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Commentary

Un-“ESCRT”-ed Budding

by 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
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
MDPI and ACS Style

Yondola, M.; Carter, C. Un-“ESCRT”-ed Budding. Viruses 2011, 3, 26-31. https://0-doi-org.brum.beds.ac.uk/10.3390/v3010026

AMA Style

Yondola M, Carter C. Un-“ESCRT”-ed Budding. Viruses. 2011; 3(1):26-31. https://0-doi-org.brum.beds.ac.uk/10.3390/v3010026

Chicago/Turabian Style

Yondola, Mark, and Carol Carter. 2011. "Un-“ESCRT”-ed Budding" Viruses 3, no. 1: 26-31. https://0-doi-org.brum.beds.ac.uk/10.3390/v3010026

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