title: Evolutionary conservation of the membrane fusion machine.
abstract: Recent structural studies of proteins mediating membrane fusion reveal intriguing similarities between diverse viral and mammalian systems. Particularly striking is the close similarity between the transmembrane envelope glycoproteins from the retrovirus HTLV-1 and the filovirus Ebola. These similarities suggest similar mechanisms of membrane fusion. The model that fits most currently available data suggests fusion activation in viral systems is driven by a symmetrical conformational change triggered by an activation event such as receptor binding or a pH change. The mammalian vesicle fusion mediated by the SNARE protein complex most likely occurs by a similar mechanism but without symmetry constraints.
authors.affiliation: St. Vincent's Institute of Medical Research, Fitzroy, Victoria, Australia.
authors.forename: P
authors.initials: P
authors.lastname: Poumbourios
authors.forename: R J
authors.initials: RJ
authors.lastname: Center
authors.forename: K A
authors.initials: KA
authors.lastname: Wilson
authors.forename: B E
authors.initials: BE
authors.lastname: Kemp
authors.forename: B
authors.initials: B
authors.lastname: Kobe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D029043:Ebolavirus / Q000235:genetics / Q000502:physiology; D019143:Evolution, Molecular; D015368:Human T-lymphotropic virus 1 / Q000235:genetics / Q000502:physiology; D006801:Humans; D008561:Membrane Fusion / Q000235:genetics / Q000502:physiology*; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D014760:Viral Fusion Proteins / Q000235:genetics / Q000502:physiology
chemical_list: D014760:Viral Fusion Proteins