title: Conserved and host-specific features of influenza virion architecture.
abstract: Viruses use virions to spread between hosts, and virion composition is therefore the primary determinant of viral transmissibility and immunogenicity. However, the virions of many viruses are complex and pleomorphic, making them difficult to analyse in detail. Here we address this by identifying and quantifying virion proteins with mass spectrometry, producing a complete and quantified model of the hundreds of host-encoded and viral proteins that make up the pleomorphic virions of influenza viruses. We show that a conserved influenza virion architecture is maintained across diverse combinations of virus and host. This 'core' architecture, which includes substantial quantities of host proteins as well as the viral protein NS1, is elaborated with abundant host-dependent features. As a result, influenza virions produced by mammalian and avian hosts have distinct protein compositions. Finally, we note that influenza virions share an underlying protein composition with exosomes, suggesting that influenza virions form by subverting microvesicle production.
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Edward C
authors.initials: EC
authors.lastname: Hutchinson
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Philip D
authors.initials: PD
authors.lastname: Charles
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Svenja S
authors.initials: SS
authors.lastname: Hester
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Thomas
authors.affiliation: 1] Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK [2].
authors.forename: David
authors.initials: D
authors.lastname: Trudgian
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Mónica
authors.initials: M
authors.lastname: Martínez-Alonso
authors.affiliation: Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
authors.forename: Ervin
authors.initials: E
authors.lastname: Fodor
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002645:Chickens; D004285:Dogs; D004847:Epithelial Cells / Q000821:virology; D015870:Gene Expression; D058507:Host Specificity / Q000235:genetics*; D053118:Influenza A Virus, H1N1 Subtype / Q000235:genetics / Q000254:growth & development / Q000648:ultrastructure*; D053122:Influenza A Virus, H3N2 Subtype / Q000235:genetics / Q000254:growth & development / Q000648:ultrastructure*; D061985:Madin Darby Canine Kidney Cells; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010063:Ovum / Q000821:virology; D016415:Sequence Alignment; D019562:Viral Load; D017361:Viral Nonstructural Proteins / Q000235:genetics*; D014771:Virion / Q000235:genetics / Q000254:growth & development / Q000648:ultrastructure*
chemical_list: C085820:INS1 protein, influenza virus; D017361:Viral Nonstructural Proteins