ArticleProceedings of the National Academy of Sciences of the United States of America2017
Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed, 38 citations in OpenAlex.
- Identification of Two Competition-Defined Neutralizing Antibody Groups Targeting the HHV-6B gH/gL/gQ1/gQ2 Complex Independent of CD134 Binding.Microbiology and immunology · 2026Article
- A potent human neutralizing antibody targeting the receptor-binding site in the glycoprotein gp350 of Epstein-Barr virus.Science China. Life sciences · 2026Article
- Article
- GB and gH/gL fusion machinery: a promising target for vaccines to prevent Epstein-Barr virus infection.Archives of virology · 2024Review
- A gH/gL-encoding replicon vaccine elicits neutralizing antibodies that protect humanized mice against EBV challenge.NPJ vaccines · 2024Article
- Potent human monoclonal antibodies targeting Epstein-Barr virus gp42 reveal vulnerable sites for virus infection.Cell reports. Medicine · 2024Article
- Epstein-Barr virus gp42 antibodies reveal sites of vulnerability for receptor binding and fusion to B cells.Immunity · 2024Article
- Non-overlapping epitopes on the gHgL-gp42 complex for the rational design of a triple-antibody cocktail against EBV infection.Cell reports. Medicine · 2023Article
- Urgency and necessity of Epstein-Barr virus prophylactic vaccines.NPJ vaccines · 2022Review
- A high-throughput neutralizing assay for antibodies and sera evaluation against Epstein-Barr virus.Virology journal · 2022Article
- Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition.Immunity · 2022Article
- Review
- Protective anti-gB neutralizing antibodies targeting two vulnerable sites for EBV-cell membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Immunization with a self-assembling nanoparticle vaccine displaying EBV gH/gL protects humanized mice against lethal viral challenge.Cell reports. Medicine · 2022Article
- A Neutralizing Antibody Targeting gH Provides Potent Protection against EBV ChallengeJournal of virology · 2022Article
- Review
- A potent and protective human neutralizing antibody targeting a novel vulnerable site of Epstein-Barr virus.Nature communications · 2021Article
- The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021Review
- Main Targets of Interest for the Development of a Prophylactic or Therapeutic Epstein-Barr Virus Vaccine.Frontiers in microbiology · 2021Review
- Structural basis for the interaction of human herpesvirus 6B tetrameric glycoprotein complex with the cellular receptor, human CD134.PLoS pathogens · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Herpesvirus entry into cells requires the coordinated action of multiple virus envelope glycoproteins, including gH, gL, and gB. For EBV, the gp42 protein assembles into complexes with gHgL heterodimers and binds HLA class II to activate gB-mediated membrane fusion with B cells. EBV tropism is dictated by gp42 levels in the virion, as it inhibits entry into epithelial cells while promoting entry into B cells. The gHgL and gB proteins are targets of neutralizing antibodies and potential candidates for subunit vaccine development, but our understanding of their neutralizing epitopes and the mechanisms of inhibition remain relatively unexplored. Here we studied the structures and mechanisms of two anti-gHgL antibodies, CL40 and CL59, that block membrane fusion with both B cells and epithelial cells. We determined the structures of the CL40 and CL59 complexes with gHgL using X-ray crystallography and EM to identify their epitope locations. CL59 binds to the C-terminal domain IV of gH, while CL40 binds to a site occupied by the gp42 receptor binding domain. CL40 binding to gHgL/gp42 complexes is not blocked by gp42 and does not interfere with gp42 binding to HLA class II, indicating that its ability to block membrane fusion with B cells represents a defect in gB activation. These data indicate that anti-gHgL neutralizing antibodies can block gHgL-mediated activation of gB through different surface epitopes and mechanisms.
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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.