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. 1997 Mar;71(3):2500–2504. 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.

S Flasinski 1, A Dzianott 1, J A Speir 1, J E Johnson 1, J J Bujarski 1
PMCID: PMC191363  PMID: 9032390

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.

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Selected References

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