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Construction and crystal structure of recombinant STNV capsids

Lane, Stephen W., Dennis, Caitriona A., Lane, Claire L., Trinh, Chi H., Rizkallah, Pierre, Stockley, Peter G. and Phillips, Simon E. V. 2011. Construction and crystal structure of recombinant STNV capsids. Journal of Molecular Biology 413 (1) , pp. 41-50. 10.1016/j.jmb.2011.07.062

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Abstract

A codon-optimised gene has been expressed in Escherichia coli to produce the coat protein (CP) of the Satellite Tobacco Necrosis Virus. This protein assembles in vivo into capsids closely resembling those of the T = 1 wild-type virus. These virus-like particles (VLPs) package the recombinant mRNA transcript and can be disassembled and reassembled using different buffer conditions. The X-ray crystal structure of the VLP has been solved and refined at 1.4 Å resolution and shown to be very similar to that of wild-type Satellite Tobacco Necrosis Virus, except that icosahedral symmetry constraints could be removed to reveal differences between subunits, presumably owing to crystal packing. An additional low-resolution X-ray crystal structure determination revealed well-ordered RNA fragments lodged near the inside surface of the capsid, close to basic clusters formed by the N-terminal helices that project into the interior of the particle. The RNA consists of multiple copies of a 3-bp helical stem, with a single unpaired base at the 3′ end, and probably consists of a number of short stem–loops where the loop region is disordered. The arrangement of the RNA is different from that observed in other satellite viruses.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: Q Science > QH Natural history > QH301 Biology
Q Science > QH Natural history > QH426 Genetics
R Medicine > R Medicine (General)
Uncontrolled Keywords: virus structure, x-ray crystallography, protein–RNA interactions, synthetic gene, virus-like particle
Publisher: Elsevier
ISSN: 0022-2836
Last Modified: 04 Jun 2017 03:45
URI: http://orca.cf.ac.uk/id/eprint/26022

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