Lewis X-containing neoglycoproteins mimic the intrinsic ability of zona pellucida glycoprotein ZP3 to induce the acrosome reaction in capacitated mouse sperm

Biol Reprod. 2004 Sep;71(3):778-89. doi: 10.1095/biolreprod.103.023820. Epub 2004 May 5.

Abstract

The binding of zona pellucida (ZP) glycoprotein ZP3 to mouse sperm surface receptors is mediated by protein-carbohydrate interactions. Subsequently, ZP3 induces sperm to undergo the acrosome reaction, an obligatory step in fertilization. We have previously identified Lewis X (Le(x); Gal beta 4[Fuc alpha 3]GlcNAc) as a potent inhibitor of in vitro sperm-ZP binding (Johnston et al. J Biol Chem 1998; 273:1888-1895). This glycan is recognized by approximately 70% of the ZP3 binding sites on capacitated, acrosome-intact mouse sperm, whereas Lewis A (Le(a); Gal beta 3[Fuc alpha 4]GlcNAc) is recognized by most of the remaining sites (Kerr et al. Biol Reprod 2004; 71:770-777). Herein, we test the hypothesis that Le(x)- and Le(a)-containing glycans, when clustered on a neoglycoprotein, bind ZP3 receptors on sperm and induce sperm to undergo the acrosome reaction via the same signaling pathways as ZP3. Results show that a Le(x)-containing neoglycoprotein induced the acrosome reaction in a dose-dependent and capacitation-dependent manner. A Le(a)-containing neoglycoprotein also induced sperm to undergo the acrosome reaction but was less potent than Le(x)-containing neoglycoproteins. In contrast, neoglycoproteins containing beta4-lactosamine (Gal beta 4GlcNAc), Lewis B (Fuc alpha 2Gal beta 3[Fuc alpha 4]GlcNAc), and sialyl-Le(x) glycans were inactive, as were four other neoglycoproteins with different nonfucosylated glycans. Consistent with these results, unconjugated Le(x)- and Le(a)-capped glycans were dose-dependent inhibitors, which at saturation, reduced the ZP-induced acrosome reaction by about 60% and 30%, respectively. Experiments utilizing pharmacological inhibitors suggest that induction of the acrosome reaction by solubilized ZP and Le(x)- and Le(a)-containing neoglycoproteins require the same calcium-dependent pathway. However, only the ZP-induced acrosome reaction requires a functional G(i) protein. Thus, Le(x)-containing neoglycoproteins bind to a major class of ZP3 receptors on capacitated sperm. A Le(a)-containing neoglycoprotein binds a second ZP3 receptor but is a less-potent inducer of the acrosome reaction.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acrosome Reaction / drug effects*
  • Animals
  • Calcium / metabolism
  • Carbohydrate Sequence
  • Dose-Response Relationship, Drug
  • Egg Proteins / metabolism*
  • Female
  • Galactose / metabolism
  • Galactose / pharmacology
  • Glycoproteins / metabolism*
  • Glycoproteins / pharmacology
  • Lactose / metabolism
  • Lactose / pharmacology
  • Lewis X Antigen / analogs & derivatives
  • Male
  • Membrane Glycoproteins / metabolism*
  • Mice
  • Mice, Inbred ICR
  • Molecular Sequence Data
  • N-Acetylneuraminic Acid / metabolism
  • N-Acetylneuraminic Acid / pharmacology
  • Receptors, Cell Surface / metabolism*
  • Serum Albumin, Bovine / metabolism
  • Serum Albumin, Bovine / pharmacology
  • Signal Transduction / drug effects
  • Signal Transduction / physiology
  • Sperm Capacitation / physiology*
  • Trisaccharides / metabolism*
  • Trisaccharides / pharmacology
  • Zona Pellucida Glycoproteins

Substances

  • Egg Proteins
  • Glycoproteins
  • Lewis X Antigen
  • Membrane Glycoproteins
  • Receptors, Cell Surface
  • Trisaccharides
  • Zona Pellucida Glycoproteins
  • Zp3 protein, mouse
  • galactosyl-(1,4)-fucopyranosyl-(1,3)-N-acetylglucosamine
  • Serum Albumin, Bovine
  • N-Acetylneuraminic Acid
  • Lactose
  • Calcium
  • Galactose