Structure-based rationale for the rescue of systemic movement of brome mosaic virus by spontaneous second-site mutations in the coat protein gene.

Abstract:

:We describe spontaneous second-site reversions within the coat protein open reading frame that rescue the systemic-spread phenotype and increase virion stability of a mutant of brome mosaic virus. Based on the crystal structure of the related cowpea chlorotic mottle virus, we show that the modified residues are spatially clustered to affect the formation of hexamers and pentamers and therefore virion stability.

journal_name

J Virol

journal_title

Journal of virology

authors

Flasinski S,Dzianott A,Speir JA,Johnson JE,Bujarski JJ

doi

10.1128/JVI.71.3.2500-2504.1997

subject

Has Abstract

pub_date

1997-03-01 00:00:00

pages

2500-4

issue

3

eissn

0022-538X

issn

1098-5514

journal_volume

71

pub_type

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