{"doi":"10.1101/2024.06.21.600001","title":"A broadly-neutralizing antibody against\n                  <i>Ebolavirus</i>\n                  glycoprotein that potentiates the breadth and neutralization potency of other antibodies","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>\n                  Ebolavirus disease (EVD) is caused by multiple species of\n                  <jats:italic>Ebolavirus</jats:italic>\n                  . Monoclonal antibodies (mAbs) against the virus glycoprotein (GP) are the only class of therapeutic approved for treatment of EVD caused by\n                  <jats:italic>Zaire ebolavirus</jats:italic>\n                  (EBOV). Therefore, mAbs targeting multiple\n                  <jats:italic>Ebolavirus</jats:italic>\n                  species may represent the next generation of EVD therapeutics. Broadly reactive anti-GP mAbs were produced; among these, mAbs 11886 and 11883 were broadly neutralizing\n                  <jats:italic>in vitro</jats:italic>\n                  . A 3.0 Å cryo-electron microscopy structure of EBOV GP bound to both mAbs shows that 11886 binds a novel epitope bridging the glycan cap (GC), 3\n                  <jats:sub>10</jats:sub>\n                  pocket and GP2 N-terminus, whereas 11883 binds the receptor binding region (RBR) and GC.\n                  <jats:italic>In vitro</jats:italic>\n                  , 11886 synergized with a range of mAbs with epitope specificities spanning the RBR/GC, including 11883. Notably, 11886 increased the breadth of neutralization by partner mAbs against different\n                  <jats:italic>Ebolavirus</jats:italic>\n                  species. These data provide a strategic route to design improved mAb-based next-generation EVD therapeutics.\n                </jats:p>","journal":null,"year":null,"id":626047,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":551195,"name":"Vamseedhar Rayaprolu","orcid":null,"position":1,"is_corresponding":false},{"id":461107,"name":"Pramila Rijal","orcid":"0000-0002-9214-9851","position":2,"is_corresponding":false},{"id":1619320,"name":"Victoria O’Dowd","orcid":null,"position":3,"is_corresponding":false},{"id":997457,"name":"Amar Parvate","orcid":"0000-0001-9282-5015","position":4,"is_corresponding":false},{"id":711287,"name":"Heather Callaway","orcid":"0000-0003-4003-3854","position":5,"is_corresponding":false},{"id":619655,"name":"Chitra Hariharan","orcid":null,"position":6,"is_corresponding":false},{"id":1619321,"name":"Dipti Parekh","orcid":null,"position":7,"is_corresponding":false},{"id":283935,"name":"Sean Hui","orcid":"0000-0002-9870-6823","position":8,"is_corresponding":false},{"id":618417,"name":"Kelly Shaffer","orcid":"0000-0002-6212-1428","position":9,"is_corresponding":false},{"id":618414,"name":"Ruben Diaz Avalos","orcid":"0000-0003-3209-7153","position":10,"is_corresponding":false},{"id":1619322,"name":"Kathryn Hastie","orcid":null,"position":11,"is_corresponding":false},{"id":555229,"name":"Lisa Schimanski","orcid":null,"position":12,"is_corresponding":false},{"id":1059411,"name":"Helena Müller-Kräuter","orcid":"0009-0009-4134-1729","position":13,"is_corresponding":false},{"id":1059412,"name":"Thomas Strecker","orcid":"0000-0002-7857-937X","position":14,"is_corresponding":false},{"id":883140,"name":"Ariane Balaram","orcid":"0009-0006-2677-4567","position":15,"is_corresponding":false},{"id":107104,"name":"Peter Halfmann","orcid":"0000-0002-1648-1625","position":16,"is_corresponding":false},{"id":104945,"name":"Erica Ollmann Saphire","orcid":"0000-0002-1206-7451","position":17,"is_corresponding":false},{"id":1619323,"name":"Daniel J. Lightwood","orcid":null,"position":18,"is_corresponding":false},{"id":1619324,"name":"Alain R. Townsend","orcid":null,"position":19,"is_corresponding":false},{"id":251520,"name":"Simon J. Draper","orcid":"0000-0002-9415-1357","position":20,"is_corresponding":false},{"id":974843,"name":"Francesca R. Donnellan","orcid":"0000-0002-4723-3560","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A broadly-neutralizing antibody against\n                  <i>Ebolavirus</i>\n                  glycoprotein that potentiates the breadth and neutralization potency of other antibodies","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>\n                  Ebolavirus disease (EVD) is caused by multiple species of\n                  <jats:italic>Ebolavirus</jats:italic>\n                  . Monoclonal antibodies (mAbs) against the virus glycoprotein (GP) are the only class of therapeutic approved for treatment of EVD caused by\n                  <jats:italic>Zaire ebolavirus</jats:italic>\n                  (EBOV). Therefore, mAbs targeting multiple\n                  <jats:italic>Ebolavirus</jats:italic>\n                  species may represent the next generation of EVD therapeutics. Broadly reactive anti-GP mAbs were produced; among these, mAbs 11886 and 11883 were broadly neutralizing\n                  <jats:italic>in vitro</jats:italic>\n                  . A 3.0 Å cryo-electron microscopy structure of EBOV GP bound to both mAbs shows that 11886 binds a novel epitope bridging the glycan cap (GC), 3\n                  <jats:sub>10</jats:sub>\n                  pocket and GP2 N-terminus, whereas 11883 binds the receptor binding region (RBR) and GC.\n                  <jats:italic>In vitro</jats:italic>\n                  , 11886 synergized with a range of mAbs with epitope specificities spanning the RBR/GC, including 11883. Notably, 11886 increased the breadth of neutralization by partner mAbs against different\n                  <jats:italic>Ebolavirus</jats:italic>\n                  species. These data provide a strategic route to design improved mAb-based next-generation EVD therapeutics.\n                </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"38979279","pmcid":null,"openalex_id":"https://openalex.org/W4399993578","authors":[],"funders":[{"funder_name":"Wellcome Trust","grant_id":"106917/Z/15/Z","title":null},{"funder_name":"UK Research and Innovation","grant_id":"MR/N01796X/1","title":"Production of New and Improved Therapeutic Human Monoclonal Antibodies for Ebola"},{"funder_name":"National Institutes of Health","grant_id":"5U19AI109762-04","title":"Consortium for Immunotherapeutics Against Viral Hemorrhagic Fevers"},{"funder_name":"Wellcome Trust","grant_id":"106917","title":"Harnessing Human Antibodies to Deliver Effective Immunoprophylaxis against Difficult Disease Targets."},{"funder_name":"NIAID NIH HHS","grant_id":"U19 AI109762","title":null},{"funder_name":"Wellcome Trust","grant_id":"","title":null}],"total_grants":6,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"green","license":"cc-by","oa_locations":[{"url":"https://www.biorxiv.org/content/biorxiv/early/2024/06/25/2024.06.21.600001.full.pdf","host_type":"repository"},{"url":"https://www.biorxiv.org/content/biorxiv/early/2024/06/25/2024.06.21.600001.full.pdf","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.1101/2024.06.21.600001","host_type":"publisher"},{"url":"http://dx.doi.org/10.1101/2024.06.21.600001","host_type":"repository"},{"url":"https://pubmed.ncbi.nlm.nih.gov/38979279","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/11230233","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC11230233/pdf/nihpp-2024.06.21.600001v1.pdf","host_type":"repository"},{"url":"https://europepmc.org/article/PPR/PPR872401","host_type":"Europe_PMC"},{"url":"https://europepmc.org/api/fulltextRepo?pprId=PPR872401&type=FILE&fileName=EMS197112-pdf.pdf&mimeType=application/pdf","host_type":"Europe_PMC"},{"url":"https://doi.org/10.1101/2024.06.21.600001","host_type":""}],"fields_of_study":["Viral Infections and Outbreaks Research","Viral gastroenteritis research and epidemiology","Hepatitis B Virus Studies","0301 basic medicine","03 medical and health sciences"],"mesh_terms":[],"keywords":["Neutralization","Potency","Antibody","Virology","Ebolavirus","Neutralizing antibody","Glycoprotein","Biology","Immunology","Ebola virus","Molecular biology","In vitro","Virus","Genetics","Article"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"refseq"},{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-04T12:08:29.993720Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}