IgG cooperativity - Is there allostery? Implications for antibody functions and therapeutic antibody development.

ABSTRACT: A central dogma in immunology is that an antibody's in vivo functionality is mediated by 2 independent events: antigen binding by the variable (V) region, followed by effector activation by the constant (C) region. However, this view has recently been challenged by reports suggesting allostery exists between the 2 regions, triggered by conformational changes or configurational differences. The possibility of allosteric signals propagating through the IgG domains complicates our understanding of the antibody structure-function relationship, and challenges the current subclass selection process in therapeutic antibody design. Here we review the types of cooperativity in IgG molecules by examining evidence for and against allosteric cooperativity in both Fab and Fc domains and the characteris

SUBMITTER: Yang D 

PROVIDER: S-EPMC5680800 | biostudies-literature | 2017 Nov/Dec

REPOSITORIES: biostudies-literature