Dorota SmolarekClaude HattabGholamreza Hassanzadeh-GhassabehSylvie CochetCarlos GutiérrezAlexandre G. De BrevernRachanee UdomsangpetchJulien PicotMagdalena GrodeckaKazimiera WasniowskaSerge MuyldermansYves ColinCaroline Le Van KimMarcin CzerwinskiOlivier BertrandInsermLudwik Hirszfeld Institute of Immunology and Experimental Therapy of the Polish Academy of SciencesInstitut National de la Transfusion SanguineUniversite Paris 7- Denis DiderotVrije Universiteit BrusselFlanders Interuniversity Institute for BiotechnologyUniversidad de Las Palmas de Gran CanariaMahidol University2018-09-242018-09-242010-10-01Cellular and Molecular Life Sciences. Vol.67, No.19 (2010), 3371-3387142090711420682X2-s2.0-77956759905https://repository.li.mahidol.ac.th/handle/20.500.14594/28636Fy 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyNeurosciencePharmacology, Toxicology and PharmaceuticsArticleSCOPUS10.1007/s00018-010-0387-6