title: Release of filamentous and spherical influenza A virus is not restricted by tetherin.
abstract: The cellular protein tetherin is thought to act as a 'leash' that anchors many enveloped viruses to the plasma membrane and prevents their release. We found that replication of multiple strains of influenza A virus was generally insensitive to alteration of tetherin levels, as assessed by output titre or scanning electron microscopy of cell-associated virions. This included human, swine, avian and equine isolates, strains that form filamentous or spherical particles and viruses that lack the M2 or NS1 proteins. Levels of cell-surface tetherin were not reduced by influenza infection, but tetherin and the viral haemagglutinin co-localized on the plasma membrane. However, tetherin could not be detected in filamentous virions, suggesting that influenza may possess a mechanism to exclude it from virions. Overall, if influenza does encode a specific antagonist of tetherin, it is not M2 or NS1 and we find no evidence for a role in host range specificity.
authors.affiliation: Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.
authors.forename: Emily A
authors.initials: EA
authors.lastname: Bruce
authors.affiliation: Division of Infectious Diseases, Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QQ, UK.
authors.forename: Truus E
authors.initials: TE
authors.lastname: Abbink
authors.affiliation: Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.
authors.forename: Helen M
authors.initials: HM
authors.lastname: Wise
authors.affiliation: School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
authors.forename: Ruth
authors.initials: R
authors.lastname: Rollason
authors.affiliation: Department of Infectious Disease, King's College London School of Medicine, Guy's Hospital, London SE1 9RT, UK.
authors.forename: Rui Pedro
authors.initials: RP
authors.lastname: Galao
authors.affiliation: School of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
authors.forename: George
authors.initials: G
authors.lastname: Banting
authors.affiliation: Department of Infectious Disease, King's College London School of Medicine, Guy's Hospital, London SE1 9RT, UK.
authors.forename: Stuart J
authors.initials: SJ
authors.lastname: Neil
authors.affiliation: Division of Virology, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.
authors.forename: Paul
authors.initials: P
authors.lastname: Digard
mesh_terms: D000818:Animals; D015703:Antigens, CD / Q000378:metabolism*; D002460:Cell Line; D002462:Cell Membrane / Q000737:chemistry; D058851:GPI-Linked Proteins / Q000378:metabolism; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000378:metabolism; D054884:Host-Pathogen Interactions; D006801:Humans; D009980:Influenza A virus / Q000254:growth & development / Q000502:physiology*; D018613:Microscopy, Confocal; D008855:Microscopy, Electron, Scanning; D019562:Viral Load; D057074:Virus Release; D000074010:Bone Marrow Stromal Antigen 2
chemical_list: D015703:Antigens, CD; D058851:GPI-Linked Proteins; D019267:Hemagglutinin Glycoproteins, Influenza Virus; C094572:BST2 protein, human; D000074010:Bone Marrow Stromal Antigen 2