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• W3187150819 abstract "ABSTRACT L9 is a potent human monoclonal antibody (mAb) that preferentially binds two adjacent NVDP minor repeats and cross-reacts with NANP major repeats of the Plasmodium falciparum circumsporozoite protein (PfCSP) on malaria-infective sporozoites. Understanding this mAb’s ontogeny and mechanisms of binding PfCSP to neutralize sporozoites will facilitate vaccine development. Here, we isolated mAbs clonally related to L9 and showed that this B-cell lineage has baseline NVDP affinity and evolves to acquire NANP reactivity. Pairing the L9 kappa light chain (L9κ) with clonally-related heavy chains resulted in chimeric mAbs that cross-linked two NVDP, cross-reacted with NANP, and more potently neutralized sporozoites compared to their original light chain. Structural analyses revealed that chimeric mAbs bound the minor repeat motif in a type-1 β-turn seen in other repeat-specific antibodies. These data highlight the importance of L9κ in binding NVDP on PfCSP to neutralize SPZ and suggest that PfCSP-based immunogens might be improved by presenting ≥2 NVDP." @default.
• W3187150819 created "2021-08-16" @default.
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• W3187150819 date "2021-08-11" @default.
• W3187150819 modified "2023-09-30" @default.
• W3187150819 title "The light chain of the L9 antibody is critical for binding circumsporozoite protein minor repeats and preventing malaria" @default.
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• W3187150819 doi "https://doi.org/10.1101/2021.08.11.455919" @default.
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