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

Un-“ESCRT”-ed Budding

1
 and 2,*
Received: 28 November 2010; in revised form: 28 December 2010 / Accepted: 3 January 2011 / Published: 18 January 2011
(This article belongs to the Section Editorial)
Download PDF [146 KB, uploaded 18 January 2011]
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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MDPI and ACS Style

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

AMA Style

Yondola M, Carter C. Un-“ESCRT”-ed Budding. Viruses. 2011; 3(1):26-31.

Chicago/Turabian Style

Yondola, Mark; Carter, Carol. 2011. "Un-“ESCRT”-ed Budding." Viruses 3, no. 1: 26-31.


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