Immunoglobulin divalence promotes B-cell antigen receptor cluster scale-dependent functions.

ABSTRACT: Antibodies, also known as immunoglobulins, share an evolutionarily conserved dimeric core structure with two antigen binding sites. However, recognition of foreign molecules can be achieved by monovalent binding domains, as evidenced by the T-cell antigen receptor and various innate immune receptors. Thus, the reason for the strict evolutionary conservation of immunoglobulin divalence remains unclear. In addition to being soluble immune effector molecules, each immunoglobulin is also expressed as a membrane-bound isoform in the context of the B-cell antigen receptor (BCR). Here, we generated monovalent BCRs and found that their signaling and antigen internalization capabilities were strongly impaired. By using advanced superresolution imaging of BCRs following stimulation with antigens of

SUBMITTER: Yilmaz E 

PROVIDER: S-EPMC12398502 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature