title: Poxvirus entry and membrane fusion.
abstract: The study of poxvirus entry and membrane fusion has been invigorated by new biochemical and microscopic findings that lead to the following conclusions: (1) the surface of the mature virion (MV), whether isolated from an infected cell or by disruption of the membrane wrapper of an extracellular virion, is comprised of a single lipid membrane embedded with non-glycosylated viral proteins; (2) the MV membrane fuses with the cell membrane, allowing the core to enter the cytoplasm and initiate gene expression; (3) fusion is mediated by a newly recognized group of viral protein components of the MV membrane, which are conserved in all members of the poxvirus family; (4) the latter MV entry/fusion proteins are required for cell to cell spread necessitating the disruption of the membrane wrapper of extracellular virions prior to fusion; and furthermore (5) the same group of MV entry/fusion proteins are required for virus-induced cell-cell fusion. Future research priorities include delineation of the roles of individual entry/fusion proteins and identification of cell receptors.
authors.affiliation: Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-0445, USA. bmoss@nih.gov
authors.forename: Bernard
authors.initials: B
authors.lastname: Moss
mesh_terms: D000818:Animals; D002459:Cell Fusion; D002462:Cell Membrane / Q000378:metabolism / Q000821:virology*; D015726:Giant Cells / Q000821:virology; D008561:Membrane Fusion; D011212:Poxviridae / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D014616:Vaccinia virus / Q000502:physiology; D014764:Viral Proteins / Q000502:physiology; D014771:Virion / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D014779:Virus Replication
chemical_list: D014764:Viral Proteins