Aug 10, 2000

Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities

J L Xu, M M Davis


All rearranging antigen receptor genes have one or two highly diverse complementarity determining regions (CDRs) among the six that typically form the ligand binding surface. We report here that, in the case of antibodies, diversity at one of these regions, CDR3 of the V(H) domain, is sufficient to permit otherwise identical IgM molecules to distinguish between a variety of hapten and protein antigens. Furthermore, we find that somatic mutation can allow such antibodies to achieve surprisingly high affinities. These results are consistent with a model in which the highly diverse CDR3 loops are the key determinant of specificity in antigen recognition in both T cell receptors (TCR) and antibodies, whereas the germline-encoded CDR1 and CDR2 sequences are much more cross-reactive.

  • References50
  • Citations265


Mentioned in this Paper

Keyhole-limpet hemocyanin
CDR1 gene
2,4-dinitrophenyl keyhole limpet hemocyanin
Ligand Binding
Somatic Mutation
Immunoglobulin Fv Fragments
Receptors, Antigen
CDR1 protein, human
Sequence Determinations
Cross Reactions

Related Feeds

Antibody Specificity

Antibodies produced by B cells are highly specific for antigen as a result of random gene recombination and somatic hypermutation and affinity maturation. As the main effector of the humoral immune system, antibodies can neutralize foreign cells. Find the latest research on antibody specificity here.