Structural Biology

Herpes virus opens up

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Science  15 Apr 2016:
Vol. 352, Issue 6283, pp. 305-306
DOI: 10.1126/science.352.6283.305-c

Two forms of glycoprotein B facilitate interface of herpes simplex virus 1 with host cells.

PHOTO: ZEEV-BEN-MORDEHAI ET AL., PNAS (2016) © 2016 NATIONAL ACADEMY OF SCIENCES

Herpes simplex virus 1 (HSV-1), the cause of cold sores, is an enveloped virus that uses glycoprotein B (gB) to fuse with host cells. Zeev-Ben-Mordehai et al. used electron cryotomography to determine the structure of gB in a native membrane. They found two conformations: One, the known trimeric postfusion conformation, has fusion loops close together and proximal to the membrane. The other is a more compact trimer with fusion loops distal to the membrane and splayed apart. The new conformation explains antibody and mutagenesis data that could not be rationalized on the basis of postfusion structure. It is likely a prefusion or intermediate conformation that may be a target for antivirals.

Proc. Natl. Acad. Sci. U.S.A. 10.1073/PNAS.1523234113 (2016).

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