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Viral fusion proteins mediate the merger of host and viral membranes during cell entry for all enveloped viruses. Baculovirus glycoprotein gp64 (gp64) is unusual in promoting entry into both insect and mammalian cells and is distinct from established class I and class II fusion proteins. We report the crystal structure of its postfusion form, which explains a number of gp64's biological properties including its cellular promiscuity, identifies the fusion peptides and shows it to be the third representative of a new class (III) of fusion proteins with unexpected structural homology with vesicular stomatitis virus G and herpes simplex virus type 1 gB proteins. We show that domains of class III proteins have counterparts in both class I and II proteins, suggesting that all these viral fusion machines are structurally more related than previously thought.

Original publication

DOI

10.1038/nsmb.1484

Type

Journal article

Journal

Nat Struct Mol Biol

Publication Date

10/2008

Volume

15

Pages

1024 - 1030

Keywords

Animals, Baculoviridae, Cell Line, Crystallography, X-Ray, Hydrogen-Ion Concentration, Membrane Fusion, Models, Molecular, Protein Structure, Quaternary, Protein Structure, Tertiary, Spodoptera, Structural Homology, Protein, Viral Fusion Proteins, Virus Internalization