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PMID: 6196910 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Synthesis and subcellular localization of the murine coronavirus nucleocapsid protein.

Virology ·Vol. 130 ·No. 2 ·1983-10-30 ·Pages 527-32

Stohlman SA, Fleming JO, Patton CD, Lai MM

Abstract

The synthesis and processing of the nucleocapsid protein (pp60) of the JHM strain of murine coronaviruses were examined. Pulse-chase experiments showed that pp60 was synthesized initially as a protein of approximately 57,000 in molecular weight (p57). Immunoprecipitation using mouse anti-JHMV antiserum indicated that p57 was virus specific. Immunoprecipitation with monoclonal antibodies specific for pp60 showed that p57 was antigenically related to pp60 and was not phosphorylated, while the intracellular protein that comigrated with the virion nucleocapsid protein, pp60, was phosphorylated. The p57 was found exclusively in the cytosol while the majority of pp60 was associated with the membrane fraction but pp60 was not an integral membrane protein.

MeSH Terms
Animals Capsid/analysis,immunology,metabolism Cell Line Cell Membrane/analysis Cytosol/analysis Epitopes/analysis Mice Molecular Weight Murine hepatitis virus/metabolism Phosphorylation Protein Precursors/metabolism Protein Processing, Post-Translational
Chemicals
Epitopes Protein Precursors
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Stohlman S A
Fleming J O
Patton C D
Lai M M
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22 references, click to expand
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Article Info
Journal
Virology
Abbr.
Virology
ISSN
0042-6822
DOI
10.1016/0042-6822(83)90106-x
Published
1983-10-30
Pages
527-32
Language
English
Region
United States
NLM ID
0110674
PMCID
PMC7131714
Subset
IM
Grants
NIAID NIH HHS · AI19244 · United States
NINDS NIH HHS · NS18146 · United States
External Links
PubMed source DOI: 10.1016/0042-6822(83)90106-x PMC Full Text View journal details
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