Analysis of amino acid variation in the P2 domain of the GII-4 norovirus VP1 protein reveals putative variant-specific epitopes

David J. Allen; Jim J. Gray; Chris I. Gallimore; Jacqueline Xerry; Miren Iturriza-Gómara

doi:10.1371/journal.pone.0001485

Analysis of amino acid variation in the P2 domain of the GII-4 norovirus VP1 protein reveals putative variant-specific epitopes

David J. Allen, Jim J. Gray, Chris I. Gallimore, Jacqueline Xerry, Miren Iturriza-Gómara

Norwich Medical School

Research output: Contribution to journal › Article › peer-review

116 Citations (Scopus)

Abstract

Our data identifies two sites in this region, which show significant amino acid substitutions associated with the appearance of variant strains responsible for epidemics with major public health impact. Homology modelling studies revealed the exposed nature of these sites on the capsid surface, providing supportive structural data that these two sites are likely to be associated with putative variant-specific epitopes. Furthermore, the patterns in the evolution of these viruses at these sites suggests that noroviruses follow a neutral network pattern of evolution.

Original language	English
Article number	e1485
Journal	PLoS One
Volume	3
Issue number	1
DOIs	https://doi.org/10.1371/journal.pone.0001485
Publication status	Published - 23 Jan 2008

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10.1371/journal.pone.0001485Licence: CC BY

Cite this

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abstract = "Our data identifies two sites in this region, which show significant amino acid substitutions associated with the appearance of variant strains responsible for epidemics with major public health impact. Homology modelling studies revealed the exposed nature of these sites on the capsid surface, providing supportive structural data that these two sites are likely to be associated with putative variant-specific epitopes. Furthermore, the patterns in the evolution of these viruses at these sites suggests that noroviruses follow a neutral network pattern of evolution.",

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AB - Our data identifies two sites in this region, which show significant amino acid substitutions associated with the appearance of variant strains responsible for epidemics with major public health impact. Homology modelling studies revealed the exposed nature of these sites on the capsid surface, providing supportive structural data that these two sites are likely to be associated with putative variant-specific epitopes. Furthermore, the patterns in the evolution of these viruses at these sites suggests that noroviruses follow a neutral network pattern of evolution.

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