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. 1982 Dec;44(3):900–906. doi: 10.1128/jvi.44.3.900-906.1982

In vitro synthesis and assembly of picornaviral capsid intermediate structures.

A C Palmenberg
PMCID: PMC256349  PMID: 6294338

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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