Cancer Diagnosis and Therapy

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Efficient tumor targeting by single-domain antibody fragments of camels

  1. Virna Cortez-Retamozo,
  2. Marc Lauwereys,
  3. Gholamreza Hassanzadeh Gh.,
  4. Martine Gobert,
  5. Katja Conrath,
  6. Serge Muyldermans,
  7. Patrick De Baetselier,
  8. Hilde Revets†,*

Article first published online: 14 JAN 2002

DOI: 10.1002/ijc.10212

Issue

International Journal of Cancer

International Journal of Cancer

Volume 98, Issue 3, pages 456–462, 20 March 2002

Additional Information

How to Cite

Cortez-Retamozo, V., Lauwereys, M., Hassanzadeh Gh., G., Gobert, M., Conrath, K., Muyldermans, S., De Baetselier, P. and Revets, H. (2002), Efficient tumor targeting by single-domain antibody fragments of camels. Int. J. Cancer, 98: 456–462. doi: 10.1002/ijc.10212

Author Information

  1. Vlaams Interuniversitair Instituut voor Biotechnologie, Vrije Universiteit Brussel, Sint Genesius Rode, Belgium

  1. †

    Fax: +32-2-359-03-59

*Department of Cellular Immunology, Flemish Interuniversity Institute for Biotechnology, Free University of Brussels, Paardenstraat 65, B-1640 Sint Genesius Rode, Belgium

Publication History

  1. Issue published online: 28 FEB 2002
  2. Article first published online: 14 JAN 2002
  3. Manuscript Accepted: 5 NOV 2001
  4. Manuscript Revised: 15 OCT 2001
  5. Manuscript Received: 2 JUL 2001

Funded by

  • Fonds Voor Wetenschappelijk Onderzoek (FWO). Grant Number: G. 046399
  • Vrije Universiteit Brussel (VUB) (Concerted Actions)
  • Instituut Voor de Aanmoediging Van Innovatie Door Wetenschap en Technologie in Vlaanderen (IWT)

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Keywords:

  • camel antibodies;
  • single-domain antibodies;
  • tumor targeting;
  • affinity;
  • lysozyme

Abstract

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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