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Virology. 2015 Jan 1;474:181-5. doi: 10.1016/j.virol.2014.10.028. Epub 2014 Nov 19.

Structural analysis of a feline norovirus protruding domain.

Author information

1
Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg 69120, Germany; Department of Infectious Diseases, Virology, University of Heidelberg, Heidelberg 69120, Germany.
2
EMBL Heidelberg, Structural and Computational Biology Unit, Heidelberg 69117, Germany.
3
University Grenoble Alpes, IBS, F-38027 Grenoble, France; CEA, IBS, F-38027 Grenoble, France; CNRS, IBS, F-38027 Grenoble, France.
4
Schaller Research Group at the University of Heidelberg and the DKFZ, Heidelberg 69120, Germany; Department of Infectious Diseases, Virology, University of Heidelberg, Heidelberg 69120, Germany. Electronic address: g.hansman@dkfz.de.

Abstract

Norovirus infects different animals, including humans, mice, dogs, and cats. Here, we show an X-ray crystal structure of a feline GIV.2 norovirus capsid-protruding (P) domain to 2.35Å resolution. The feline GIV.2 P domain was reminiscent of human norovirus P domains, except for a novel P2 subdomain α-helix and an extended P1 subdomain interface loop. These new structural features likely obstructed histo-blood group antigens, which are attachment factors for human norovirus, from binding at the equivalent sites on the feline GIV.2 P domain. Additionally, an ELISA showed that the feline GIV.2 was antigenically distinct from a human GII.10 norovirus.

KEYWORDS:

Diarrhea; Norovirus; Virus capsid; X-ray crystallography

PMID:
25463616
DOI:
10.1016/j.virol.2014.10.028
[Indexed for MEDLINE]
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