title: Structural organization of an encephalitic human isolate of Banna virus (genus Seadornavirus, family Reoviridae).
abstract: Banna virus (BAV) is the type species of the genus Seadornavirus within the family Reoviridae. The Chinese BAV isolate (BAV-Ch), which causes encephalitis in humans, was shown to have a structural organization and particle morphology reminiscent of that of rotaviruses, with fibre proteins projecting from the surface of the particle. Intact BAV-Ch virus particles contain seven structural proteins, two of which (VP4 and VP9) form the outer coat. The inner (core) particles contain five additional proteins (VP1, VP2, VP3, VP8 and VP10) and are 'non-turreted', with a relatively smooth surface appearance. VP2 is the 'T = 2' protein that forms the innermost 'subcore' layer, whilst VP8 is the 'T = 13' protein forming the core-surface layer. Sequence comparisons indicate that BAV VP9 and VP10 are equivalent to the VP8* and VP5* domains, respectively, of rotavirus outer-coat protein VP4 (GenBank accession no. P12976). VP9 has also been shown to be responsible for virus attachment to the host-cell surface and may be involved in internalization. These similarities reveal a previously unreported genetic link between the genera Rotavirus and Seadornavirus, although the expression of BAV VP9 and VP10 from two separate genome segments, rather than by the proteolytic cleavage of a single gene product (as seen in rotavirus VP4), suggests a significant evolutionary jump between the members of these two genera.
authors.affiliation: Unité des Virus Emergents: EFS Alpes-Méditerranée and Faculté de Médecine de Marseille, Université de la Méditerranée, 27 Boulevard Jean Moulin, 13005 Marseille cedex 5, France.
authors.forename: Fauziah Mohd
authors.initials: FM
authors.lastname: Jaafar
authors.affiliation: Unité des Virus Emergents: EFS Alpes-Méditerranée and Faculté de Médecine de Marseille, Université de la Méditerranée, 27 Boulevard Jean Moulin, 13005 Marseille cedex 5, France.
authors.forename: Houssam
authors.initials: H
authors.lastname: Attoui
authors.affiliation: Institute for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Woking, Surrey GU24 0NF, UK.
authors.forename: Peter P C
authors.initials: PPC
authors.lastname: Mertens
authors.affiliation: Unité des Virus Emergents: EFS Alpes-Méditerranée and Faculté de Médecine de Marseille, Université de la Méditerranée, 27 Boulevard Jean Moulin, 13005 Marseille cedex 5, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: de Micco
authors.affiliation: Maladies Virales Émergentes et Systèmes d'Information UR034, Institut de Recherche pour le Développement, Marseille, France.|Unité des Virus Emergents: EFS Alpes-Méditerranée and Faculté de Médecine de Marseille, Université de la Méditerranée, 27 Boulevard Jean Moulin, 13005 Marseille cedex 5, France.
authors.forename: Xavier
authors.initials: X
authors.lastname: de Lamballerie
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018162:Coltivirus / Q000145:classification / Q000235:genetics* / Q000302:isolation & purification / Q000648:ultrastructure; D004586:Electrophoresis; D018792:Encephalitis, Viral / Q000821:virology*; D016679:Genome, Viral; D006801:Humans; D051379:Mice; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010802:Phylogeny; D012088:Reoviridae Infections / Q000821:virology*; D012401:Rotavirus / Q000235:genetics; D017422:Sequence Analysis, DNA; D014758:Viral Core Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014771:Virion / Q000648:ultrastructure
chemical_list: D014758:Viral Core Proteins; D015678:Viral Structural Proteins