title: Structural analysis of a feline norovirus protruding domain.
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.
authors.affiliation: 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.
authors.forename: Bishal K
authors.initials: BK
authors.lastname: Singh
authors.affiliation: EMBL Heidelberg, Structural and Computational Biology Unit, Heidelberg 69117, Germany.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Glatt
authors.affiliation: University Grenoble Alpes, IBS, F-38027 Grenoble, France; CEA, IBS, F-38027 Grenoble, France; CNRS, IBS, F-38027 Grenoble, France.
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Ferrer
authors.affiliation: 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.
authors.forename: Anna D
authors.initials: AD
authors.lastname: Koromyslova
authors.affiliation: 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.
authors.forename: Mila M
authors.initials: MM
authors.lastname: Leuthold
authors.affiliation: 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.
authors.forename: Jessica
authors.initials: J
authors.lastname: Dunder
authors.affiliation: 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.
authors.forename: Grant S
authors.initials: GS
authors.lastname: Hansman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000956:Antigens, Viral / Q000737:chemistry / Q000235:genetics; D036022:Capsid Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D002415:Cats / Q000821:virology*; D018360:Crystallography, X-Ray; D004285:Dogs; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D029322:Norovirus / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D017386:Sequence Homology, Amino Acid
chemical_list: D000956:Antigens, Viral; D036022:Capsid Proteins
keywords: Diarrhea; Norovirus; Virus capsid; X-ray crystallography