Conformational changes during proteolytic processing of a picornavirus capsid proteins

M.S. Smyth, A. Trudgett, J.H. Martin, E.M. Hoey, S.J. Martin

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


We have used synthetic peptide antibodies to probe conformational changes that occur during the cleavage cascade which generates the capsid proteins of a picornavirus. The initial translation product of 97 kDa, the precursor of all four structural proteins, is cleaved to form a 63 kDa fragment which, we show, has significantly different folding characteristics to both its larger parent and its products. We demonstrate that proteolytic cleavages as distant as 520 residues from epitopes confer sufficiently large conformational changes as to render them unrecognisable. To our knowledge, this is the first demonstration of this phenomenon in the picornavirus system.
Original languageEnglish
Pages (from-to)1473-1479
Number of pages7
JournalArchives of Virology
Issue number7
Publication statusPublished - 01 Jan 2000


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