Naturally occurring antibodies devoid of light chains


RANDOM association of VL and VH repertoires contributes considerably to antibody diversity1. The diversity and the affinity are then increased by hypermutation in B cells located in germinal centres2. Except in the case of 'heavy chain' disease3, naturally occurring heavy-chain antibodies have not been described, although antigen binding has been demonstrated for separated heavy chains4 or cloned VH domains5. Here we investigate the presence of considerable amounts of IgG-like material of Mr 100K in the serum of the camel (Camelus dromedarius)6. 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.

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Hamers-Casterman, C., Atarhouch, T., Muyldermans, S. et al. Naturally occurring antibodies devoid of light chains. Nature 363, 446–448 (1993).

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