ArticleNature structural & molecular biology2018
Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB.
Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
66 citing papers in PubMed.
- The native conformational landscape and priming mechanism of herpes simplex virus glycoprotein B.Science advances · 2026Article
- Prefusion-specific glycoprotein B human antibodies protect against neonatal HSV-2 infection.bioRxiv : the preprint server for biology · 2026Article
- Engineering HSV-1 for oncolytic therapy: From molecular entry mechanisms to retargeting strategies.Genes & diseases · 2026Review
- Pre-assembled complexes and allosteric effects: parallels between eukaryotic phosphorylation cascades and membrane fusion during herpesviral entry.Journal of virology · 2026Review
- Isolation and characterization of broadly-neutralizing anti-HCMV-gB antibodies from human donors using a prefusion-stabilized HCMV gB variant.PLoS pathogens · 2026Article
- The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026Article
- Article
- Progress and prospects for herpesvirus vaccination using gB antigens.Frontiers in immunology · 2026Review
- Modulation of specific interactions within a viral fusion protein predicted from machine learning blocks membrane fusion.Nanoscale · 2025Article
- Article
- Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B.Nature microbiology · 2025Article
- Structures of vesicular stomatitis virus glycoprotein G alone and bound to a neutralizing antibody.PLoS pathogens · 2025Article
- Article
- Article
- Structure of the Kaposi's sarcoma-associated herpesvirus gB in post-fusion conformation.Journal of virology · 2025Article
- Review
- Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.Trends in biochemical sciences · 2024Review
- Allosteric mechanism of membrane fusion activation in a herpesvirus.bioRxiv : the preprint server for biology · 2024Article
- The Autonomous Fusion Activity of Human Cytomegalovirus Glycoprotein B Is Regulated by Its Carboxy-Terminal Domain.Viruses · 2024Article
- Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch.Nature communications · 2024Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
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. Our data suggest a model for how this dynamic, membrane-dependent 'clamp' controls the fusogenic refolding of gB.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.