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 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.
Conrath
K E
KE
Department of Immunology, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Paardenstraat 65, B-1640, Sint Genesius Rode, Belgium.
Wernery
U
U
Muyldermans
S
S
Nguyen
V K
VK
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000235:genetics*; D001483:Base Sequence; D001665:Binding Sites; D005075:Biological Evolution; D002162:Camelus / Q000276:immunology*; D022801:Complementarity Determining Regions / Q000737:chemistry; D015321:Gene Rearrangement; D007127:Immunoglobulin Constant Regions / Q000235:genetics; D007143:Immunoglobulin Heavy Chains / Q000235:genetics*; D007135:Immunoglobulin Variable Region / Q000235:genetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D027041:Somatic Hypermutation, Immunoglobulin
D000906:Antibodies; D022801:Complementarity Determining Regions; D007127:Immunoglobulin Constant Regions; D007143:Immunoglobulin Heavy Chains; D007135:Immunoglobulin Variable Region