Complement activation by IgG subclasses is governed by their ability to oligomerize upon antigen binding.

ABSTRACT: Complement activation through antibody-antigen complexes is crucial in various pathophysiological processes and utilized in immunotherapies to eliminate infectious agents, regulatory immune cells, or cancer cells. The tertiary structures of the four IgG antibody subclasses are largely comparable, with the most prominent difference being the hinge regions connecting the Fab and Fc domains, providing them with unique structural flexibility. Complement recruitment and activation depend strongly on IgG subclass, which is commonly rationalized by differences in hinge flexibility and the respective affinities for C1, the first component of the classical complement pathway. However, a unifying mechanism of how these different IgG subclass properties combine to modulate C1 activation has not yet b

SUBMITTER: Frischauf N 

PROVIDER: S-EPMC11536094 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature