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

Un-“ESCRT”-ed Budding

1
 and
2,*
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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Abstract

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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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

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