the precursor contained an apoprotein with a molecular weight of 60,000. The finished virion glycoprotein (gp70) was largely resistant to the action of endoglycosidase H. Chromatography of the glycopeptides of Pr80env in conjunction with endoglycosidase H digestion studies suggested that the precursor contained two distinct major glycosylation sites. Analysis of partial proteolytic cleavage fragments of Pr80env before and after endoglycosidase H treatment placed the two glycosylation sites within a 30,000-dalton region of the apoprotein sequence. Kinetic experiments showed that carbohydrate processing as well as proteolytic cleavage are late steps in the maturation of Pr80env.

MeSH Terms
Apoproteins/analysis Glycoproteins/analysis Molecular Weight Moloney murine leukemia virus/analysis,drug effects,metabolism Protein Precursors/analysis,metabolism Tunicamycin/pharmacology Viral Proteins/analysis,metabolism
Chemicals
Apoproteins Glycoproteins Protein Precursors Viral Proteins Tunicamycin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Witte O N
Wirth D F
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37 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
Published
1979-02-00
Pages
735-43
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC353205
Subset
IM
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