title: Modeling of the rotavirus group C capsid predicts a surface topology distinct from other rotavirus species.
abstract: Rotavirus C (RVC) causes sporadic gastroenteritis in adults and is an established enteric pathogen of swine. Because RVC strains grow poorly in cell culture, which hinders generation of virion-derived RVC triple-layered-particle (TLP) structures, we used the known Rotavirus A (RVA) capsid structure to model the human RVC (Bristol) capsid. Comparative analysis of RVA and RVC capsid proteins showed major differences at the VP7 layer, an important target region for vaccine development due to its antigenic properties. Our model predicted the presence of a surface extended loop in RVC, which could form a major antigenic site on the capsid. We analyzed variations in the glycosylation patterns among RV capsids and identified group specific conserved sites. In addition, our results showed a smaller RVC VP4 foot, which protrudes toward the intermediate VP6 layer, in comparison to that of RVA. Finally, our results showed major structural differences at the VP8* glycan recognition sites.
authors.affiliation: Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: elif.eren@nih.gov.
authors.forename: Elif
authors.initials: E
authors.lastname: Eren
authors.affiliation: Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
authors.forename: Kimberly
authors.initials: K
authors.lastname: Zamuda
authors.affiliation: Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
authors.forename: John T
authors.initials: JT
authors.lastname: Patton
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000956:Antigens, Viral / Q000235:genetics / Q000276:immunology; D001666:Binding Sites, Antibody / Q000235:genetics*; D002213:Capsid / Q000276:immunology* / Q000648:ultrastructure*; D036022:Capsid Proteins / Q000235:genetics / Q000276:immunology; D017124:Conserved Sequence / Q000235:genetics; D000939:Epitopes / Q000276:immunology; D000882:Haplorhini; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008992:Monkey Diseases / Q000821:virology; D016601:RNA-Binding Proteins / Q000235:genetics; D012401:Rotavirus / Q000145:classification / Q000235:genetics* / Q000276:immunology*; D012400:Rotavirus Infections / Q000821:virology; D022243:Rotavirus Vaccines / Q000276:immunology; D016415:Sequence Alignment; D013552:Swine; D013553:Swine Diseases / Q000821:virology; D017361:Viral Nonstructural Proteins / Q000235:genetics
chemical_list: D000956:Antigens, Viral; D036022:Capsid Proteins; D000939:Epitopes; D016601:RNA-Binding Proteins; D022243:Rotavirus Vaccines; C060339:VP4 protein, Rotavirus; C061332:VP6 protein, Rotavirus; C050779:VP7 protein, Rotavirus; D017361:Viral Nonstructural Proteins; C079234:NS35 protein, rotavirus
keywords: Antigenic topology; Capsid structure; Rotavirus