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Advances in Virology
Volume 2011, Article ID 370606, 14 pages
Review Article

Association of Influenza Virus Proteins with Membrane Rafts

Department of Immunology and Molecular Biology, Veterinary Faculty, Free University Berlin, Philippstraße 13, 10115 Berlin, Germany

Received 15 March 2011; Accepted 2 May 2011

Academic Editor: Carolina B. Lopez

Copyright © 2011 Michael Veit and Bastian Thaa. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Assembly and budding of influenza virus proceeds in the viral budozone, a domain in the plasma membrane with characteristics of cholesterol/sphingolipid-rich membrane rafts. The viral transmembrane glycoproteins hemagglutinin (HA) and neuraminidase (NA) are intrinsically targeted to these domains, while M2 is seemingly targeted to the edge of the budozone. Virus assembly is orchestrated by the matrix protein M1, binding to all viral components and the membrane. Budding progresses by protein- and lipid-mediated membrane bending and particle scission probably mediated by M2. Here, we summarize the experimental evidence for this model with emphasis on the raft-targeting features of HA, NA, and M2 and review the functional importance of raft domains for viral protein transport, assembly and budding, environmental stability, and membrane fusion.