|Title||Nanobodies: natural single-domain antibodies.|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Journal||Annu Rev Biochem|
|Keywords||Animals, Antibodies, Antibody Affinity, Biotechnology, Camelids, New World, Camels, Immunoglobulin Heavy Chains, Single-Domain Antibodies|
Sera of camelids contain both conventional heterotetrameric antibodies and unique functional heavy (H)-chain antibodies (HCAbs). The H chain of these homodimeric antibodies consists of one antigen-binding domain, the VHH, and two constant domains. HCAbs fail to incorporate light (L) chains owing to the deletion of the first constant domain and a reshaped surface at the VHH side, which normally associates with L chains in conventional antibodies. The genetic elements composing HCAbs have been identified, but the in vivo generation of these antibodies from their dedicated genes into antigen-specific and affinity-matured bona fide antibodies remains largely underinvestigated. However, the facile identification of antigen-specific VHHs and their beneficial biochemical and economic properties (size, affinity, specificity, stability, production cost) supported by multiple crystal structures have encouraged antibody engineering of these single-domain antibodies for use as a research tool and in biotechnology and medicine.
|Alternate Journal||Annu. Rev. Biochem.|