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Glycobiology Advance Access originally published online on July 19, 2007
Glycobiology 2007 17(10):1120-1126; 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 Parry5, Nyet-Kui Wong2,5, Richard L Easton3,5, Maria Panico5, Stuart M Haslam5, Howard R Morris5,6,, Peggy Anderson7, Kenneth L Klotz7, John C Herr7, Alan B Diekman4,7 and Anne Dell1,5

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

1 To whom correspondence should be addressed: Tel: +44-207-5945219; Fax: +44-207-2250458; e-mail: a.dell{at}imperial.ac.uk

Received on June 13, 2007; revised on July 9, 2007; accepted on July 10, 2007

CD52 is composed of a 12 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-immobilizing antibodies in infertile patients making this antigen an important target for immunocontraception and fertility studies. Although the amount of posttranslational 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 fucosy- lated O-glycans are also present including some struc- tures with putative Ley epitopes (NeuAc0–1Fuc1–3Hex1–2 HexNAc0–1HexNAcitol). 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: CD52 / O-glycan / mass spectrometry

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

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

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


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