The polypeptide backbone of recombinant human zona pellucida glycoprotein-3 initiates acrosomal exocytosis in human spermatozoa in vitro

Neil R. Chapman, Efronssini Kessopoulou, Paul D. Andrews, David Hornby, Christopher L. R. Barratt

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Human gamete interaction is of fundamental biological importance, yet the molecular interactions between spermatozoa and the zona pellucida are poorly understood. Surprisingly, the role of the polypeptide backbone of zona pellucida glycoprotein 3 (ZP3), the putative ligand for spermatozoa activation, has been largely overlooked. Purified recombinant human ZP3 was expressed in Escherichia coli as a C-terminal fusion to the dimeric glutathione S-transferase (GST) from Schistosoma japonicum and was shown to induce acrosomal exocytosis in live, capacitated human spermatozoa. The level of exocytosis is comparable with that obtained using purified, glycosylated, recombinant human ZP3 [van Duin, M., Polman, J.E.M., DeBreet, I.T.M., Van Ginneken, K., Bunschoten, H., Grootenhuis, A., Brindle, J. and Aitken, R.J. (1994). Biol Reprod. 51, 607-617]. These data imply that the polypeptide chain of human ZP3 contributes to recognition of spermatozoa during acrosomal exocytosis in vitro.

Original languageEnglish
Pages (from-to)839-845
Number of pages7
JournalBiochemical Journal
Volume330 ( Pt 2)
DOIs
Publication statusPublished - 1 Mar 1998

Keywords

  • Acrosome/physiology
  • Blotting, Western
  • Egg Proteins/analysis
  • Electrophoresis, Polyacrylamide Gel
  • Exocytosis
  • Glutathione Transferase/genetics
  • Humans
  • In Vitro Techniques
  • Male
  • Membrane Glycoproteins/analysis
  • Receptors, Cell Surface/chemistry
  • Recombinant Fusion Proteins/chemistry
  • Zona Pellucida/chemistry
  • Zona Pellucida Glycoproteins

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