title: Viral membrane fusion.
abstract: Infection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral 'fusion proteins' facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-triggered, large-scale conformational change in the fusion protein is coupled to apposition and merger of the two bilayers. We describe three examples--the influenza virus hemagglutinin, the flavivirus E protein and the vesicular stomatitis virus G protein--in some detail, to illustrate the ways in which different structures have evolved to implement this common mechanism. Fusion inhibitors can be effective antiviral agents.
authors.affiliation: Jack and Eileen Connors Structural Biology Laboratory, Harvard Medical School, Laboratory of Molecular Medicine, Children's Hospital Boston, Howard Hughes Medical Institute, 250 Longwood Avenue, Boston, MA 02115, USA. harrison@crystal.harvard.edu
authors.forename: Stephen C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D000818:Animals; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000378:metabolism; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000378:metabolism; D014775:Virus Activation; D053586:Virus Internalization
chemical_list: C028391:G protein, vesicular stomatitis virus; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins; C065696:glycoprotein E, Flavivirus