Influenza A virus belongs to the Orthomyxoviridae family. It is an enveloped virus that contains a segmented and negative-sense RNA genome. Influenza A viruses cause annual epidemics and occasional major pandemics, are a major cause of morbidity and mortality worldwide, and have a significant financial impact on society. Assembly and budding of new viral particles are a complex and multi-step process involving several host and viral factors. Influenza viruses use lipid raft domains in the apical plasma membrane of polarized epithelial cells as sites of budding. Two viral glycoproteins, haemagglutinin and neuraminidase, concentrate in lipid rafts, causing alterations in membrane curvature and initiation of the budding process. Matrix protein 1 (M1), which forms the inner structure of the virion, is then recruited to the site followed by incorporation of the viral ribonucleoproteins and matrix protein 2 (M2). M1 can alter membrane curvature and progress budding, whereas lipid raft-associated M2 stabilizes the site of budding, allowing for proper assembly of the virion. In the later stages of budding, M2 is localized to the neck of the budding virion at the lipid phase boundary, where it causes negative membrane curvature, leading to scission and virion release.
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October 2014
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Conference Article|
September 18 2014
Alterations of membrane curvature during influenza virus budding
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Coronavirus
Agnieszka Martyna;
Agnieszka Martyna
*School of Biosciences, University of Kent, Canterbury CT2 7NJ, U.K.
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Jeremy Rossman
Jeremy Rossman
1
*School of Biosciences, University of Kent, Canterbury CT2 7NJ, U.K.
1To whom correspondence should be addressed (emailj.s.rossman@kent.ac.uk).
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Publisher: Portland Press Ltd
Received:
May 12 2014
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem Soc Trans (2014) 42 (5): 1425–1428.
Article history
Received:
May 12 2014
Citation
Agnieszka Martyna, Jeremy Rossman; Alterations of membrane curvature during influenza virus budding. Biochem Soc Trans 1 October 2014; 42 (5): 1425–1428. doi: https://doi.org/10.1042/BST20140136
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