ArticlemBio2012
The KGD motif of Epstein-Barr virus gH/gL is bifunctional, orchestrating infection of B cells and epithelial cells.
Article in mBio, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
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Who cites it
36 citing papers in PubMed, 52 citations in OpenAlex.
- Molecular mimicry of host short linear motif-mediated interactions utilised by viruses for entry.Molecular biology reports · 2023Review
- New insight into Epstein-Barr virus infection using models of stratified epithelium.PLoS pathogens · 2023Article
- Clinical and experimental bacteriophage studies: Recommendations for possible approaches for standing against SARS-CoV-2.Microbial pathogenesis · 2022Review
- Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses.Nature communications · 2020Article
- Phages in the fight against COVID-19?Future microbiology · 2020Article
- Epithelial cell infection by Epstein-Barr virus.FEMS microbiology reviews · 2019Article
- Cryo-EM Structures of Eastern Equine Encephalitis Virus Reveal Mechanisms of Virus Disassembly and Antibody Neutralization.Cell reports · 2018Article
- An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus.Immunity · 2018Article
- The Immunomodulatory Capacity of an Epstein-Barr Virus Abortive Lytic Cycle: Potential Contribution to Viral Tumorigenesis.Cancers · 2018Review
- Ephrin receptor A2 is a functional entry receptor for Epstein-Barr virus.Nature microbiology · 2018Article
- Perspectives of Phage-Eukaryotic Cell Interactions to Control Epstein-Barr Virus Infections.Frontiers in microbiology · 2018Article
- A comparative review of viral entry and attachment during large and giant dsDNA virus infections.Archives of virology · 2017Review
- Epstein-Barr Virus Fusion with Epithelial Cells Triggered by gB Is Restricted by a gL Glycosylation Site.Journal of virology · 2017Article
- Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.Nature communications · 2016Article
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- Structural and Mechanistic Insights into the Tropism of Epstein-Barr Virus.Molecules and cells · 2016Review
- Comparative Mutagenesis of Pseudorabies Virus and Epstein-Barr Virus gH Identifies a Structural Determinant within Domain III of gH Required for Surface Expression and Entry Function.Journal of virology · 2015Article
- Scanning Mutagenesis of Human Cytomegalovirus Glycoprotein gH/gL.Journal of virology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Epstein-Barr virus (EBV), a member of the herpesvirus family, is the causative agent of common human infections and specific malignancies. EBV entry into target cells, including B cells and epithelial cells, requires the interaction of multiple virus-encoded glycoproteins. Glycoproteins H and L (gH/gL) cooperate with glycoprotein B (gB) to mediate fusion of the viral envelope with target cell membranes. Both the gH/gL complex and gB are required for fusion, whereas glycoprotein 42 (gp42) acts as a tropism switch and is required for B cell infection and inhibits epithelial cell infection. Our previous studies identified a prominent KGD motif located on the surface of gH/gL. In the current study, we found that this motif serves as a bifunctional domain on the surface of gH/gL that directs EBV fusion of B cells and epithelial cells. Mutation of the KGD motif to AAA decreased fusion with both epithelial and B cells and reduced the binding of gH/gL to epithelial cells and to gp42. We also demonstrate that deletion of amino acids 62 to 66 of gp42 selectively reduces binding to wild-type gH/gL, but not the KGD mutant, suggesting that the KGD motif of gH/gL interacts with the N-terminal amino acids 62 to 66 of gp42.
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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.