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Structural analysis of a feline norovirus protruding domain

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...

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Hauptverfasser: Singh, Bishal (VerfasserIn) , Glatt, Sebastian (VerfasserIn) , Ferrer, Jean-Luc (VerfasserIn) , Koromyslova, Anna D. (VerfasserIn) , Leuthold, Mila (VerfasserIn) , Dunder, Jessica (VerfasserIn) , Hansman, Grant S. (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2015
In: Virology
Year: 2014, Jahrgang: 474, Pages: 181-185
ISSN:1096-0341
DOI:10.1016/j.virol.2014.10.028
Online-Zugang:lizenzpflichtig
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Verfasserangaben:Bishal K. Singh, Sebastian Glatt, Jean-Luc Ferrer, Anna D. Koromyslova, Mila M. Leuthold, Jessica Dunder, Grant S. Hansman
Beschreibung
Zusammenfassung: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.
Beschreibung:Available online 19 November 2014
Gesehen am 17.06.2020
Beschreibung:Online Resource
ISSN:1096-0341
DOI:10.1016/j.virol.2014.10.028

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