Title | Nanobodies: natural single-domain antibodies. |
Publication Type | Journal Article |
Year of Publication | 2013 |
Authors | Muyldermans, S. |
Journal | Annu Rev Biochem |
Volume | 82 |
Pagination | 775-97 |
Date Published | 2013 |
ISSN | 1545-4509 |
Keywords | Animals, Antibodies, Antibody Affinity, Biotechnology, Camelids, New World, Camels, Immunoglobulin Heavy Chains, Single-Domain Antibodies |
Abstract | 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. |
DOI | 10.1146/annurev-biochem-063011-092449 |
Alternate Journal | Annu. Rev. Biochem. |
PubMed ID | 23495938 |
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