ArticleJournal of virology2003
Mutational analysis of the HLA class II interaction with Epstein-Barr virus glycoprotein 42.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Neutralizing antibodies against EBV gp42 show potentEmerging microbes & infections · 2023Article
- Epstein-Barr virus-acquired immunodeficiency in myalgic encephalomyelitis-Is it present in long COVID?Journal of translational medicine · 2023Review
- The impact of HLA polymorphism on herpesvirus infection and disease.Immunogenetics · 2023Review
- CD4+ Cytotoxic T Cells Involved in the Development of EBV-Associated Diseases.Pathogens (Basel, Switzerland) · 2022Review
- Epstein-Barr Virus and the Origin of Myalgic Encephalomyelitis or Chronic Fatigue Syndrome.Frontiers in immunology · 2021Review
- 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
- HLA-DQJCI insight · 2017Article
- Article
- Detailed study of the interaction between human herpesvirus 6B glycoprotein complex and its cellular receptor, human CD134.Journal of virology · 2014Article
- A soluble form of Epstein-Barr virus gH/gL inhibits EBV-induced membrane fusion and does not function in fusion.Virology · 2013Article
- 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
- Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Characteristics of Epstein-Barr virus envelope protein gp42.Virus genes · 2010Article
- Cleavage and secretion of Epstein-Barr virus glycoprotein 42 promote membrane fusion with B lymphocytes.Journal of virology · 2009Article
- Structure of Epstein-Barr virus glycoprotein 42 suggests a mechanism for triggering receptor-activated virus entry.Structure (London, England : 1993) · 2009Article
- Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis.Journal of virology · 2009Article
- Binding-site interactions between Epstein-Barr virus fusion proteins gp42 and gH/gL reveal a peptide that inhibits both epithelial and B-cell membrane fusion.Journal of virology · 2007Article
- Epstein-Barr virus gp42 is posttranslationally modified to produce soluble gp42 that mediates HLA class II immune evasion.Journal of virology · 2005Article
- Mutational analyses of Epstein-Barr virus glycoprotein 42 reveal functional domains not involved in receptor binding but required for membrane fusion.Journal of virology · 2004Article
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Authors and funding
5 authors.
Funding
Abstract
Entry of Epstein-Barr virus (EBV) into B lymphocytes requires the binding of viral glycoprotein 42 (gp42), a C-type lectin family member, to HLA class II. Recently, the structure of the gp42:HLA-DR1 complex was determined. In order to confirm the interaction as determined in the structural study and to identify other potential interactive residues, a mutational analysis of HLA class II was performed. A secreted form of gp42 (sgp42) reacted with a conformation-specific monoclonal antibody and blocked EBV infection. The binding of sgp42 and EBV entry to two sets of HLA class II mutants were tested. The first set of mutants were based on the known interaction of the C-type lectin Ly49A with HLA class I, and the second set of mutants were based on the identified interface in the gp42:HLA-DR1 complex. As expected, none of the mutants that would be predicted to interfere with the interaction of Ly49A with class I affected the interaction of gp42 with HLA class II, whereas mutants in amino acids identified in the gp42:HLA-DR1 structure inhibited sg42 binding to class II. In general, sgp42 binding correlated with efficient entry of EBV, as demonstrated by the necessity of glutamic acid 46 or arginine 72 in class II molecules. Furthermore, other HLA class II residues buried within the interface of gp42 and HLA class II when mutated had either no effect or a decrease in both binding and entry and implicate a region of class II important in stabilizing the interaction with gp42. These studies provide insight into the entry and fusion processes of the critical interaction between gp42 and HLA class II.
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