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Alterations of membrane curvature during influenza virus budding

Rossman, Jeremy S., Martyna, Agnieszka (2014) Alterations of membrane curvature during influenza virus budding. Biochemical Society Transactions, 42 (5). pp. 1425-1428. ISSN 0300-5127. (doi:10.1042/BST20140136) (KAR id:42830)

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http://dx.doi.org/10.1042/BST20140136

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1042/BST20140136
Uncontrolled keywords: assembly, budding, influenza virus, membrane curvature, membrane scission, matrix protein 2 (M2)
Subjects: Q Science > QR Microbiology
Divisions: Divisions > Division of Natural Sciences > School of Biosciences
Depositing User: Jeremy Rossman
Date Deposited: 04 Sep 2014 12:43 UTC
Last Modified: 19 Jun 2019 13:55 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/42830 (The current URI for this page, for reference purposes)
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