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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/28636
Title: A recombinant dromedary antibody fragment (VHH or nanobody) directed against human Duffy antigen receptor for chemokines
Authors: 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
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
Keywords: Biochemistry, Genetics and Molecular Biology;Neuroscience;Pharmacology, Toxicology and Pharmaceutics
Issue Date: 1-Oct-2010
Citation: Cellular and Molecular Life Sciences. Vol.67, No.19 (2010), 3371-3387
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=77956759905&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/28636
ISSN: 14209071
1420682X
Appears in Collections:Scopus 2006-2010

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