Shark variable new antigen receptor (VNAR) single domain antibody fragments: stability and diagnostic applications
Open accessAbstract
The single variable new antigen receptor domain antibody fragments (VNARs) derived from shark immunoglobulin new antigen receptor antibodies (IgNARs) represent some of the smallest known immunoglobulin-based protein scaffolds. As single domains, they demonstrate favorable size and cryptic epitope recognition properties, making them attractive in diagnosis and therapy of numerous disease states. Here, we examine the stability of VNAR domains with a focus on a family of VNARs specific for apical membrane antigen 1 (AMA-1) from Plasmodium falciparum. The VNARs are compared to traditional monoclonal antibodies (mAbs) in liquid, lyophilized and immobilized nitrocellulose formats. When maintained in various formats at 45 °C, VNARs have improved stability compared to mAbs for periods of up to four weeks. Using circular dichroism spectroscopy we demonstrate that VNAR domains are able to refold following heating to 80 °C. We also demonstrate that VNAR domains are stable during incubation under potential in vivo conditions such as stomach acid, but not to the protease rich environment of murine stomach scrapings. Taken together, our results demonstrate the suitability of shark VNAR domains for various diagnostic platforms and related applications.
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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 [229]
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- Authors
- Griffiths, K., Dolezal, O., Parisi, K., Angerosa, J., Dogovski, C., Barraclough, M., Sanalla, A., Casey, J., González, I., Perugini, M., Nuttall, S., & Foley, M.
- Affiliations
- La Trobe University (AU)
- Commonwealth Scientific and Industrial Research Organisation (AU)
- FIND (CH)
- Corresponding author
- Foley, Michael
- Venue
- Antibodies
- Publisher
- MDPI AG
- Published
- 2013-01-25
- Volume
- 2
- Issue
- 1
- Pages
- 66-81
- ISSN
- 2073-4468 (ISSN-L)
- OpenAlex
- W2130769674
- Cited by
- 64
- References
- 35
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 2 · 2023: 9 · 2022: 9 · 2021: 4 · 2020: 6 · 2019: 5 · 2018: 7 · 2017: 5 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 1
- FWCI
- 2.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Antibodies (publishedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Institutes of Health
- Medical Research Council
- Australian Research Council (FT0991245)
- National Health and Medical Research Council (487339)
- 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 › Biochemical and Structural Characterization
- Keywords
- single-domain antibody fragments, protein stability, thermal stability, refolding, freeze-drying, Plasmodium falciparum, AMA1, malaria diagnosis, protease resistance, gastric acid
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