Functional antibodies exhibit light chain coherence.

ABSTRACT: The vertebrate adaptive immune system modifies the genome of individual B cells to encode antibodies that bind particular antigens¹. In most mammals, antibodies are composed of heavy and light chains that are generated sequentially by recombination of V, D (for heavy chains), J and C gene segments. Each chain contains three complementarity-determining regions (CDR1-CDR3), which contribute to antigen specificity. Certain heavy and light chains are preferred for particular antigens^2-22. Here we consider pairs of B cells that share the same heavy chain V gene and CDRH3 amino acid sequence and were isolated from different donors, also known as public clonotypes^23,24. We show that for naive antibodies (those not yet adapted to antigens), the probability that the

SUBMITTER: Jaffe DB 

PROVIDER: S-EPMC9607724 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature