{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Chun J"],"funding":["NIAID NIH HHS","NIH HHS"],"pubmed_abstract":["The monoclonal antibody L9 mediates high-level protection against malaria in children for up to 6 months in Africa. L9 preferentially binds with high affinity to the NVDP minor repeat on the <i>P. falciparum</i> circumsporozoite protein (PfCSP). Here, we sought to improve the affinity of L9 to enhance protection against rare strains with two spatially separated minor repeats or a single minor repeat. Site saturation mutagenesis and yeast display-screening identified a panel of affinity-improved variants. <i>In vivo</i> challenge showed one variant, L9_yd19, to be modestly more potent against a chimeric transgenic <i>Plasmodium</i> encoding PfCSP with two widely spaced minor repeats from a Kenyan parasite strain, with no loss in potency against the benchmark 3D7 strain with its standard com"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2025.09.30.679367"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12621802"],"repository":["biostudies-literature"],"pubmed_title":["Anti-Malaria Antibody Engineering Broadens Recognition Motifs and Reveals New Homotypic Interactions that Enhance Protective Breadth."],"pmcid":["PMC12621802"],"funding_grant_id":["R01 AI192975","DP5 OD023118","R01 AI181684"],"pubmed_authors":["Hurlburt NK","Miura K","Lee GA","Teng IT","Lei H","Zavala F","Tripathi P","Fahad AS","Zhou T","Flores-Garcia Y","DeKosky BJ","Madan B","Chun J","Pancera M","Idris AH","Seder RA","Flynn BJ","Kwong PD"],"additional_accession":[]},"is_claimable":false,"name":"Anti-Malaria Antibody Engineering Broadens Recognition Motifs and Reveals New Homotypic Interactions that Enhance Protective Breadth.","description":"The monoclonal antibody L9 mediates high-level protection against malaria in children for up to 6 months in Africa. L9 preferentially binds with high affinity to the NVDP minor repeat on the <i>P. falciparum</i> circumsporozoite protein (PfCSP). Here, we sought to improve the affinity of L9 to enhance protection against rare strains with two spatially separated minor repeats or a single minor repeat. Site saturation mutagenesis and yeast display-screening identified a panel of affinity-improved variants. <i>In vivo</i> challenge showed one variant, L9_yd19, to be modestly more potent against a chimeric transgenic <i>Plasmodium</i> encoding PfCSP with two widely spaced minor repeats from a Kenyan parasite strain, with no loss in potency against the benchmark 3D7 strain with its standard com","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-11T03:10:43.32Z","creation":"2026-06-11T03:07:52.21Z"},"accession":"S-EPMC12621802","cross_references":{"pubmed":["41256528"],"doi":["10.1101/2025.09.30.679367"]}}