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J Biol Chem, Vol. 274, Issue 42, 29862-29873, October 15, 1999

Male-specific Modification of Human CD52

Sabine SchröterDagger , Petra DerrDagger , Harald S. Conradt§, Manfred Nimtz§, Geoffrey Hale, and Christiane KirchhoffDagger

From the Dagger  Institute for Hormone and Fertility Research at the University of Hamburg, Grandweg 64, D-22529 Hamburg, Germany, the § Gesellschaft für Biotechnologische Forschung mbH, Mascheroder Weg 1, D-38124 Braunschweig, Germany, and the  Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom

CD52 is an unusually short, bipolar glycopeptide bearing a highly charged N-linked carbohydrate moiety and a glycosylphosphatidylinositol membrane anchor. It is exclusively expressed on lymphocytes and in the male genital tract where it is shed into the seminal plasma and inserts into the sperm membrane. The sperm surface molecule has potential significance as a target for antibodies that inhibit sperm function and gamete interaction. Western blot analyses suggested cell type-specific modifications of the antigen. It was purified from seminal plasma and a detailed structural analysis performed. The majority of anchor structures in male genital tract CD52 showed 2-inositol palmitoylation, rendering molecules insensitive toward phospholipase C, and a sn-1-alkyl-2-lyso-glycerol structure in place of the diacylated anchor described by Treumann et al. (Treumann, A., Lifely, M. R., Schneider, P., and Ferguson, M. A. (1995) J. Biol. Chem. 270, 6088-6099). N-Glycans of the male genital tract product were based on bi-, tri-, and tetraantennary structures of highly charged (up to -7), terminally sialylated complex-type sugars. A substantial proportion carried varying numbers of lactosamine repeats of which nearly 30% were branched. Different from lymphocytes, 10-15% of all N-glycans of the male genital tract antigen also contained peripheral fucose. These data confirm that male genital tract CD52 is distinct from the lymphocyte form by both N-linked glycans and COOH-terminal attached lipid anchor.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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