Naturally occurring antibodies devoid of light chains.

TitleNaturally occurring antibodies devoid of light chains.
Publication TypeJournal Article
Year of Publication1993
AuthorsHamers-Casterman, C., T. Atarhouch, S. Muyldermans, G. Robinson, C. Hamers, E. B. Songa, N. Bendahman, and R. Hamers
JournalNature
Volume363
Issue6428
Pagination446-8
Date Published1993 Jun 3
ISSN0028-0836
KeywordsAmino 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
Abstract

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.

DOI10.1038/363446a0
Alternate JournalNature
PubMed ID8502296