|Title||Naturally occurring antibodies devoid of light chains.|
|Publication Type||Journal Article|
|Year of Publication||1993|
|Authors||Hamers-Casterman, C., T. Atarhouch, S. Muyldermans, G. Robinson, C. Hamers, E. B. Songa, N. Bendahman, and R. Hamers|
|Date Published||1993 Jun 3|
|Keywords||Amino Acid Sequence, Animals, Antigens, Protozoan, Base Sequence, Camels, DNA, Single-Stranded, Humans, Immunoglobulin Constant Regions, Immunoglobulin G, Immunoglobulin Heavy Chains, Immunoglobulin Variable Region, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Trypanosomiasis|
Random association of VL and VH repertoires contributes considerably to antibody diversity. The diversity and the affinity are then increased by hypermutation in B cells located in germinal centres. Except in the case of 'heavy chain' disease, naturally occurring heavy-chain antibodies have not been described, although antigen binding has been demonstrated for separated heavy chains or cloned VH domains. Here we investigate the presence of considerable amounts of IgG-like material of M(r) 100K in the serum of the camel (Camelus dromedarius). These molecules are composed of heavy-chain dimers and are devoid of light chains, but nevertheless have an extensive antigen-binding repertoire, a finding that calls into question the role of light chains in the camel. Camel heavy-chain IgGs lack CH1, which in one IgG class might be structurally replaced by an extended hinge. Heavy-chain IgGs are a feature of all camelids. These findings open new perspectives in the engineering of antibodies.