ArticleProceedings of the National Academy of Sciences of the United States of America2024
Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like conformation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Article
- CAR T cell therapy beyond cancer: current status, challenges and future prospects.Signal transduction and targeted therapy · 2026Review
- The native conformational landscape and priming mechanism of herpes simplex virus glycoprotein B.Science advances · 2026Article
- Mapping the monoclonal antibody landscape of human cytomegalovirus.Journal of virology · 2026Review
- Recent advances in Epstein-Barr virus vaccines development from mechanistic exploration to clinical translation.NPJ vaccines · 2026Review
- Article
- Prefusion-specific glycoprotein B human antibodies protect against neonatal HSV-2 infection.bioRxiv : the preprint server for biology · 2026Article
- Isolation and characterization of broadly-neutralizing anti-HCMV-gB antibodies from human donors using a prefusion-stabilized HCMV gB variant.PLoS pathogens · 2026Article
- Article
- Structure and immunogenicity of an engineered soluble prefusion-stabilized EBV gB antigen.Nature communications · 2026Article
- Progress and prospects for herpesvirus vaccination using gB antigens.Frontiers in immunology · 2026Review
- Selective decoupling of IgG1 binding to viral Fc receptors restores antibody-mediated NK cell activation against HCMV.Cell reports · 2025Article
- Article
- Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B.Nature microbiology · 2025Article
- Article
- Replication-deficient whole-virus vaccines against cytomegalovirus induce protective immunity in a guinea pig congenital infection model.Journal of virology · 2025Article
- Human herpesvirus 6B glycoprotein B postfusion structure, vulnerability mapping, and receptor recognition.PLoS pathogens · 2025Article
- Structure and Antigenicity of Kaposi's Sarcoma-Associated Herpesvirus Glycoprotein B.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A human cytomegalovirus prefusion-like glycoprotein B subunit vaccine elicits humoral immunity similar to that of postfusion gB in mice.Journal of virology · 2025Article
- Design, Structure, and Immunogenicity of a Soluble Prefusion-stabilized EBV gB Antigen.bioRxiv : the preprint server for biology · 2025Article
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19 authors.
Funding
Abstract
Human cytomegalovirus (HCMV) glycoprotein B (gB) is a class III membrane fusion protein required for viral entry. HCMV vaccine candidates containing gB have demonstrated moderate clinical efficacy, but no HCMV vaccine has been approved. Here, we used structure-based design to identify and characterize amino acid substitutions that stabilize gB in its metastable prefusion conformation. One variant containing two engineered interprotomer disulfide bonds and two cavity-filling substitutions (gB-C7), displayed increased expression and thermostability. A 2.8 Å resolution cryoelectron microscopy structure shows that gB-C7 adopts a prefusion-like conformation, revealing additional structural elements at the membrane-distal apex. Unlike previous observations for several class I viral fusion proteins, mice immunized with postfusion or prefusion-stabilized forms of soluble gB protein displayed similar neutralizing antibody titers, here specifically against an HCMV laboratory strain on fibroblasts. Collectively, these results identify initial strategies to stabilize class III viral fusion proteins and provide tools to probe gB-directed antibody responses.
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