Publication: A recombinant dromedary antibody fragment (VHH or nanobody) directed against human Duffy antigen receptor for chemokines
Issued Date
2010-10-01
Resource Type
ISSN
14209071
1420682X
1420682X
Other identifier(s)
2-s2.0-77956759905
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Mahidol University
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SCOPUS
Bibliographic Citation
Cellular and Molecular Life Sciences. Vol.67, No.19 (2010), 3371-3387
Suggested Citation
Dorota Smolarek, Claude Hattab, Gholamreza Hassanzadeh-Ghassabeh, Sylvie Cochet, Carlos Gutiérrez, Alexandre G. De Brevern, Rachanee Udomsangpetch, Julien Picot, Magdalena Grodecka, Kazimiera Wasniowska, Serge Muyldermans, Yves Colin, Caroline Le Van Kim, Marcin Czerwinski, Olivier Bertrand A recombinant dromedary antibody fragment (VHH or nanobody) directed against human Duffy antigen receptor for chemokines. Cellular and Molecular Life Sciences. Vol.67, No.19 (2010), 3371-3387. doi:10.1007/s00018-010-0387-6 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/28636
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Title
A recombinant dromedary antibody fragment (VHH or nanobody) directed against human Duffy antigen receptor for chemokines
Other Contributor(s)
Inserm
Ludwik Hirszfeld Institute of Immunology and Experimental Therapy of the Polish Academy of Sciences
Institut National de la Transfusion Sanguine
Universite Paris 7- Denis Diderot
Vrije Universiteit Brussel
Flanders Interuniversity Institute for Biotechnology
Universidad de Las Palmas de Gran Canaria
Mahidol University
Ludwik Hirszfeld Institute of Immunology and Experimental Therapy of the Polish Academy of Sciences
Institut National de la Transfusion Sanguine
Universite Paris 7- Denis Diderot
Vrije Universiteit Brussel
Flanders Interuniversity Institute for Biotechnology
Universidad de Las Palmas de Gran Canaria
Mahidol University
Abstract
Fy blood group antigens are carried by the Duffy antigen receptor for chemokines (DARC), a red cells receptor for Plasmodium vivax broadly implicated in human health and diseases. Recombinant VHHs, or nanobodies, the smallest intact antigen binding fragment derivative from the heavy chain-only antibodies present in camelids, were prepared from a dromedary immunized against DARC N-terminal extracellular domain and selected for DARC binding. A described VHH, CA52, does recognize native DARC on cells. It inhibits P. vivax invasion of erythrocytes and displaces interleukin-8 bound to DARC. The targeted epitope overlaps the well-defined DARC Fy6 epitope. KDof CA52-DARC equilibrium is sub-nanomolar, hence ideal to develop diagnostic or therapeutic compounds. Immunocapture by immobilized CA52 yielded highly purified DARC from engineered K562 cells. This first report on a VHH with specificity for a red blood cell protein exemplifies VHHs' potentialities to target, to purify, and to modulate the function of cellular markers. © 2010 Springer Basel AG.