Can immunoglobulin C(H)1 constant region domain modulate antigen binding affinity of antibodies?

O Pritsch; G Hudry-Clergeon; M Buckle; Y Petillot; J P Bouvet; J Gagnon; G Dighiero

doi:10.1172/JCI119033

Published November 15, 1996 - More info

View PDF

Abstract

Although the switch process is frequently associated with affinity maturation, the constant region is not assumed to play a role in Ag-Ab binding. In the present work, we demonstrate that two clonally related human monoclonal Igs sharing identical V(H) and V(L) sequences, but expressing different isotypes (IgA1kappa(PER) and IgG1kappa(PER)), bind tubulin with significantly different affinities. This difference was mainly accounted for by a disparity in the association rate constants. These results suggest that affinity maturation of this clone could be achieved through class switching in the absence of further somatic mutations. Since the differences observed were found at the Fab level, they also suggest a role for the C(H)1 domain in structuring the Ag-binding site into a more kinetically competent form.

Can immunoglobulin C(H)1 constant region domain modulate antigen binding affinity of antibodies?

O Pritsch, G Hudry-Clergeon, M Buckle, Y Petillot, J P Bouvet, J Gagnon, and G Dighiero

Article tools

Metrics

Go to

Can immunoglobulin C(H)1 constant region domain modulate antigen binding affinity of antibodies?

O Pritsch, G Hudry-Clergeon, M Buckle, Y Petillot, J P Bouvet, J Gagnon, and G Dighiero

Article tools

Metrics

Go to

Sign up for email alerts