Annual Review of Biochemistry· 2013Q1· Review
Nanobodies: Natural Single-Domain Antibodies
- 2,318citations
- Q1SCImago
- 2013year
Short summary
Camelid heavy-chain antibodies (HCAbs) are naturally occurring single-domain antibodies (VHHs) lacking light chains, offering advantages in size, affinity, stability, and production cost for research and therapeutic applications.
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Key points
- Camelids produce heavy-chain antibodies (HCAbs) that naturally lack light chains.
- The antigen-binding region of HCAbs is a single VHH domain.
- HCAbs are generated from dedicated genes, but the in vivo process is not fully understood.
- VHH domains offer beneficial properties: small size, high affinity, specificity, stability, and low production cost.
- These properties support the use of engineered VHHs as research tools and in biotechnology and medicine.
AI-generated from the title and abstract; the full text is not read.
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.
The authors' abstract, as published at the source. Annual Review of Biochemistry, 2013 · DOI ↗
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