| Literature DB >> 16332457 |
Sophie Sibéril1, Christophe de Romeuf, Nicolas Bihoreau, Nadine Fernandez, Jean-Luc Meterreau, Annie Regenman, Emmanuel Nony, Christine Gaucher, Arnaud Glacet, Sylvie Jorieux, Philippe Klein, Mark P Hogarth, Wolf-Herman Fridman, Dominique Bourel, Roland Béliard, Jean-Luc Teillaud.
Abstract
The substitution of plasmatic anti-RhD polyclonal antibodies by a monoclonal antibody (mAb) for preventing the hemolytic disease of the newborn (HDN) is an important issue due to supply and safety concerns. Since it has been suggested that FcgammaR are involved in the prevention of HDN, the in vitro functional properties of two anti-RhD mAbs differing through their glycosylation profiles were compared using FcgammaR-based assays to select a candidate mAb. T125(YB2/0), a low fucosylated antibody, bound strongly to both activating FcgammaRIII and inhibitory FcgammaRII, as opposed to its highly fucosylated counterpart. It also exerted a strong ADCC against RhD+ RBCs and a potent FcgammaRIIB-mediated inhibition of cytokine release. Moreover, an in vivo RhD+ red blood cells (RBCs) clearance assay showed that this antibody exhibits a RhD+ RBCs clearance as potent as polyclonal anti-RhD antibodies in NOD-SCID mice. Thus, T125(YB2/O) has been selected to be tested for the prevention of anti-RhD allo-immunization.Entities:
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Year: 2005 PMID： 16332457 DOI： 10.1016/j.clim.2005.10.008
Source DB: PubMed Journal: Clin Immunol ISSN： 1521-6616 Impact factor: 3.969