Neutral oligosaccharide structures linked to asparagines of porcine zona pellucida glycoproteins

Mori, Etsuko; Takasaki, S.; Hedrick, Jerry L.; Wardrip, Nathan J.; Mori, Tsuneatsu; Kobata, Akira

doi:10.1021/bi00222a012

Cited by 68 publications

(37 citation statements)

References 41 publications

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“…Groups led by Yurewicz (24), Kobata (25,26), Vliegenthart (27, 28), Nakano (14, 29 -37), and Takasaki (38) have analyzed the carbohydrate sequences associated with this matrix. The majority of the N-and O-linked oligosaccharides express extended polylactosamine chains of heterogeneous size that are highly substituted with sulfate groups and sialic acid at their terminal ends.…”

Section: Discussionmentioning

confidence: 99%

Structural Analysis of Murine Zona Pellucida Glycans

Easton¹,

Patankar²,

Lattanzio³

et al. 2000

Journal of Biological Chemistry

103

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Murine sperm initiate fertilization by binding to specific oligosaccharides linked to the zona pellucida, the specialized matrix coating the egg. Biophysical analyses have revealed the presence of both high mannose and complex-type N-glycans in murine zona pellucida. The predominant high mannose-type glycan had the composition Man 5 GlcNAc 2 , but larger oligosaccharides of this type were also detected. Biantennary, triantennary, and tetraantennary complex-type N-glycans were found to be terminated with the following antennae: Gal␤1-4GlcNAc, NeuAc␣2-3Gal␤1-4GlcNAc, NeuGc␣2-3Gal␤1-4GlcNAc, the Sd a antigen (NeuAc␣2-3[GalNAc␤1-4]Gal-␤1-4GlcNAc, NeuGc␣2-3[GalNAc␤1-4]Gal␤1-4GlcNAc), and terminal GlcNAc. Polylactosamine-type sequence was also detected on a subset of the antennae. Analysis of the O-glycans indicated that the majority were core 2-type (Gal␤1-4GlcNAc␤1-6[Gal␤1-3]GalNAc). The ␤1-6-linked branches attached to these O-glycans were terminated with the same sequences as the N-glycans, except for terminal GlcNAc. Glycans bearing Gal␤1-4GlcNAc␤1-6 branches have previously been suggested to mediate initial murine gamete binding. Oligosaccharides terminated with GalNAc␤1-4Gal have been implicated in the secondary binding interaction that occurs following the acrosome reaction. The significant implications of these observations are discussed.The initial event in the life of all sexually reproducing metazoans is the fertilization of an individual egg by a single sperm. Murine sperm begin this process by binding to the specialized extracellular matrix of the egg known as the mZP 1 (1). This matrix has been shown to be composed of three major glycoproteins (designated mZP1, mZP2, and mZP3) (2). There is strong evidence to suggest that binding occurs via the interaction of mZP3-associated glycans with lectin-like proteins on the sperm surface (3, 4) that in turn induce a signal transduction event known as the acrosome reaction (5). During this reaction, the plasma membrane of the sperm fuses with the outer membrane of a lysosome-like organelle known as the acrosome lying just beneath the surface of the sperm. The resulting membrane complex then blebs off to expose the inner acrosomal membrane. In the mouse model, this inner acrosomal membrane then undergoes secondary binding to mZP2. Sperm move through the mZP and fuse with the egg, thus completing the process of fertilization.Initial studies performed by Wassarman and co-workers (3) indicate that either Pronase glycopeptides (3) or O-linked oligosaccharides (4) obtained from mZP3 block murine sperm-egg binding. Several major models for the initial murine gamete binding interaction have subsequently been proposed that are based upon specific carbohydrate recognition (6 -9). A recent study involving recombinant mZP3 synthesized in murine F9 embryonal carcinoma cells suggests that vicinal presentation of O-linked oligosaccharides within a specific region of mZP3 is necessary for initial sperm-egg binding (10). mZP2 has been proposed to be the glycoprotein that mediates...

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Section: Discussionmentioning

confidence: 99%

Structural Analysis of Murine Zona Pellucida Glycans

Easton¹,

Patankar²,

Lattanzio³

et al. 2000

Journal of Biological Chemistry

103

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“…PZP proteins have neutral and acidic N-linked chains and the structures of main components in the neutral N-linked chains from unfractionated PZP protein [17] and those from PZP3 family retaining sperm receptor activity [4] have been determined. The highly heterogeneous nature of PZP proteins is due not to these neutral chains but to the acidic chains.…”

Section: Discussionmentioning

confidence: 99%

Structure of the acidic N‐linked carbohydrate chains of the 55‐kDa glycoprotein family (PZP3) from porcine zona pellucida

Noguchi

Nakano

1992

European Journal of Biochemistry

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Here we report the structures of the acidic chains. Only two kinds of acidic fragments were released from PZP3 by endo-P-galactosidase digestion following p-elimination of 0-linked chains. 500-MHz one-dimensional and two-dimensional 'H-NMR spectroscopy revealed their structures to be Siaa(2-3)Gal~(1-4)[HSO3-6]GlcNAc~(1 -3)Gal and HS03-6GlcNAc/j( 1-3)Gal, showing that the sulfate-containing acidic chains are constructed with non-branched N-acetyllactosamine repeats which have sialic acid(s) at the non-reducing end(s) and sulfate at the C-6 position of GlcNAc residues. The acidic N-linked chains obtained from PZP3 by hydrazinolysis were separated into diantennary chains (34%) and tri-and tetra-antennary chains (66%) by concanavalin-A -agarose gel chromatography. The diantennary chains and their sialidase digests were fractionated by DEAE-HPLC. From the analyses of the endo-P-galactosidase digests of each fraction, structures of the diantennary acidic chains were determined. They are classified into four groups. The first group is the sialylated chains without the sulfated N-acetyllactosamine repeating unit. The other three groups have the chains of various lengths differing in the number of monosulfated N-acetyllactosamine unit. These chains are extended from the Mana(1-3) branch of the trimannosyl core in the second group, from the Mancl(1-6) branch in the third group, and from both branches in the fourth group. The structural features of the tri-and tetra-antennary acidic chains are also presented.Zona pellucida, the mammalian egg coat, plays several roles in the early phase of fertilization. That is, the zona of many animals is the site for recognition by homologous sperm and for the block to polyspermy upon the establishment of fertilization [I]. After fertilization, the zona protects the embryo until implantation. However, the molccular mechanism of these biological functions is not yet fully understood. l h e porcine zona pellucida (PZP) is suitable for understanding the zona functions at the molecular level, because the zona can be obtained from ovaries of slaughtered gilts in relatively large amounts. The porcine zona is composed of three families, PZPl -3, of glycoproteins differing in molecular mass [2]. The carbohydrate chains of PZP3, the 55-kDa family, are reported to retain the sperm receptor activity [3]. We have separated N-linked chains of PZP3 into the neutral and acidic groups and determined the structures of the main components of the neutral chain [4]. We also found that the mixture of the neutral chains possesses the sperm receptor activity and that of the acidic chains does not [4]. The PZP proteins are highly heterogeneous owing mainly to differences in the amount of sulfated N-acetyllactosamine and sialic acids in the acidic chains [5]. Furthermore, diantennary, triantennary, and tetraantennary chains are present in the acidic group [4]. Hence, the complete determination o f the structures of these chains are very difficult, although the structural analysis is indispensable in order to cla...

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“…† Molar ratios are relative to GalNAcol taken as 1.0. to mediate binding of sperm because sperm surface ␤1,4-galactosyltransferase recognizes this structure (38). Although the essential role of the O-linked oligosaccharides in ZP3 seems clear, only limited information is available concerning their structure (36,37), as compared with detailed information on the N-linked oligosaccharides (39,40). Similarly, in the bivalve, unio elongatulus, O-linked oligosaccharides derived from a 220-kDa vitelline coat glycoprotein have been suggested to be responsible for sperm binding (41,42) and although there is evidence that a fucose residue is involved in the binding properties of the 220-kDa glycoprotein, the structure of the oligosaccharide containing the Fuc has not been determined (41).…”

Section: Discussionmentioning

confidence: 99%

Identification of sulfated oligosialic acid units in theO-linked glycan of the sea urchin egg receptor for sperm

Kitazume-Kawaguchi

Inoue

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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The Strongylocentrotus purpuratus sea urchin egg receptor for sperm is a cell surface glycoprotein with a molecular mass of 350 kDa. Recent studies indicate that the sulfated O-linked glycans isolated from the receptor bind to acrosome-reacted sperm. The purified receptor was analyzed with respect to amino acid and carbohydrate content and shown to be composed of 70% carbohydrate by weight. Compositional analysis indicated that both N-and O-linked oligosaccharide chains were present. After peptide:N-glycanase treatment of the receptor to remove most of the N-linked glycan chains, the majority of the sialic acid residues remained associated with the receptor and were shown by several types of experiments to be composed of sulfated oligosialic acid units attached to the O-linked glycan chains of the receptor. Chemical and physical studies on oligosialic chains discovered earlier in the Pronase-generated glycopeptide fraction isolated from the egg cell surface complex of another species of sea urchin, Hemicentrotus pulcherrimus, established that these molecules had the structure: (SO 4 ؊ )-9Neu5Gc␣2(35-O glycolyl Neu5Gc␣23) n . Based on comparative and analytical studies, it was concluded that this sulfated oligosaccharide is a component of a GalNAc-containing chain that is O-linked to the polypeptide chain of the sea urchin egg receptor for sperm. Using a competitive inhibition of fertilization bioassay it was shown that the sulfated oligosialic acid chains derived from the S. purpuratus egg cell surface complex inhibited fertilization; the nonsulfated form of this oligosialic chain had little inhibitory activity.In fertilization, cell surface molecules of the egg and sperm play a central role in the species-specific interactions that occur in many organisms (1, 2). In the case of the sea urchin, earlier studies showed that the sperm protein, bindin, which is a component of the acrosome granule, plays a key role in gamete recognition (3, 4). Following early work in which a high molecular weight glycoprotein on the egg cell surface was implicated as a receptor for sperm (5-7), it was shown that Pronase-generated glycopeptides prepared from this crude receptor preparation inhibited fertilization, but without species specificity (8, 9). Later, a cell surface glycoprotein with a molecular mass of 350 kDa was identified as the egg receptor in Strongylocentrotus purpuratus (10,11). This molecule, as well as a 70-kDa extracellular fragment generated by lysyl endoproteinase C digestion of intact eggs, were shown to contain sugars typical of both N-and O-linked oligosaccharides, as well as sulfate (10, 12). These oligosaccharide chains were fractionated, and the putative O-linked chains were shown to inhibit fertilization and bind without species specificity to acrosome-reacted, but not to unreacted sperm (13). In a subsequent study it was shown that attachment of these chains via a neoglycoprotein to beads mediated kinetically stable binding of sperm to such beads (14).In earlier studies, ␣235-O glycolyl -linked p...

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Neutral oligosaccharide structures linked to asparagines of porcine zona pellucida glycoproteins

Cited by 68 publications

References 41 publications

Structural Analysis of Murine Zona Pellucida Glycans

Structural Analysis of Murine Zona Pellucida Glycans

Structure of the acidic N‐linked carbohydrate chains of the 55‐kDa glycoprotein family (PZP3) from porcine zona pellucida

Identification of sulfated oligosialic acid units in theO-linked glycan of the sea urchin egg receptor for sperm

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