TY - JOUR
T1 - Conformational changes during proteolytic processing of a picornavirus capsid proteins
AU - Smyth, M.S.
AU - Trudgett, A.
AU - Martin, J.H.
AU - Hoey, E.M.
AU - Martin, S.J.
PY - 2000/1/1
Y1 - 2000/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033643617&partnerID=8YFLogxK
M3 - Article
C2 - 10963351
VL - 145
SP - 1473
EP - 1479
JO - Archives of Virology
JF - Archives of Virology
IS - 7
ER -