Plate tectonics of virus shell assembly and reorganization in phage φ8, a distant relative of mammalian reoviruses.

ABSTRACT: The hallmark of a virus is its capsid, which harbors the viral genome and is formed from protein subunits, which assemble following precise geometric rules. dsRNA viruses use an unusual protein multiplicity (120 copies) to form their closed capsids. We have determined the atomic structure of the capsid protein (P1) from the dsRNA cystovirus Φ8. In the crystal P1 forms pentamers, very similar in shape to facets of empty procapsids, suggesting an unexpected assembly pathway that proceeds via a pentameric intermediate. Unlike the elongated proteins used by dsRNA mammalian reoviruses, P1 has a compact trapezoid-like shape and a distinct arrangement in the shell, with two near-identical conformers in nonequivalent structural environments. Nevertheless, structural similarity with the analogous p

SUBMITTER: El Omari K 

PROVIDER: S-EPMC3737474 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature