title: Un-“ESCRT”-ed budding.
abstract: In their recent publication, Rossman et al. 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 and other laboratories 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. Understanding how intrinsic properties of these influenza virus proteins permit ESCRT-independent budding expands our understanding of the budding process itself.
authors.affiliation: Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10128, USA. mark.yondola@mssm.edu
authors.forename: Mark
authors.initials: M
authors.lastname: Yondola
authors.forename: Carol
authors.initials: C
authors.lastname: Carter
mesh_terms: D002462:Cell Membrane / Q000378:metabolism; D056827:Endosomal Sorting Complexes Required for Transport / Q000378:metabolism*; D006388:Hemagglutinins / Q000378:metabolism*; D009980:Influenza A virus / Q000378:metabolism*; D009439:Neuraminidase / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000378:metabolism*; D057074:Virus Release / Q000502:physiology*; D000086082:Viroporin Proteins
chemical_list: D056827:Endosomal Sorting Complexes Required for Transport; D006388:Hemagglutinins; D009439:Neuraminidase; D014763:Viral Matrix Proteins; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins