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Molecular Human Reproduction, Vol. 9, No. 6, 337-343, June 2003
© 2003 European Society of Human Reproduction and Embryology

Article

Epitope analysis for human sperm-immobilizing monoclonal antibodies, MAb H6-3C4, 1G12 and campath-1

Submitted on September 11, 2002; resubmitted on January 15, 2003. accepted on January 23, 2003

A. Hasegawa1, Y. Fu1, H. Tsubamoto2, Y. Tsuji2, H. Sawai1, S. Komori1,2 and K. Koyama1,2,3

1 Laboratory of Developmental Biology and Reproduction, Institute for Advanced Medical Sciences and 2 Department of Obstetrics and Gynecology, Hyogo College of Medicine, 1-1, Mukogawa-cho, Nishinomiya, 663-8501, Japan

3 To whom correspondence should be addressed. e-mail: kkoyama{at}hyo-med.ac.jp

Human monoclonal antibody, MAb H6-3C4, possesses strong sperm immobilizing activity. MAb H6-3C4 has been suggested by several research groups to react with a carbohydrate moiety of male reproductive tract CD52 (mrtCD52). In the present study, we analysed the epitope on mrtCD52 for MAb H6-3C4 and found that it was polymorphic in Western blot analysis and disappeared after enzymatic removal of the N-linked carbohydrate moiety. Two other monoclonal antibodies (1G12, campath-1) with sperm-immobilizing activity recognized mrtCD52 in a polymorphic manner similar to MAb H6-3C4. Further analysis showed that 1G12 recognized a structure formed by the peptide and/or a glycosylphosphatidylinositol (GPI) anchor portion as does campath-1. Results of a lectin binding assay suggested the presence of O-linked carbohydrates on mrtCD52. Our results also indicated that the peptide portion of CD52 could serve as an epitope for sperm-immobilizing antibodies. It was concluded that the epitope of MAb H6-3C4 is similar to, but distinct from, those of 1G12 and campath-1, and that mrtCD52 contains different antigenic epitopes.

Key words: anti-sperm antibody/CD52/complement-dependent sperm immobilization/GPI anchor protein/immunological infertility


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