Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid.

ABSTRACT: Nudaurelia capensis omega virus-like particles have been characterized as a 480-A procapsid and a 410-A capsid, both with T=4 quasisymmetry. Procapsids transition to capsids when pH is lowered from 7.6 to 5.0. Capsids undergo autoproteolysis at residue 570, generating the 74-residue C-terminal polypeptide that remains with the particle. Here we show that the particle size becomes smaller under conditions between pH 6.8 and 6.0 without activating cleavage and that the particle remains at an intermediate size when the pH is carefully maintained. At pH 5.8, cleavage is very slow, becoming detectable only after 9 h. The optimum pH for cleavage is 5.0 (half-life, approximately 30 min), with a significant reduction in the cleavage rate at pH values below 5. We also show that lowering the pH is r

SUBMITTER: Matsui T 

PROVIDER: S-EPMC2612371 | biostudies-literature | 2009 Jan

REPOSITORIES: biostudies-literature