ArticleJournal of virology2004
Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusion.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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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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
40 citing papers in PubMed, 47 citations in OpenAlex.
- Transgenic mouse-derived human monoclonal antibodies targeting EBV gp350 and gp42 provide basis for therapeutic development.Cell reports. Medicine · 2026Article
- 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
- Neutralizing antibodies against EBV gp42 show potentEmerging microbes & infections · 2023Article
- The structural basis of herpesvirus entry.Nature reviews. Microbiology · 2021Review
- Article
- 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
- 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
- Article
- gH/gL supercomplexes at early stages of herpesvirus entry.Current opinion in virology · 2016Review
- 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
- The conserved disulfide bond within domain II of Epstein-Barr virus gH has divergent roles in membrane fusion with epithelial cells and B cells.Journal of virology · 2014Article
- 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
- The large groove found in the gH/gL structure is an important functional domain for Epstein-Barr virus fusion.Journal of virology · 2013Article
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- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Epstein-Barr virus (EBV) is a human gammaherpesvirus associated with malignancies of both epithelial and lymphoid origin. Efficient infection of the latent host reservoir B lymphocytes involves the binding of glycoproteins gp350/220 for initial attachment, followed by the concerted action of gH, gL, gB, and gp42 for membrane fusion. The type II membrane protein gp42 is required for infection of B cells and assembles into a complex with gH and gL. The cellular host receptor for gp42, class II human leukocyte antigen (HLA), has been structurally verified by crystallization analyses of gp42 bound to HLA-DR1. Interestingly, the crystal structure revealed a hydrophobic pocket consisting of many aromatic and aliphatic residues from the predicted C-type lectin domain of gp42 that in other members of the C-type lectin family binds major histocompatibility complex class I or other diverse ligands. Although the hydrophobic pocket does not bind HLA class II, mutational analyses presented here indicate that this domain is essential for EBV-induced membrane fusion. In addition, mutational analysis of the region of gp42 contacting HLA class II in the gp42-HLA-DR1 cocrystal confirms that this region interacts with HLA class II and that this interaction is also important for EBV-induced membrane fusion.
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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.