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The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78371

Maurer,  Ulrike E.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78147

Huiskonen,  Juha T.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78038

Grünewald,  Kay
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Maurer, U. E., Zeev-Ben-Mordehai, T., Pandurangan, A. P., Cairns, T. M., Hannah, B. P., Whitbeck, J. C., et al. (2013). The Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein Interaction. STRUCTURE, 21(8), 1396-1405. doi:10.1016/j.str.2013.05.018.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-4EA4-F
Abstract
Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion.