title: New insights into the mechanism of virus-induced membrane fusion.
abstract: Infection by enveloped viruses requires fusion between the viral and cellular membranes, a process mediated by specific viral envelope glycoproteins. Information from studies with whole viruses, as well as protein dissection, has suggested that the fusion glycoprotein (F) from Paramyxoviridae, a family that includes major human pathogens, has two hydrophobic segments, termed fusion peptides. These peptides are directly responsible for the membrane fusion event. The recently determined three-dimensional structure of the pre-fusion conformation of the F protein supported these predictions and enabled the formulation of: (1) a detailed model for the initial interaction between F and the target membrane, (2) a new model for Paramyxovirus-induced membrane fusion that can be extended to other viral families, and (3) a novel strategy for developing better inhibitors of paramyxovirus infection.
authors.affiliation: Dept of Biological Chemistry, Weizmann Institute of Science, 76100, The Harold S. and Harriet B. Professorial Chair in Cancer Research., Rehovot, Israel.
authors.forename: Sergio G
authors.initials: SG
authors.lastname: Peisajovich
authors.forename: Yechiel
authors.initials: Y
authors.lastname: Shai
mesh_terms: D000595:Amino Acid Sequence; D008561:Membrane Fusion / Q000502:physiology*; D008954:Models, Biological; D008969:Molecular Sequence Data; D010252:Paramyxoviridae / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D014760:Viral Fusion Proteins / Q000737:chemistry / Q000502:physiology
chemical_list: D014760:Viral Fusion Proteins