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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.

Original publication

DOI

10.1038/ncomms5816

Type

Journal article

Journal

Nat Commun

Publication Date

16/09/2014

Volume

5

Keywords

Amino Acid Sequence, Animals, Cattle, Chickens, Dogs, Epithelial Cells, Gene Expression, Host Specificity, Influenza A Virus, H1N1 Subtype, Influenza A Virus, H3N2 Subtype, Madin Darby Canine Kidney Cells, Models, Molecular, Molecular Sequence Data, Ovum, Sequence Alignment, Viral Load, Viral Nonstructural Proteins, Virion