ArticleStructure (London, England : 1993)2013
The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction.
Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Syncytium-forming HSV-1 in cancer gene therapy: From molecular mechanisms to clinical translation.Virulence · 2026Review
- Modulation of specific interactions within a viral fusion protein predicted from machine learning blocks membrane fusion.Nanoscale · 2025Article
- Structures of Epstein-Barr virus and Kaposi's sarcoma-associated herpesvirus virions reveal species-specific tegument and envelope features.Journal of virology · 2024Article
- Herpes Simplex Virus 1 Entry Glycoproteins Form Complexes before and during Membrane Fusion.mBio · 2022Article
- High-resolution in situ structure determination by cryo-electron tomography and subtomogram averaging using emClarity.Nature protocols · 2022Review
- DNA origami signposts for identifying proteins on cell membranes by electron cryotomography.Cell · 2021Article
- The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021Review
- Entry of Alphaherpesviruses.Current issues in molecular biology · 2021Review
- Stunning symmetries involved in the self-assembly of the HSV-1 capsid.The journal of the Korean Physical Society · 2021Review
- The prefusion structure of herpes simplex virus glycoprotein B.Science advances · 2020Article
- A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation.Nature communications · 2020Article
- HVEM signaling promotes protective antibody-dependent cellular cytotoxicity (ADCC) vaccine responses to herpes simplex viruses.Science immunology · 2020Article
- Herpes Simplex Virus Cell Entry Mechanisms: An Update.Frontiers in cellular and infection microbiology · 2020Review
- Advances in cryo-electron tomography and subtomogram averaging and classification.Current opinion in structural biology · 2019Review
- Structure-Function Dissection of Pseudorabies Virus Glycoprotein B Fusion Loops.Journal of virology · 2018Article
- Cryo-electron tomography: an ideal method to study membrane-associated proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Article
- Native structure of a retroviral envelope protein and its conformational change upon interaction with the target cell.Journal of structural biology · 2017Article
- Characterization of Vesicular Stomatitis Virus Pseudotypes Bearing Essential Entry Glycoproteins gB, gD, gH, and gL of Herpes Simplex Virus 1.Journal of virology · 2016Article
- The Microtubule Inhibitor Podofilox Inhibits an Early Entry Step of Human Cytomegalovirus.Viruses · 2016Article
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Authors and funding
11 authors.
Funding
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.
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