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| Title | Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 113, Issue 15, Page 4176-4181, Year 2016 |
| Publish date | Apr 12, 2016 |
 Authors | Tzviya Zeev-Ben-Mordehai / Daven Vasishtan / Anna Hernández Durán / Benjamin Vollmer / Paul White / Arun Prasad Pandurangan / C Alistair Siebert / Maya Topf / Kay Grünewald /  |
| PubMed Abstract | Many viruses are enveloped by a lipid bilayer acquired during assembly, which is typically studded with one or two types of glycoproteins. These viral surface proteins act as the primary interface ...Many viruses are enveloped by a lipid bilayer acquired during assembly, which is typically studded with one or two types of glycoproteins. These viral surface proteins act as the primary interface between the virus and the host. Entry of enveloped viruses relies on specialized fusogen proteins to help merge the virus membrane with the host membrane. In the multicomponent herpesvirus fusion machinery, glycoprotein B (gB) acts as this fusogen. Although the structure of the gB ectodomain postfusion conformation has been determined, any other conformations (e.g., prefusion, intermediate conformations) have so far remained elusive, thus restricting efforts to develop antiviral treatments and prophylactic vaccines. Here, we have characterized the full-length herpes simplex virus 1 gB in a native membrane by displaying it on cell-derived vesicles and using electron cryotomography. Alongside the known postfusion conformation, a novel one was identified. Its structure, in the context of the membrane, was determined by subvolume averaging and found to be trimeric like the postfusion conformation, but appeared more condensed. Hierarchical constrained density-fitting of domains unexpectedly revealed the fusion loops in this conformation to be apart and pointing away from the anchoring membrane. This vital observation is a substantial step forward in understanding the complex herpesvirus fusion mechanism, and opens up new opportunities for more targeted intervention of herpesvirus entry. |
 External links | Proc Natl Acad Sci U S A / PubMed:27035968 / PubMed Central |
| Methods | EM (subtomogram averaging) |
| Resolution | 23.0 Å |
| Structure data |  EMDB-3362: |
| Source |
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Human herpesvirus 1 (Herpes simplex virus type 1)