El Omari, Kamel, Sutton, Geoff, Ravantti, Janne J, Zhang, Hanwen, Walter, Thomas S, Grimes, Jonathan M, Bamford, Dennis H, Stuart, David I and Mancini, Erika J (2013) Plate tectonics of virus shell assembly and reorganization in phage φ8, a distant relative of mammalian reoviruses. Structure, 21 (8). pp. 1384-1395. ISSN 1878-4186

Preview

PDF - Published Version Available under License Creative Commons Attribution No Derivatives. Download (4MB) | Preview

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 protein from the mammalian viruses suggests a common ancestor. The unusual shape of the molecule may facilitate dramatic capsid expansion during phage maturation, allowing P1 to switch interaction interfaces to provide capsid plasticity.

Item Type:	Article
Schools and Departments:	School of Life Sciences > Biochemistry
Subjects:	Q Science > QH Natural history > QH0301 Biology
Depositing User:	Tom Gittoes
Date Deposited:	23 Apr 2015 09:37
Last Modified:	15 Mar 2017 01:34
URI:	http://sro.sussex.ac.uk/id/eprint/53719

View download statistics for this item

📧 Request an update