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The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines

Kadlec, J., Loureiro, S., Abrescia, N. G. A., Stuart, D. I. and Jones, I. M. (2008) The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nature Structural & Molecular Biology, 15 (10). pp. 1024-1030. ISSN 1545-9985

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To link to this article DOI: 10.1038/nsmb.1484

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences
ID Code:9830
Uncontrolled Keywords:VIRUS MEMBRANE-FUSION, HELICAL COILED COILS, CRYSTAL-STRUCTURE, GLYCOPROTEIN-B, TRANSGENE EXPRESSION, ENVELOPE PROTEIN, DIFFRACTION, DATA, FORM, PH, CELLS

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