Antibody repertoire development in camelids.
The humoral immune response of the Camelidae is unique as these animals are the only known mammals that seem to possess functional homodimeric heavy-chain antibodies besides the classical heteromeric antibodies composed of heavy (H) and light (L) chains. By definition, the heavy-chain antibodies lack the L-chain, and it was noticed that their H-chain is devoid of the typical first constant domain (CH1) and contains a dedicated variable domain, referred to as VHH. The VHH exon is assembled from separate V-D-J gene segments. The recombined VHH region is subjected to somatic hypermutations; however, the timing and actual mechanism of the class switch from mu to the dedicated gamma-isotype remains elusive. Interestingly, antigen-specific VHHs are easily retrieved after panning of a phage-displayed rearranged V-gene pool cloned from an immunised camelid. These single-domain antigen binding entities possess a number of biophysical properties that offer particular advantages in various medical and biotechnological applications.
De Genst
Erwin
E
Laboratory of Cellular & Molecular Immunology, Department of Molecular & Cellular Interactions, Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Building E, Room 8.2, Pleinlaan 2, 1050 Brussel, Belgium.
Saerens
Dirk
D
Muyldermans
Serge
S
Conrath
Katja
K
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology / Q000378:metabolism; D002161:Camelids, New World / Q000235:genetics / Q000276:immunology*; D002162:Camelus / Q000235:genetics / Q000276:immunology*; D015321:Gene Rearrangement; D007143:Immunoglobulin Heavy Chains / Q000096:biosynthesis / Q000097:blood / Q000737:chemistry / Q000235:genetics; D007147:Immunoglobulin Light Chains / Q000096:biosynthesis / Q000097:blood / Q000737:chemistry / Q000235:genetics
D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains