Camelid and shark single domain antibodies: Structural features and therapeutic potential
Abstract
In addition to canonical antibodies composed of heavy and light chains, the adaptive immune systems of camelids and cartilaginous fish comprise heavy-chain only isotypes (HcAb) devoid of light chains, where antigen-binding is mediated exclusively by one variable domain. Due to their inherent favorable attributes, such as high affinity and specificity for their cognate antigen, extraordinary stability, small size and, most importantly, the possibility to complement classical antibodies in terms of 'drugable' target-space, HcAb-derived entities evolved as promising candidates for biomedical applications of which many have already proven to be successful in early stage clinical trials.
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The extended CDR3 loop of nanobodies has the capacity to form a finger-like structure with greater structural flexibility, likely fixed in one single conformation upon antigen-binding.
“The extended CDR3 loop of nanobodies has the capacity to form a finger-like structure with greater structural flexibility which, in turn, is likely fixed in one single conformation upon antigen-binding [14,15].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [15]
Cites
The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins
Feige, M. J., Gräwert, M. A., Marcinowski, M., Hennig, J., Behnke, J., Ausländer, D., Herold, E. M., Peschek, J., Castro, C. D., Flajnik, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321502111 · Cited by 91 · see citing works
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CD38 ecto-enzyme in immune cells is induced during aging and regulates NAD+ and NMN levels
Chini, C. C. S., Peclat, T. R., Warner, G. M., Kashyap, S., Espindola-Netto, J. M., de Oliveira, G. C., Gomez, L. S., Hogan, K. A., Tarragó, M. G., Puranik, A. S., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-00298-z · Cited by 349 · see citing works
Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
“The extended CDR3 loop of nanobodies has the capacity to form a finger-like structure with greater structural flexibility which, in turn, is likely fixed in one single conformation upon antigen-binding [14,15].”
BackgroundsdAb-DB: the single domain antibody database
Wilton, E. E., Opyr, M. P., Kailasam, S., Kothe, R. F., & Wieden, H.-J. (2018) · ACS Synthetic Biology · doi:10.1021/acssynbio.8b00407 · Cited by 84 · see citing works
Lucas, A. T., Moody, A., Schorzman, A. N., & Zamboni, W. C. (2021) · Antibodies · doi:10.3390/antib10030030 · Cited by 40 · see citing works
- Authors
- Könning, D., Zielonka, S., Grzeschik, J., Empting, M., Valldorf, B., Krah, S., Schröter, C., Sellmann, C., Hock, B., & Kolmar, H.
- Affiliations
- Technische Universität Darmstadt (DE)
- Helmholtz Institute for Pharmaceutical Research Saarland (DE)
- Merck KGaA, Darmstadt (Germany) (DE)
- Corresponding author
- Hock, Björn
- Kolmar, Harald
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2017-08
- Volume
- 45
- Pages
- 10-16
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2550623601
- Cited by
- 214
- References
- 1
- Citations by year
- 2026: 18 · 2025: 20 · 2024: 24 · 2023: 28 · 2022: 18 · 2021: 30 · 2020: 24 · 2019: 20 · 2018: 21 · 2017: 11
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Technische Universität Darmstadt
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- nanobodies, camelid antibodies, heavy-chain antibodies, antibody structure, therapeutic antibodies, antibody engineering, antibody stability, therapeutic target
- MeSH terms
- Camelidae, Protein Domains, Animals, Humans, Sharks, Single-Domain Antibodies
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