The Journal of Experimental Medicine
BioLegend: PerCP, PerCP/Cy5.5 Ab Conjugates
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Journal of Experimental Medicine, Vol 180, 1609-1617, Copyright © 1994 by Rockefeller University Press


ARTICLES

Altered glycosylation of leukosialin, CD43, in HIV-1-infected cells of the CEM line

JC Lefebvre, V Giordanengo, M Limouse, A Doglio, M Cucchiarini, F Monpoux, R Mariani and JF Peyron
Laboratoire de Virologie, Faculte de Medecine, Hopital de Cimiez, France.

CD43 (leukosialin, gpL115, sialophorin) is a major sialoglycoprotein widely expressed on hematopoietic cells that is defective in the congenital immunodeficiency Wiskott-Aldrich syndrome. It is thought to play an important role in cell-cell interactions and to be a costimulatory molecule for T lymphocyte activation. Using a metabolic 35SO4(2-) radiolabeling assay or biotinylation of cell surface proteins, we describe here that CD43 are sulfated molecules the glycosylation of which is altered in human immunodeficiency virus type 1 (HIV-1)-infected leukemic T cells of the CEM line. Hyposialylation of O-glycans and changed substitution on N-acetylgalactosamine residues are observed. The glycosylation defect is associated with an impairment of CD43-mediated homotypic aggregation which can be restored by resialylation. The hyposialylation of CD43 on HIV-1+ cells may explain the high prevalence of autoantibodies directed against nonsialylated CD43 that have been detected in HIV-1-infected individuals. A defect in glycosylation of important molecules such as CD43 or, as we recently described, CD45 may explain alterations of T cell functions and viability in HIV-1-infected individuals. In addition, a possible implication of hyposialylation in the HIV-1-infected cells entrapment in lymph nodes could be envisioned.
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