Journal
SCIENCE
Volume 333, Issue 6050, Pages 1761-1764Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1207438
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) [BBF0083091]
- Royal Society
- Breeden-Adams Foundation
- Life Sciences Mission Enhancement Reproductive Biology Program
- state of Missouri
- University Research Committee, University of Hong Kong
- Taiwan National Science Council [NSC99-3112-B-001-025]
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Human fertilization begins when spermatozoa bind to the extracellular matrix coating of the oocyte, known as the zona pellucida (ZP). One spermatozoan then penetrates this matrix and fuses with the egg cell, generating a zygote. Although carbohydrate sequences on the ZP have been implicated in sperm binding, the nature of the ligand was unknown. Here, ultrasensitive mass spectrometric analyses revealed that the sialyl-Lewis(x) sequence [NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc], a well-known selectin ligand, is the most abundant terminal sequence on the N- and O-glycans of human ZP. Sperm-ZP binding was largely inhibited by glycoconjugates terminated with sialyl-Lewis(x) sequences or by antibodies directed against this sequence. Thus, the sialyl-Lewis(x) sequence represents the major carbohydrate ligand for human sperm-egg binding.
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