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PMID: 6092710 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Association of poliovirus proteins with the endoplasmic reticulum.

Journal of virology ·Vol. 52 ·No. 3 ·1984-12-00 ·Pages 777-83

Tershak DR

Abstract

Poliovirus proteins, except P3-7c, are associated with the endoplasmic reticulum after extraction of the cytoplasm and centrifugation of membranes to equilibrium in sucrose gradients. Proteins P3-2, P2-X, and P3-9 are found preferentially among the rough endoplasmic reticulum, whereas P3-7c is located in smooth endoplasmic reticulum fractions. P3-7c is probably not membrane associated, since it can be separated from membranes after centrifugation in buffer. However, P3-4a, P2-5b, P2-X, and P3-9 are avidly bound to membranes and cannot be dislodged with high-ionic-strength buffer containing EDTA or 4 M urea. These proteins are digested by trypsin, indicating peripheral rather than internal localization.

MeSH Terms
Detergents/pharmacology Endoplasmic Reticulum/metabolism Guanidines/pharmacology Intracellular Membranes/metabolism Molecular Weight Poliovirus/metabolism Protein Binding/drug effects Ribonucleases Trypsin Ultrasonics Urea/pharmacology Viral Proteins/metabolism Virus Replication
Chemicals
Detergents Guanidines Viral Proteins Urea Ribonucleases Trypsin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Tershak D R
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.52.3.777-783.1984
Published
1984-12-00
Pages
777-83
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC254596
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.52.3.777-783.1984 PMC Full Text View journal details
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