ArticleProceedings of the National Academy of Sciences of the United States of America2009
Fusion of epithelial cells by Epstein-Barr virus proteins is triggered by binding of viral glycoproteins gHgL to integrins alphavbeta6 or alphavbeta8.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 147 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
147 citing papers in PubMed, 205 citations in OpenAlex.
- Review
- Epstein-Barr Virus-Mediated Apoptosis Evasion in Epithelial Malignancies: Molecular Mechanisms and Therapeutic Implications.Biology · 2026Review
- A Biomedical Researcher's Guide for Analyzing Short Tandem Repeat (STR) Genotypes of Human Cell Lines and in Vitro Tissue Samples Using Three Standard Authentication Algorithms.Current protocols · 2026Article
- Epstein-Barr virus receptors: classification, functional mechanisms, and pathogenic implications.Journal of virology · 2026Review
- Recent advances in Epstein-Barr virus vaccines development from mechanistic exploration to clinical translation.NPJ vaccines · 2026Review
- Structure and immunogenicity of an engineered soluble prefusion-stabilized EBV gB antigen.Nature communications · 2026Article
- Desmocollin 2 is a dominant entry receptor for Epstein-Barr virus infection of epithelial cells.Nature microbiology · 2025Article
- Article
- Design, Structure, and Immunogenicity of a Soluble Prefusion-stabilized EBV gB Antigen.bioRxiv : the preprint server for biology · 2025Article
- Review
- High IgG titers against EBV glycoprotein 42 correlate with lower risk of nasopharyngeal carcinoma.The Journal of clinical investigation · 2025Article
- Microbial oncogenesis within the gastric niche: how the gastric microbiota influencesFrontiers in microbiology · 2025Review
- The Functional Interaction Between Epstein-Barr Virus and MYC in the Pathogenesis of Burkitt Lymphoma.Cancers · 2024Review
- An In Silico Approach to Discover Efficient Natural Inhibitors to Tie Up Epstein-Barr Virus Infection.Pathogens (Basel, Switzerland) · 2024Article
- Potent human monoclonal antibodies targeting Epstein-Barr virus gp42 reveal vulnerable sites for virus infection.Cell reports. Medicine · 2024Article
- Review
- Helicobacter pylori and Epstein-Barr virus infection in cell polarity alterations.Folia microbiologica · 2024Review
- Virus-Induced Cell Fusion and Syncytia Formation.Results and problems in cell differentiation · 2024Article
- The Epstein-Barr Virus Glycoprotein BDLF2 Is Essential for Efficient Viral Spread in Stratified Epithelium.Journal of virology · 2023Article
- Viruses Binding to Host Receptors Interacts with Autophagy.International journal of molecular sciences · 2023Review
87 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Epstein-Barr virus (EBV) is a ubiquitous human herpesvirus that is causally implicated in the development of lymphoid and epithelial tumors. Entry of virus requires fusion of virus envelopes and cell membranes. Fusion with B lymphocytes requires virus glycoprotein gB and a 3-part complex of glycoproteins, gHgLgp42. It is triggered by interactions between glycoprotein 42 (gp42) and HLA class II. However, fusion with epithelial cells is impeded by gp42 and instead is triggered by interactions between an unknown epithelial protein and a 2-part complex of gHgL. We report here that gHgL binds with high affinity to epithelial cells and that affinity of binding is increased by 3 orders of magnitude in the presence of Mn(2+). Binding and infection can be reduced by fibronectin and vitronectin, by down-regulation of integrin alphav, or by a peptide corresponding to 13 aa of gH which include a KGDE motif. Fusion of cells expressing gB and gHgL can be blocked by vitronectin or triggered by addition of soluble truncated integrins alphavbeta6 and alphavbeta8. We conclude that the direct interaction between EBV gHgL and integrins alphavbeta6 and alphavbeta8 can provide the trigger for fusion of EBV with an epithelial cell.
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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.