To achieve fertilization, sperm and egg are equipped with specific molecules which mediate the steps of gamete interaction. In mammals, the first interaction between sperm and egg occurs at an egg-specific extracellular matrix, the zona pellucida (zp). The three glycoproteins, ZP1, ZP2, and ZP3, that comprise the zp have been characterized from many species and assigned different roles in gamete interaction. A large number of candidate-binding partners for the zp proteins have been described; a subset of these have been characterized structurally and functionally. Galactosyltransferase, sp56, zona receptor kinase, and spermadhesins are thought to participate in the primary binding between sperm and zp and may initiate the exocytotic release of hydrolytic enzymes in the sperm head, the acrosome reaction. Digestion of the zp by these enzymes enables sperm to traverse the zp, at which time the proteins PH20, proacrosin, sp38, and Sp17 are thought to participate in secondary binding between the acrosome-reacted sperm and zp. Once through the zp, sperm and egg plasma membranes meet and fuse in a process reported to involve the egg integrin alpha 6 beta 1 and the sperm proteins DE and fertilin. These molecules and the processes involved in gamete interaction are reviewed in this chapter within a physiological context.

Molecules involved in mammalian sperm-egg interaction.

During fertilization in mice, free-swimming sperm bind to mZP3, an 83-kDa glycoprotein present in the egg extracellular coat, the zona pellucida [Wassarman, P. M. (1990) Development 108, 1-17]. Mouse sperm recognize and bind to a specific class of serine/threonine-linked (O-linked) oligosaccharides present on mZP3. After binding to mZP3, sperm undergo a form of cellular exocytosis, the acrosome reaction, thereby enabling them to penetrate the zona pellucida and fertilize the egg. Thus, gamete interactions in mice are carbohydrate-mediated. In this context, we tested 15 O-linked-related oligosaccharide constructs with defined structures for their ability to inhibit binding of mouse sperm to ovulated eggs and to induce sperm to undergo the acrosome reaction in vitro. Thirteen of the oligosaccharides were constructed and characterized in our laboratory [Seppo, A., Pentilla, L., Niemela, R., Maaheimo, H., Renkonen, O., & Keane, A. (1995) Biochemistry 34, 4655-4661]; two were obtained commercially. We found that, while none of the oligosaccharides induced sperm to undergo the acrosome reaction, a few of them inhibited binding of sperm to eggs at relatively low concentrations (ID50 < 5 microM). In certain cases, sperm formed head-to-head aggregates in the presence of the oligosaccharides. The results suggest that the ability of oligosaccharides to inhibit binding of sperm to eggs is dependent on several parameters, including the size and branching pattern of the oligosaccharide, as well as on the nature of the sugar residue at the nonreducing end of the oligosaccharide.

Oligosaccharide Constructs with Defined Structures That Inhibit Binding of Mouse Sperm to Unfertilized Eggs in Vitro

The zona pellucida (ZP) is the extracellular matrix that plays important roles in sperm-egg interaction. The ZP is composed of three major glycoproteins that exhibit heterogeneity due to extensive pos

Structure and function of the proteins of the mammalian Zona pellucida.

Towards molecular mechanisms for gamete adhesion and fusion during mammalian fertilization

Publisher Summary This chapter describes gamete surface components that support tight species-specific binding of the free-swimming mammalian sperm to unfertilized eggs. Such binding is mediated in part, by carbohydrate. The zona pellucida glycoprotein, “ZP3,” serves as sperm receptor during fertilization in mammals. Close inspection of the characteristics of this glycoprotein, coupled with some speculation, may shed light on sperm–egg recognition mechanisms in mammals. ZP3 consists of at least two different functional domains, perhaps separated from each other, by a hinge region of the polypeptide. One of the domains is thought to include the C-terminal third of the ZP3 polypeptide, which possesses the O-linked oligosaccharides that constitute, at least in part, the combining site for the sperm.

Sperm--egg recognition mechanisms in mammals.

The zona pellucida surrounding the mammalian oocyte contains a major glycoprotein species, ZP3, that serves as a cell- and species-specific receptor for spermatozoa. In this study we have determined the primary amino acid structure of marmoset ZP3 (marZP3) and examined the expression of marZP3 mRNA within the ovary. The marZP3 gene possesses an open reading frame of 1272 nucleotides which is expressed specifically by the oocyte and encodes a polypeptide chain of 424 amino acids that exhibits 91% homology with the human ZP3 sequence. The disparity between these molecules was confined to a short domain spanning residues 322-352; otherwise the molecules were very similar, showing conservation of many structural features including the N-linked glycosylation sites, location and number of cysteine and proline residues and hydrophobicity profile. The results of this study have important implications for the use of the marmoset monkey as an animal model for the development of contraceptive vaccines targeting ZP3.

https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0967199400001350

Cloning, sequencing and oocyte-specific expression of the marmoset sperm receptor protein, ZP3.

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Cloning, sequencing and oocyte-specific expression of the marmoset sperm receptor protein, ZP3.