Immunoglobulin constant regions provide stabilization to the paratope and enforce epitope specificity.

ABSTRACT: Constant domains in antibody molecules at the level of the Fab (C_H1 and C_L) have long been considered to be simple scaffolding elements that physically separate the paratope-defining variable (V) region from the effector function-mediating constant (C) regions. However, due to recent findings that C domains of different isotypes can modulate the fine specificity encoded in the V region, elucidating the role of C domains in shaping the paratope and influencing specificity is a critical area of interest. To dissect the relative contributions of each C domain to this phenomenon, we generated antibody fragments with different C regions omitted, using a set of antibodies targeting capsular polysaccharides from the fungal pathogen, Cryptococcus neoformans. Antigen specifici

SUBMITTER: McConnell SA 

PROVIDER: S-EPMC11215335 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature