Nanobodies: natural single-domain antibodies.

TitleNanobodies: natural single-domain antibodies.
Publication TypeJournal Article
Year of Publication2013
AuthorsMuyldermans, S.
JournalAnnu Rev Biochem
Volume82
Pagination775-97
Date Published2013
ISSN1545-4509
KeywordsAnimals, 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.

DOI10.1146/annurev-biochem-063011-092449
Alternate JournalAnnu. Rev. Biochem.
PubMed ID23495938