{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Buck TK"],"funding":["NIAID NIH HHS","HHS | NIH | National Institute of Allergy and Infectious Diseases"],"pagination":["e0127822"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9426445"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(4)"],"pubmed_abstract":["Lassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is particularly resistant to antibody neutralization. Lineage I LASV evades neutralization by half of known antibodies in the GPC-A antibody competition group and all but one of the antibodies in the GPC-B competition group. Here, we solve two cryo-electron microscopy (cryo-EM) structures of LI GP in complex with a GPC-A and a GPC-B antibody. We used complementary structural and biochemical techniques to identify single-amino-acid substitutions in LI that are responsible for immune evasion by each antibody group. Further, we show that LI infection is more dependent on the endosomal receptor lysosome-"],"journal":["mBio"],"pubmed_title":["Neutralizing Antibodies against Lassa Virus Lineage I."],"pmcid":["PMC9426445"],"funding_grant_id":["R21 AI137809","U19 AI142790","R01 AI141251","T32 AI125179","R01AI141251"],"pubmed_authors":["Li H","Harkins SS","Zandonatti MA","Moon-Walker A","Robinson JE","Garry RF","Buck TK","Branco LM","Hastie KM","Schendel SL","Enriquez AS","Saphire EO"],"additional_accession":[]},"is_claimable":false,"name":"Neutralizing Antibodies against Lassa Virus Lineage I.","description":"Lassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is particularly resistant to antibody neutralization. Lineage I LASV evades neutralization by half of known antibodies in the GPC-A antibody competition group and all but one of the antibodies in the GPC-B competition group. Here, we solve two cryo-electron microscopy (cryo-EM) structures of LI GP in complex with a GPC-A and a GPC-B antibody. We used complementary structural and biochemical techniques to identify single-amino-acid substitutions in LI that are responsible for immune evasion by each antibody group. Further, we show that LI infection is more dependent on the endosomal receptor lysosome-","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-06-13T06:03:42.717Z","creation":"2025-02-19T03:28:59.031Z"},"accession":"S-EPMC9426445","cross_references":{"pubmed":["35730904"],"doi":["10.1128/mbio.01278-22"]}}