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The Journal of Immunology, 2001, 166: 5018-5026.
Copyright © 2001 by The American Association of Immunologists

HLA-G2, -G3, and -G4 Isoforms Expressed as Nonmature Cell Surface Glycoproteins Inhibit NK and Antigen-Specific CTL Cytolysis1

Béatrice Riteau2,*, Nathalie Rouas-Freiss2,*, Catherine Menier*, Pascale Paul*, Jean Dausset{dagger} and Edgardo D. Carosella3,*

* Service de Recherches en Hémato-Immunologie, Commissariat à l’Energie Atomique-Direction des Sciences du Vivant-Department de Recherche Médicale, Institut Universitaire d’Hématologie, Hôpital Saint Louis, and {dagger} Fondation Jean Dausset, Paris, France

HLA-G is a nonclassical MHC class I molecule that plays a major role in maternal-fetal tolerance. Four membrane-bound (HLA-G1 to -G4) and two soluble (HLA-G5, and -G6) proteins are generated by alternative splicing. Only HLA-G1 has been extensively studied in terms of both expression and function. We provide evidence here that HLA-G2, -G3, and -G4 truncated isoforms reach the cell surface of transfected cells, as endoglycosidase H-sensitive glycoproteins, after a 2-h chase period. Moreover, cytotoxicity experiments show that these transfected cells are protected from the lytic activity of both innate (NK cells) and acquired (CTL) effectors. These findings highlight the immunomodulatory role that HLA-G2, -G3, and -G4 proteins will assume during physiologic or pathologic processes in which HLA-G1 expression is altered.




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