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• W4313309975 endingPage "3780" @default.
• W4313309975 startingPage "3776" @default.
• W4313309975 abstract "Abstract Abs using the κII-A2 V gene segment predominate the human Ab repertoire to the Haemophilus influenzae b (Hib) polysaccharide (PS). All A2 anti-Hib PS Abs sequenced to date possess a 10-amino acid L chain complementarity-determining region-3 (CDR-3) having an insertional arginine (Arg) at position 95a, the V-J junction. These findings suggest an essential requirement for this conserved Arg residue in determining Hib PS-binding affinity. We examined this requirement by performing chain recombination experiments in which a series of A2 L chains, differing at position 95a, were combined individually with an Fd region known to generate a Hib PS-combining site when paired with an A2-Arg(95a)-Jκ1 V region. Hib PS binding of the recombinant Fabs was evaluated quantitatively using a radioantigen-binding assay. Fabs having A2 L chains with either Arg or lysine in position 95a in combination with Jκ1 gave equivalent and strongest binding to Hib PS. Fabs having A2-Jκ1 L chains with either tyrosine, glycine, alanine, leucine, serine, or threonine in position 95a, or having an A2-Arg(95a)-Jκ3 L chain, gave intermediate binding. Fabs having A2-Jκ1 L chains with glutamate or aspartate at 95a or with no junctional residue showed little or no Hib PS binding. These results demonstrate the importance of L chain junctional residue, as well as Jκ usage and CDR-3 length, in determining Hib PS-binding affinity. Contrary to expectation, an Arg junctional residue is not essential for generating either high or intermediate affinity-binding sites." @default.
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• W4313309975 date "1998-10-01" @default.
• W4313309975 modified "2023-10-04" @default.
• W4313309975 title "Role of κII-A2 Light Chain CDR-3 Junctional Residues in Human Antibody Binding to the<i>Haemophilus influenzae</i>Type b Polysaccharide" @default.
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• W4313309975 doi "https://doi.org/10.4049/jimmunol.161.7.3776" @default.
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