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.
Highlights
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
Viruses 2011, 3 required for transport; reviewed in [8,9]) machinery is an active participant in this process came from identification of Tsg101, a component of ESCRT-1, as a binding partner of the budding determinant in the Gag polyprotein of HIV-1 [10,11,12]
M1 protein binds the ESCRT-1 factor Vps28 but the significance of this interaction remains to be determined since depletion of endogenous Vps28 has no detectable effect on influenza virus budding [19]
Summary
Rossman et al [1] describe how the inherent budding capability of its M2 protein allows influenza A virus to bypass recruitment of the cellular. Since nucleic acid and lipid do not have intrinsic affinity for each other, the encapsidation process requires proteins to serve as adaptors, as initiators of membrane deformation and as mediators of bud scission.
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