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Glycobiology Advance Access published online on July 19, 2007
Glycobiology, doi:10.1093/glycob/cwm076
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© The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

The Sperm Agglutination Antigen-1 (SAGA-1) Glycoforms of CD52 are O-glycosylated

Simon Parry1, Nyet-Kui Wong1,4, Richard L Easton1,5, Maria Panico1, Stuart M Haslam1, Howard R Morris1,2, Peggy Anderson3, Kenneth L Klotz3, John C Herr3, Alan B Diekman3,6 and Anne Dell1,*

1 Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, UK
2 M-SCAN Ltd., Wokingham, Berks RG41 2TZ, UK
3 Department of Cell Biology, University of Virginia, Charlottesville, VA 22908, USA

* Corresponding author: phone: 44-207-5945219, fax: 44-207-2250458 e-mail: a.dell{at}imperial.ac.uk

Received on June 13, 2007; accepted on July 10, 2007

CD52 is composed of a twelve amino acid peptide with N-linked glycans bound to the single potential glycosylation site at position 3, and a glycosylphosphatidylinositol-anchor attached at the C-terminus. Some glycoforms of this molecule expressed in the male reproductive tract are recognized by complement-dependent sperm-immobilising antibodies in infertile patients making this antigen an important target for immunocontraception and fertility studies. Although the amount of post-translational modification is already remarkable for such a small polypeptide, O-glycosylation of CD52 has additionally been implicated by several studies but never rigorously characterized. In this report we show clear evidence for the presence of O-glycans in CD52 preparations immunopurified using the murine S19 monoclonal antibody generated against sperm agglutination antigen-1 (SAGA-1), a male reproductive tract specific form of CD52. The O-glycans have been characterized by MALDI-TOF and tandem mass spectrometry after reductive elimination and permethylation. The data indicate that the major SAGA-1 O-glycans are core 1 and 2 mucin-type structures, with and without sialic acid (NeuAc0-2Hex1-3HexNAc1-2HexNAcitol). Minor fucosylated O-glycans are also present including some structures with putative Ley epitopes (NeuAc0-1Fuc1-3Hex1-2HexNAc0-1HexNAcitol). Analysis of O-glycopeptides by tandem mass spectrometry provided an additional level of support for the O-glycosylation of SAGA-1. Elucidation of the O-glycosylation of SAGA-1 adds to the complexity of this molecule and may help to explain its biological activity.

Key words: O-glycan / CD52 / mass spectrometry

4 Present address: School of Science and Technology, University Malaysia Sabah, Kota Kinabalu, Sabah, Malaysia

5 Present address: M-SCAN Ltd., Wokingham, Berks RG41 2TZ, UK

6 Present address: Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA


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