Emergence and evolution of functional heavy-chain antibodies in Camelidae.

TitleEmergence and evolution of functional heavy-chain antibodies in Camelidae.
Publication TypeJournal Article
Year of Publication2003
AuthorsConrath, K. E., U. Wernery, S. Muyldermans, and V. K. Nguyen
JournalDev Comp Immunol
Volume27
Issue2
Pagination87-103
Date Published2003 Feb
ISSN0145-305X
KeywordsAmino Acid Sequence, Animals, Antibodies, Base Sequence, Binding Sites, Biological Evolution, Camels, Complementarity Determining Regions, Gene Rearrangement, Immunoglobulin Constant Regions, Immunoglobulin Heavy Chains, Immunoglobulin Variable Region, Molecular Sequence Data, Phylogeny, Somatic Hypermutation, Immunoglobulin
Abstract

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 gamma-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.

Alternate JournalDev. Comp. Immunol.
PubMed ID12543123