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- W4309891838 abstract "The tight junction protein claudin 6 (CLDN6) is differentially expressed on cancer cells with almost no expression in healthy tissue. However, achieving therapeutic MAb specificity for this 4 transmembrane protein is challenging because it is nearly identical to the widely expressed CLDN9, with only 3 extracellular amino acids different. Most other CLDN6 MAbs, including those in clinical development, are cross-reactive with CLDN9, and several trials have now been stopped. Here we isolated rare MAbs that bind CLDN6 with up to picomolar affinity and display minimal cross-reactivity with CLDN9, 22 other CLDN family members, or across the human membrane proteome. Amino acid-level epitope mapping distinguished the binding sites of our MAbs from existing clinical-stage MAbs. Atomic-level epitope mapping identified the structural mechanism by which our MAbs differentiate CLDN6 and CLDN9 through steric hindrance at a single molecular contact point, the γ carbon on CLDN6 residue Q156." @default.
- W4309891838 created "2022-11-29" @default.
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- W4309891838 date "2022-12-01" @default.
- W4309891838 modified "2023-09-30" @default.
- W4309891838 title "Antibody specificity against highly conserved membrane protein Claudin 6 driven by single atomic contact point" @default.
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- W4309891838 doi "https://doi.org/10.1016/j.isci.2022.105665" @default.
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