Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB

Cooper, Rebecca S.; Georgieva, Elka R.; Borbat, Peter P.; Freed, Jack H.; Heldwein, Ekaterina E.

doi:10.1038/s41594-018-0060-6

Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB

Journal Article · Fri May 04 00:00:00 EDT 2018 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/s41594-018-0060-6· OSTI ID:1437476

Cooper, Rebecca S. ^[1]; Georgieva, Elka R. ^[2]; Borbat, Peter P. ^[2]; Freed, Jack H. ^[2]; ^[1]

Tufts Univ. School of Medicine, Boston, MA (United States)
Cornell Univ., Ithaca, NY (United States)

Viral fusogens merge viral and cell membranes during cell penetration. Their ectodomains drive fusion by undergoing large-scale refolding, but little is known about the functionally important regions located within or near the membrane. Here we report the crystal structure of full-length glycoprotein B (gB), the fusogen from herpes simplex virus, complemented by electron spin resonance measurements. The membrane-proximal (MPR), transmembrane (TMD), and cytoplasmic (CTD) domains form a uniquely folded trimeric pedestal beneath the ectodomain, which balances dynamic flexibility with extensive, stabilizing membrane interactions. The postfusion conformation of the ectodomain suggests that the CTD likewise adopted the postfusion form. However, hyperfusogenic mutations, which destabilize the prefusion state of gB, target key interfaces and structural motifs that reinforce the observed CTD structure. Thus, a similar CTD structure must stabilize gB in its prefusion state. In conclusion, our data suggest a model for how this dynamic, membrane-dependent ‘clamp’ controls the fusogenic refolding of gB.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: Burroughs Wellcome Fund; NIH; NIH Ruth L. Kirschstein NRSA postdoctoral fellowship; NIH-ORIP HEI; USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Scientific User Facilities Division

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1437476

Journal Information:: Nature Structural & Molecular Biology, Journal Name: Nature Structural & Molecular Biology Journal Issue: 5 Vol. 25; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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