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PMID: 3467351 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.

Implications of the picornavirus capsid structure for polyprotein processing.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 84 ·No. 1 ·1987-01-00 ·Pages 21-5

Arnold E, Luo M, Vriend G, Rossmann MG, Palmenberg AC, Parks GD, Nicklin MJ, Wimmer E

Abstract

Mature picornaviral proteins are derived by progressive, posttranslational cleavage of a precursor polyprotein. These cleavages play a role in the control of virus functions. Although the processed termini are separated by as much as 75 A in the native virus capsid, the fold and arrangement of polypeptide chains in a protomer before proteolysis are likely to be similar to that found in the mature virus. The three-dimensional structures of rhinovirus and Mengo virus suggest that the cleavage sites within the protomeric precursor are in structurally flexible regions. The final proteolytic processing event, maturation of the virion peptide VP0 (also called peptide 1AB) appears to occur by an unusual autocatalytic serine protease-type mechanism possibly involving viral RNA basic groups that would serve as proton-abstractors during the cleavage reaction.

MeSH Terms
Capsid/genetics,metabolism Dipeptides Genes Genes, Viral Models, Molecular Picornaviridae/genetics,metabolism Protein Conformation Protein Processing, Post-Translational
Chemicals
Dipeptides
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Arnold E
Luo M
Vriend G
Rossmann M G
Palmenberg A C
Parks G D
Nicklin M J
Wimmer E
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32 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.84.1.21
Published
1987-01-00
Pages
21-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC304133
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.84.1.21 PMC Full Text View journal details
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