Nanobodies: natural 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.
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VHH and V-NAR domains contain more hydrophilic residues on the surface that interfaces with VL domains, and some hydrophobic residues analogous to those at the VH/VL interface are used for interacting with hydrophobic residues in the CDR3 loop.
“Compared to the VH domains, the VHH and V-NAR domains contain more hydrophilic residues on the surface that interfaces with the VL domains, and some hydrophobic residues, that are fixed in the sequences, are analogous to those at the VH/VL interface and are used for interacting with hydrophobic residues in the CDR3 loop [11,12].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [12]
Nanobody paratopes contain on average nearly three additional residues, and the paratope is drawn from a wider set of aligned sequence positions than classical antibody VH domain paratopes, comparable to the set used by the entire VH-VL paratope.
“Perhaps more significant in terms of challenges to computational modelling tools is that nanobody paratopes contain on average nearly three additional residues, and moreover the paratope is drawn from a wider set of aligned sequence positions than classical antibody VH domain paratopes, comparable to the set used by the entire VH-VL paratope [230, 232].”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [230]
Nanobodies are naturally occurring H chain only antibodies in camelids and sharks.
“One of the most promising is the H chain only antibody, or nanobody that are naturally occurring in camelids (llamas, alpacas and camels) [27] and sharks [228, 229] (reviewed by Muyldermans [230] and Bannas et al. [27]).”
From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [230]
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“Furthermore, the nanobody CDRH3 loop is on average three to four residues longer than its antibody counterpart, and significantly more diverse in terms of both primary sequence and tertiary structure configuration, defying the canonical antibody VH-domain-based rules and enabling nanobody CDRH3 loops to exhibit finger…”
BackgroundInfluentialBiomolecular sensors for advanced physiological monitoring
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“Compared to the VH domains, the VHH and V-NAR domains contain more hydrophilic residues on the surface that interfaces with the VL domains, and some hydrophobic residues, that are fixed in the sequences, are analogous to those at the VH/VL interface and are used for interacting with hydrophobic residues in the CDR3 lo…”
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- Authors
- Muyldermans, S.
- Affiliations
- Vrije Universiteit Brussel (BE)
- Corresponding author
- Muyldermans, Serge
- ORCID
- Muyldermans, Serge
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2013-06-02
- Volume
- 82
- Issue
- 1
- Pages
- 775-797
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2169610187
- Cited by
- 2,304
- References
- 150
- Citations by year
- 2026: 225 · 2025: 226 · 2024: 252 · 2023: 216 · 2022: 245 · 2021: 235 · 2020: 202 · 2019: 161 · 2018: 138 · 2017: 120 · 2016: 105 · 2015: 88 · 2014: 78 · 2013: 13
- FWCI
- 13.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
- Keywords
- nanobodies, VHH, heavy-chain antibodies, camelid antibodies, antibody engineering, antigen-binding domain, affinity maturation, antibody stability
- MeSH terms
- Animals, Antibodies, Antibody Affinity, Biotechnology, Camelids, New World, Camelus, Immunoglobulin Heavy Chains, Single-Domain Antibodies
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