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

S Flasinski; A Dzianott; J A Speir; J E Johnson; J J Bujarski

doi:10.1128/JVI.71.3.2500-2504.1997

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

J Virol. 1997 Mar;71(3):2500-4. doi: 10.1128/JVI.71.3.2500-2504.1997.

Authors

S Flasinski¹, A Dzianott, J A Speir, J E Johnson, J J Bujarski

Affiliation

¹ Plant Biology Division, S.R. Noble Foundation, Inc., Ardmore, Oklahoma 73402, USA.

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Bromovirus / isolation & purification*
Bromovirus / ultrastructure
Capsid / chemistry*
Capsid / genetics*
Crystallography, X-Ray
Mutagenesis, Site-Directed
RNA, Viral / metabolism*

Substances

RNA, Viral

Abstract

Publication types

MeSH terms

Substances

Grants and funding