ArticleJournal of virology2009
Cleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 39 citations in OpenAlex.
- An In Silico Approach to Discover Efficient Natural Inhibitors to Tie Up Epstein-Barr Virus Infection.Pathogens (Basel, Switzerland) · 2024Article
- Neutralizing antibodies against EBV gp42 show potentEmerging microbes & infections · 2023Article
- Identification of presented SARS-CoV-2 HLA class I and HLA class II peptides using HLA peptidomics.Cell reports · 2021Article
- The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021Review
- Epithelial cell infection by Epstein-Barr virus.FEMS microbiology reviews · 2019Article
- Epstein-Barr Virus and the Human Leukocyte Antigen Complex.Current clinical microbiology reports · 2019Article
- Electrofusion of single cells in picoliter droplets.Scientific reports · 2018Article
- Human MHC-II with Shared Epitope Motifs Are Optimal Epstein-Barr Virus Glycoprotein 42 Ligands-Relation to Rheumatoid Arthritis.International journal of molecular sciences · 2018Review
- Article
- Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus.The Journal of biological chemistry · 2016Article
- Article
- Epstein-Barr virus infection mechanisms.Chinese journal of cancer · 2014Review
- 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
- Assembly and architecture of the EBV B cell entry triggering complex.PLoS pathogens · 2014Article
- Epstein-Barr virus transcytosis through polarized oral epithelial cells.Journal of virology · 2013Article
- A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Virology · 2013Article
- Review
- Article
- Investigation of the function of the putative self-association site of Epstein-Barr virus (EBV) glycoprotein 42 (gp42).Virology · 2011Article
- Fusing structure and function: a structural view of the herpesvirus entry machinery.Nature reviews. Microbiology · 2011Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Epstein-Barr virus (EBV) membrane glycoprotein 42 (gp42) is required for viral entry into B lymphocytes through binding to human leukocyte antigen (HLA) class II on the B-cell surface. EBV gp42 plays multiple roles during infection, including acting as a coreceptor for viral entry into B cells, binding to EBV glycoprotein H (gH) and gL during the process of membrane fusion, and blocking T-cell recognition of HLA class II-peptide complexes through steric hindrance. EBV gp42 occurs in two forms in infected cells, a full-length membrane-bound form and a soluble form generated by proteolytic cleavage that is secreted from infected cells due to loss of the N-terminal transmembrane domain. Both the full-length and the secreted gp42 forms bind to gH/gL and HLA class II, and the functional significance of gp42 cleavage is currently unclear. We found that in a virus-free cell-cell fusion assay, enhanced secretion of gp42 promoted fusion with B lymphocytes, and mutation of the site of gp42 cleavage inhibited membrane fusion activity. The site of gp42 cleavage was found to be physically distinct from the residues of gp42 necessary for binding to gH/gL. These results suggest that cleavage and secretion of gp42 are necessary for the process of membrane fusion with B lymphocytes, providing the first indicated functional difference between full-length and cleaved, secreted gp42.
Indexed as
Identifiers
What OpenQuestion holds
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.