{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen WH"],"funding":["CCR NIH HHS","Intramural NIH HHS","NCRR NIH HHS","NCI NIH HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["2135-2148.e6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9815946"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["55(11)"],"pubmed_abstract":["Epstein-Barr virus (EBV) is nearly ubiquitous in adults. EBV causes infectious mononucleosis and is associated with B cell lymphomas, epithelial cell malignancies, and multiple sclerosis. The EBV gH/gL glycoprotein complex facilitates fusion of virus membrane with host cells and is a target of neutralizing antibodies. Here, we examined the sites of vulnerability for virus neutralization and fusion inhibition within EBV gH/gL. We developed a panel of human monoclonal antibodies (mAbs) that targeted five distinct antigenic sites on EBV gH/gL and prevented infection of epithelial and B cells. Structural analyses using X-ray crystallography and electron microscopy revealed multiple sites of vulnerability and defined the antigenic landscape of EBV gH/gL. One mAb provided near-complete protection against viremia and lymphoma in a humanized mouse EBV challenge model. Our findings provide structural and antigenic knowledge of the viral fusion machinery, yield a potential therapeutic antibody to prevent EBV disease, and emphasize gH/gL as a target for herpesvirus vaccines and therapeutics."],"journal":["Immunity"],"pubmed_title":["Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition."],"pmcid":["PMC9815946"],"funding_grant_id":["HHSN261200800001E","S10 RR028976","ZIA AI000978","HHSN261200800001C","P30 GM124165","S10 OD027000","S10 OD021527"],"pubmed_authors":["Peterson CE","Tsybovsky Y","Hostal A","Joyce MG","Board NL","Yang ES","Cohen JI","Pegu A","Fisher BE","Andrews SF","Choe M","Kim J","Kanekiyo M","Pittaluga S","McDermott AB","Bu W","Mascola JR","Gillespie RA","Chen WH","Wang Y","Stephens T"],"additional_accession":[]},"is_claimable":false,"name":"Epstein-Barr virus gH/gL has multiple sites of vulnerability for virus neutralization and fusion inhibition.","description":"Epstein-Barr virus (EBV) is nearly ubiquitous in adults. EBV causes infectious mononucleosis and is associated with B cell lymphomas, epithelial cell malignancies, and multiple sclerosis. The EBV gH/gL glycoprotein complex facilitates fusion of virus membrane with host cells and is a target of neutralizing antibodies. Here, we examined the sites of vulnerability for virus neutralization and fusion inhibition within EBV gH/gL. We developed a panel of human monoclonal antibodies (mAbs) that targeted five distinct antigenic sites on EBV gH/gL and prevented infection of epithelial and B cells. Structural analyses using X-ray crystallography and electron microscopy revealed multiple sites of vulnerability and defined the antigenic landscape of EBV gH/gL. One mAb provided near-complete protection against viremia and lymphoma in a humanized mouse EBV challenge model. Our findings provide structural and antigenic knowledge of the viral fusion machinery, yield a potential therapeutic antibody to prevent EBV disease, and emphasize gH/gL as a target for herpesvirus vaccines and therapeutics.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-28T02:06:28.225Z","creation":"2025-04-19T20:16:02.724Z"},"accession":"S-EPMC9815946","cross_references":{"pubmed":["36306784"],"doi":["10.1016/j.immuni.2022.10.003"]}}