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PMID: 6294338 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

In vitro synthesis and assembly of picornaviral capsid intermediate structures.

Journal of virology ·Vol. 44 ·No. 3 ·1982-12-00 ·Pages 900-6

Palmenberg AC

Abstract

Cell-free translation of encephalomyocarditis RNA in extracts of rabbit reticulocytes results in the synthesis of viral proteins indistinguishable from those produced during virus infection of cells. The viral capsid proteins are produced in an active form capable of assembly into viral capsid intermediate structures. Protomers (5S), pentamers (14S), and shell-like structures (75 to 85S) can be detected after prolonged incubation in the extracts. Proteolytic cleavage of capsid precursor proteins appears to be a prerequisite for assembly, in apparent contrast to cell-associated assembly. Assembly of pentamers is also preceded by conversion of protein epsilon 1 to epsilon in a step which may reflect an amino-terminal blocking reaction.

MeSH Terms
Animals Capsid/genetics,isolation & purification Encephalomyocarditis virus/genetics Molecular Weight Protein Biosynthesis RNA, Messenger/genetics RNA, Viral/genetics Rabbits Reticulocytes/metabolism Viral Proteins/genetics Virion/genetics
Chemicals
RNA, Messenger RNA, Viral Viral Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Palmenberg A C
References (20)
20 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.44.3.900-906.1982
Published
1982-12-00
Pages
900-6
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC256349
Subset
IM
Grants
NIAID NIH HHS · AI-17331 · United States
External Links
PubMed source DOI: 10.1128/JVI.44.3.900-906.1982 PMC Full Text View journal details
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