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Viruses 2011, 3(1), 26-31; doi:10.3390/v3010026

Un-“ESCRT”-ed Budding

1 Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10128, USA 2 Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794, USA
* Author to whom correspondence should be addressed.
Received: 28 November 2010 / Revised: 28 December 2010 / Accepted: 3 January 2011 / Published: 18 January 2011
(This article belongs to the Section Editorial)
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In their recent publication, Rossman et al. [1] describe how the inherent budding capability of its M2 protein allows influenza A virus to bypass recruitment of the cellular ESCRT machinery enlisted by several other enveloped RNA and DNA viruses, including HIV, Ebola, rabies, herpes simplex type 1 and hepatitis B. Studies from the same laboratory [2] and other laboratories [3–6] indicate that budding of plasmid-derived virus-like particles can be mediated by the influenza virus hemagglutinin and neuraminidase proteins in the absence of M2. These events are also independent of canonical ESCRT components [2,7]. Understanding how intrinsic properties of these influenza virus proteins permit ESCRT-independent budding expands our understanding of the budding process itself.
Keywords: influenza virus; M2; ESCRT; budding; HA; NA; cholesterol; membrane rafts influenza virus; M2; ESCRT; budding; HA; NA; cholesterol; membrane rafts
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Yondola, M.; Carter, C. Un-“ESCRT”-ed Budding. Viruses 2011, 3, 26-31.

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