ArticleProceedings of the National Academy of Sciences of the United States of America2004
Cell-surface expression of a mutated Epstein-Barr virus glycoprotein B allows fusion independent of other viral proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
What it found
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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.
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Who cites it
56 citing papers in PubMed.
- Structure and immunogenicity of an engineered soluble prefusion-stabilized EBV gB antigen.Nature communications · 2026Article
- Article
- Article
- Design, Structure, and Immunogenicity of a Soluble Prefusion-stabilized EBV gB Antigen.bioRxiv : the preprint server for biology · 2025Article
- Epstein-Barr virus gp42 antibodies reveal sites of vulnerability for receptor binding and fusion to B cells.Immunity · 2024Article
- Epstein-Barr Virus Envelope Glycoprotein gp110 Inhibits IKKi-Mediated Activation of NF-κB and Promotes the Degradation of β-Catenin.Microbiology spectrum · 2023Article
- Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition.Immunity · 2022Article
- Herpes Simplex Virus 1 Entry Glycoproteins Form Complexes before and during Membrane Fusion.mBio · 2022Article
- Article
- Epstein-Barr Virus gH/gL and Kaposi's Sarcoma-Associated Herpesvirus gH/gL Bind to Different Sites on EphA2 To Trigger Fusion.Journal of virology · 2020Article
- Epithelial cell infection by Epstein-Barr virus.FEMS microbiology reviews · 2019Article
- Article
- Ephrin Receptor A4 is a New Kaposi's Sarcoma-Associated Herpesvirus Virus Entry Receptor.mBio · 2019Article
- Ovine Herpesvirus 2 Glycoproteins B, H, and L Are Sufficient for, and Viral Glycoprotein Ov8 Can Enhance, Cell-Cell Membrane Fusion.Journal of virology · 2017Article
- The β-Lactamase Assay: Harnessing a FRET Biosensor to Analyse Viral Fusion Mechanisms.Sensors (Basel, Switzerland) · 2016Review
- Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.Journal of virology · 2015Article
- Neuropilin 1 is an entry factor that promotes EBV infection of nasopharyngeal epithelial cells.Nature communications · 2015Article
- The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Journal of virology · 2014Article
- Epstein-Barr virus transcytosis through polarized oral epithelial cells.Journal of virology · 2013Article
- Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Epstein-Barr virus (EBV) infects human B lymphocytes and epithelial cells. We have compared the requirements for EBV glycoprotein-induced cell fusion between Chinese hamster ovary effecter cells and human B lymphoblasts or epithelial cells by using a virus-free cell fusion assay. EBV-encoded gB, gH, gL, and gp42 glycoproteins were required for efficient B cell fusion, whereas EBV gB, gH, and gL glycoproteins were required for Chinese hamster ovary effecter cell fusion with epithelial cell lines (AGS and SCC68) or the human embryonic kidney cell line 293-P. Fusion with human embryonic kidney 293-P cells was greater than fusion observed with B cells, indicative of an important role for cell contact. An antibody directed against the gH and gL complex inhibited epithelial cell fusion. Increased surface expression of gB alone as a result of truncations or point mutants in the carboxyl-terminal tail allowed gB-mediated fusion with epithelial cells, albeit at a lower level than with coexpression of gB, gH, and gL. Overall, gB appears to be the critical component for EBV glycoprotein-mediated cell fusion.
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