The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Efficient tumor targeting by single‐domain antibody fragments of camels
Open accessAbstract
The variable domain of functional heavy chain antibodies (VHH) devoid of light chains, found in camels, constitute the smallest intact antigen‐binding domain fragment. Two camel single‐domain fragments, cAb‐Lys2 and cAb‐Lys3, recognizing an overlapping epitope of lysozyme with a dissociation constant of 2 nM and 65 nM, respectively, and a bivalent cAb‐Lys3 were investigated for their ability to target transgenic tumors expressing lysozyme on their membrane. Biodistribution studies revealed that these non‐immunogenic monomeric and bivalent camel single‐domain antigen binders specifically target lysozyme‐expressing tumors and metastatic lesions. The excess of antibody is rapidly eliminated from the blood circulation and no cAb retention was observed in normal organs. The tumor to organ cAb‐ratios at 2 and 8 hr were in the (2.1–10.8):1 and (6.2–23.7):1 range, respectively. The degree and specificity of tumor retention is independent of the affinity of the recombinant camel single‐domain fragments for their antigen and from their univalent monomeric (15 kDa) or bivalent format (33 kDa). This study demonstrates the successful and specific in vivo targeting of tumors by camel single‐domain fragments. It may open perspectives for their future use as tumor‐targeting vehicle, due to their small size, soluble behaviour and because they are non‐immunogenic and interact with epitopes that are less antigenic for conventional antibodies. © 2002 Wiley‐Liss, Inc.
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Naturally occurring antibodies devoid of light chains
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Self-citationSingle-Chain Antigen-Binding Proteins
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Isolation of high affinity human antibodies directly from large synthetic repertoires.
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Anatomy of the antibody molecule
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Selection and identification of single domain antibody fragments from camel heavy‐chain antibodies
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Impact of albumin on drug delivery — New applications on the horizon
Elsadek, B., & Kratz, F. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.09.069 · Cited by 832
Properties, production, and applications of camelid single-domain antibody fragments
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“Until now, multiple injections of VHHs have not shown any immunogenicity in mice, as assessed by the presence of specific antibodies, T cell proliferation, or cytokine levels (Cortez-Retamozo et al. 2002; Coppieters et al. 2006).”
BackgroundNanobodies and nanobody-based human heavy chain antibodies as antitumor therapeutics
Bannas, P., Hambach, J., & Koch-Nolte, F. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01603 · Cited by 572
“VHH domains typically display a high sequence identity with human type 3 VH domains (VH3), likely accounting for their low immunogenicity (40).”
BackgroundActive targeting of gold nanoparticles as cancer therapeutics
Goddard, Z. R., Marín, M. J., Russell, D. A., & Searcey, M. (2020) · Chemical Society Reviews · doi:10.1039/d0cs01121e · Cited by 282
David vs. Goliath: The Structure, Function, and Clinical Prospects of Antibody Fragments
Bates, A., & Power, C. A. (2019) · Antibodies · doi:10.3390/antib8020028 · Cited by 237
Metadata
- Authors
- Cortez‐Retamozo, V., Lauwereys, M., Hassanzadeh Gh., G., Gobert, M., Conrath, K., Muyldermans, S., De Baetselier, P., & Revets, H.
- Venue
- International Journal of Cancer
- Publisher
- Wiley
- Published
- 2002-01-14
- Volume
- 98
- Issue
- 3
- Pages
- 456-462
- ISSN
- 0020-7136 (ISSN-L)
- 1097-0215
- OpenAlex
- W2014041882
- Cited by
- 260
- References
- 27
- FWCI
- 4.98
- Type
- journal article
- Language
- en
- Open access
- bronze
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