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14. Structural analysis of a feline norovirus protruding domain.

Author

Singh BK, Glatt S, Ferrer JL, Koromyslova AD, Leuthold MM, Dunder J, and Hansman GS

Subjects
Amino Acid Sequence, Animals, Antigens, Viral chemistry, Antigens, Viral genetics, Capsid Proteins genetics, Capsid Proteins immunology, Crystallography, X-Ray, Dogs, Humans, Mice, Models, Molecular, Molecular Sequence Data, Norovirus genetics, Norovirus immunology, Protein Conformation, Protein Interaction Domains and Motifs, Sequence Homology, Amino Acid, Capsid Proteins chemistry, Cats virology, Norovirus chemistry
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., (Copyright © 2014 Elsevier Inc. All rights reserved.)

Published
2015
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