Structural analysis of bovine norovirus protruding domain

Bishal Kumar Singh; Anna Koromyslova; Grant S. Hansman

doi:10.1016/j.virol.2015.10.022

Structural analysis of bovine norovirus protruding domain

Bishal Kumar Singh, Anna Koromyslova, Grant S. Hansman

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

5 Scopus citations

Abstract

We determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibody that was capable of binding the five different (GI-GV) P domains. Our data suggests that genetically diverse noroviruses still contain common epitopes.

Original language	English (US)
Pages (from-to)	296-301
Number of pages	6
Journal	Virology
Volume	487
DOIs	https://doi.org/10.1016/j.virol.2015.10.022
State	Published - Jan 1 2016
Externally published	Yes

Keywords

Antibodies
Bovine norovirus
Cross-reactivity

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2015.10.022

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title = "Structural analysis of bovine norovirus protruding domain",

abstract = "We determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibody that was capable of binding the five different (GI-GV) P domains. Our data suggests that genetically diverse noroviruses still contain common epitopes.",

keywords = "Antibodies, Bovine norovirus, Cross-reactivity",

author = "Singh, {Bishal Kumar} and Anna Koromyslova and Hansman, {Grant S.}",

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doi = "10.1016/j.virol.2015.10.022",

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AU - Singh, Bishal Kumar

AU - Koromyslova, Anna

AU - Hansman, Grant S.

PY - 2016/1/1

Y1 - 2016/1/1

N2 - We determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibody that was capable of binding the five different (GI-GV) P domains. Our data suggests that genetically diverse noroviruses still contain common epitopes.

AB - We determined a structure of a bovine (genogroup III, GIII) norovirus capsid protruding (P) domain using X-ray crystallography. The bovine P domain was reminiscent of other norovirus genogroups (GI, GII, GIV, and GV), but closely matched the human GI P domain. We also identified a monoclonal antibody that was capable of binding the five different (GI-GV) P domains. Our data suggests that genetically diverse noroviruses still contain common epitopes.

KW - Antibodies

KW - Bovine norovirus

KW - Cross-reactivity

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DO - 10.1016/j.virol.2015.10.022

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AN - SCOPUS:84947267975

SN - 0042-6822

VL - 487

SP - 296

EP - 301

JO - Virology

JF - Virology

ER -

Structural analysis of bovine norovirus protruding domain

Abstract

Keywords

ASJC Scopus subject areas

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