Implications of the picornavirus capsid structure for polyprotein processing

E. Arnold, M. Luo, G. Vriend, M. G. Rossmann, A. C. Palmenberg, G. D. Parks, M. J. Nicklin, E. Wimmer

Research output: Contribution to journalArticlepeer-review

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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 Å 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.

Original languageEnglish (US)
Pages (from-to)21-25
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number1
DOIs
StatePublished - 1987
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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