Journal
JOURNAL OF GENERAL VIROLOGY
Volume 93, Issue -, Pages 963-969Publisher
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.038778-0
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Funding
- Gates Cambridge Trust
- BBSRC [BB/G021031/1, BBS/E/D/20241864] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/G021031/1, BBS/E/D/20241864] Funding Source: researchfish
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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.
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