Emergence and evolution of functional heavy-chain antibodies in Camelidae

Antibodies of jawed-vertebrates are composed of paired heavy (H) and light (L) polypeptide chains. Surprisingly, the sera of camelids, nurse shark and wobbegong shark, and possibly ratfish contain antibodies that lack L-chains. In camelids, these Heavy-chain antibodies (HCAbs) are γ-isotypes, and ar...

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Bibliographic Details
Published in:Developmental and Comparative Immunology 2003-02, Vol.27 (2), p.87-103
Main Authors: Conrath, K.E, Wernery, U, Muyldermans, S, Nguyen, V.K
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antibodies - genetics
Base Sequence
Binding Sites
Biological Evolution
Camelidae
Camelus - immunology
Combinatorial diversity
Complementarity Determining Regions - chemistry
Gene Rearrangement
Heavy-chain antibody
Immunoglobulin Constant Regions - genetics
Immunoglobulin Heavy Chains - genetics
Immunoglobulin Variable Region - genetics
Immunoglobulins
Molecular Sequence Data
Phylogeny
Somatic Hypermutation, Immunoglobulin
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Summary:Antibodies of jawed-vertebrates are composed of paired heavy (H) and light (L) polypeptide chains. Surprisingly, the sera of camelids, nurse shark and wobbegong shark, and possibly ratfish contain antibodies that lack L-chains. In camelids, these Heavy-chain antibodies (HCAbs) are γ-isotypes, and are functional in antigen binding. In this review we focus on the dedicated immunoglobulin (Ig) genes that encode the HCAb in Camelidae (camels, dromedaries and llamas), about their origin, and how these camel immunoglobulins evolved and acquire a large and diverse repertoire of antigen binding sites in absence of the H–L combinatorial diversity.
ISSN:0145-305X
1879-0089
DOI:10.1016/S0145-305X(02)00071-X