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Herpesvirus gB: A Finely Tuned Fusion Machine

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA 02111, USA
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Author to whom correspondence should be addressed.
Academic Editor: Andrew Ward
Viruses 2015, 7(12), 6552-6569; https://doi.org/10.3390/v7122957
Received: 16 October 2015 / Revised: 15 November 2015 / Accepted: 27 November 2015 / Published: 11 December 2015
(This article belongs to the Special Issue Viral Glycoprotein Structure)
Enveloped viruses employ a class of proteins known as fusogens to orchestrate the merger of their surrounding envelope and a target cell membrane. Most fusogens accomplish this task alone, by binding cellular receptors and subsequently catalyzing the membrane fusion process. Surprisingly, in herpesviruses, these functions are distributed among multiple proteins: the conserved fusogen gB, the conserved gH/gL heterodimer of poorly defined function, and various non-conserved receptor-binding proteins. We summarize what is currently known about gB from two closely related herpesviruses, HSV-1 and HSV-2, with emphasis on the structure of the largely uncharted membrane interacting regions of this fusogen. We propose that the unusual mechanism of herpesvirus fusion could be linked to the unique architecture of gB. View Full-Text
Keywords: herpesviruses; cell entry; membrane fusion; glycoproteins; virions; X-ray crystallography; electron microscopy; electron tomography herpesviruses; cell entry; membrane fusion; glycoproteins; virions; X-ray crystallography; electron microscopy; electron tomography
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Cooper, R.S.; Heldwein, E.E. Herpesvirus gB: A Finely Tuned Fusion Machine. Viruses 2015, 7, 6552-6569.

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