Search PubMed⌕ Search

Biomedical subjects

A Dell

Publications and source records attributed to A Dell.

At least 55 records · Page 3Linked to original sources
PubMed1998

Identification of xanthurenic acid as the putative inducer of malaria development in the mosquito.

Malaria is transmitted from vertebrate host to mosquito vector by mature sexual blood-living stages called gametocytes. Within seconds of ingestion into the mosquito bloodmeal, gametocytes undergo gametogenesis. Induction requires the simultaneous exposure to at least two stimuli in vitro: a drop in bloodmeal temperature to 5 degrees C below that of the vertebrate host, and a rise in pH from 7.4 to 8.0-8.2. In vivo the mosquito bloodmeal has a pH of between 7.5 and 7.6. It is thought that in vivo the second inducer is an unknown mosquito-derived gametocyte-activating factor. Here we show that this factor is xanthurenic acid. We also show that low concentrations of xanthurenic acid can act together with pH to induce gametogenesis in vitro. Structurally related compounds are at least ninefold less effective at inducing gametogenesis in vitro. In Drosophila mutants with lesions in the kynurenine pathway of tryptophan metabolism (of which xanthurenic acid is a side product), no alternative active compound was detected in crude insect homogenates. These data could form the basis of the rational development of new methods of interrupting the transmission of malaria using drugs or new refractory mosquito genotypes to block parasite gametogenesis.

Animals↗
PubMed1998

Glycodelins: role in regulation of reproduction, potential for contraceptive development and diagnosis of male infertility.

Glycodelins are glycoproteins synthesized in various glands, with sequence homology to beta-lactoglobulins, and named according to their unique oligosaccharide structures. We purified, cloned and sequenced endometrium- and seminal plasma-derived glycodelins (GdA and GdS respectively) and found that they are involved in various types of cell-cell communications. These include interactions between the spermatozoon and the egg, and between immune cells and their targets. Endometrial GdA inhibits sperm-egg binding, whereas the differently glycosylated GdS in seminal plasma does not. These observation are of interest for reproductive physiology, detection of causes of infertility, and they also may have potential for contraceptive development.

Biomarkers↗
PubMed1998

Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.

The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT). The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase. The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge. The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation. A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae. The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates. The catalytic behavior of these two enzyme forms were found to be very similar if not identical. These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.

Apolipoprotein A-I↗
PubMed1997

Galactosamine in walls of slow-growing mycobacteria.

Galactosamine was found consistently as a minor component of the envelope of five species of slow-growing mycobacteria, including all the major human pathogens, but not three rapid-growing species. The amino sugar was a component of the arabinogalactan of the cell wall skeleton, and occurred at the level of about one residue per arabinogalactan chain. Its amino group was in the free, un-N-acetylated state. Examination of oligosaccharides released by partial acid hydrolysis of arabinogalactan by fast atom bombardment-MS and gas chromatography-MS identified a series of oligoarabinans, each possessing one GalN unit, linked to position 2 of arabinose. It is proposed that the GalN residues occur as stub branches of 1-->5-linked arabinose chains in the arabinogalactan. Possible functions of GalN are discussed.

Carbohydrate Sequence↗
PubMed1997

Novel tetrasaccharides isolated from squid cartilage chondroitin sulfate E contain unusual sulfated disaccharide units GlcA(3-O-sulfate)beta1-3GalNAc(6-O-sulfate) or GlcA(3-O-sulfate)beta1-3GalNAc.

We previously isolated novel tetrasaccharides containing 3-O-sulfated glucuronic acid from king crab cartilage chondroitin sulfate K and demonstrated that the disaccharide units containing 3-O-sulfated glucuronic acid were decomposed by chondroitinase ABC digestion (Sugahara, K., Tanaka, Y., Yamada, S., Seno, N., Kitagawa, H., Haslam, S. M., Morris, H. R., and Dell, A. (1996) J. Biol. Chem. 271, 26745-26754). The findings indicated the necessity to re-evaluate the disaccharide compositions of chondroitin sulfate preparations purified from other biological sources and analyzed using the above enzyme. In this study, to evaluate squid cartilage chondroitin sulfate E a series of even-numbered oligosaccharides were isolated after exhaustive digestion with sheep testicular hyaluronidase and subsequent fractionation by gel chromatography. The tetrasaccharide fraction was subfractionated by high performance liquid chromatography on an amine-bound silica column. Systematic structural analysis of five major fractions, h, l, m, n, and q, by fast atom bombardment mass spectrometry, enzymatic digestions in conjunction with capillary electrophoresis, and 500-MHz 1H NMR spectroscopy revealed one disulfated, three trisulfated, and one tetrasulfated tetrasaccharide structure: fraction h, GlcAbeta1-3GalNAc(4S)beta1-4GlcAbeta1-3GalNAc(4S); fraction l, GlcA(3S)beta1-3GalNAc(6S)beta1-4GlcAbeta1-3GalNAc(4S); fraction m, GlcA(3S)beta1-3GalNAc(4S)beta1-4GlcAbeta1-3GalNAc(4S); fraction n, GlcAbeta1-3GalNAc(4S,6S)beta1-4GlcAbeta1-3GalNAc(4S); and fraction q, GlcA(3S)beta1-3GalNAc(4S,6S)beta1-4GlcAbeta1-3GalNAc(4S), where 3S, 4S, and 6S represent 3-O-, 4-O- and 6-O-sulfate, respectively. The structures found in fractions h and m as well as the unsaturated counterpart of that found in fraction n have been reported, whereas those in fractions l and q are novel in that they contained unusual disulfated and trisulfated disaccharide units where GlcA(3S) is directly linked to GalNAc(6S) and GalNAc(4S,6S), respectively. These novel tetrasaccharide sequences are distinct from those found in other chondroitin sulfate isoforms and may play key roles in the biological functions and activities of chondroitin sulfate E not only from squid cartilage but also from mammalian cells and tissues.

Animals↗
PubMed1997

A novel pentasaccharide sequence GlcA(3-sulfate)(beta1-3)GalNAc(4-sulfate)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4-sulfate) in the oligosaccharides isolated from king crab cartilage chondroitin sulfate K and its differential susceptibility to chondroitinases and hyaluronidase.

Novel sulfated tetrasaccharide structures containing 3-O-sulfated GlcA were isolated recently from king crab cartilage chondroitin sulfate K [Sugahara, K., Tanaka, Y., Yamada, S., Seno, N., Kitagawa, H., Haslam, S. M., Morris, H. R., & Dell, A. (1996) J. Biol. Chem. 271, 26745-26754]. In this study, we prepared a series of oligosaccharides from the same source after exhaustive digestion with testicular hyaluronidase and determined the structures of a pentasaccharide, two hexasaccharides, and two heptasaccharides by means of fast atom bombardment mass spectrometry and 500-MHz 1H-NMR spectroscopy. All the oligosaccharides had the following hitherto unreported structures including a novel glucuronate 3-O-sulfate: GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)GlcA(3S)(beta1-3)GalNAc( 4S)(beta1-4)GlcA(beta1-3)GalNAc(4S), GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)GlcA(3S)(beta1-3)GalNAc( 4S)(beta1-4)GlcA(3S)(beta1-3)-GalNAc(4S), GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4S), GlcA(3S)(beta1-3)-GalNAc(4S)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4S)(beta1-4)GlcA(beta1-3)GalNAc (4S), and GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)GlcA(3S)(beta1-3)GalNAc( 4S)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4S), where 3S or 4S represent 3-O- or 4-O-sulfate, respectively. Furthermore, the three latter structures contained a novel combination of both 3-O-sulfated and 3-O-fucosylated GlcA residues. The pentasaccharide with 3-O-fucosylated GlcA at the internal position remained totally resistant to chondroitinase AC-II, whereas it was degraded by chondroitinase ABC into a disaccharide unit containing GlcA(3S) derived from the nonreducing side and a trisaccharide unit containing fucose from the reducing side.

Animals↗
PubMed1997

Characterisation of the phosphorylcholine-containing N-linked oligosaccharides in the excretory-secretory 62 kDa glycoprotein of Acanthocheilonema viteae.

The major excretory-secretory product of the rodent filarial nematode Acanthocheilonema viteae is a 62 kDa glycoprotein (ES-62), which has phosphorylcholine, attached to the N-linked carbohydrates. In this paper, we describe structural studies of N-glycans released from ES-62 by peptide N-glycosidase F. Three major classes of N-glycan structures were observed: high mannose type structures; those which had been fully trimmed to the trimannosyl core and were sub-stoichiometrically fucosylated; and those with a trimannosyl core, with and without core fucosylation, carrying between one and four additional N-acetylglucosamine resides. Of the three classes of glycans, only the last was found to be substituted with detectable levels of phosphorylcholine. The implications of these results with respect to the probable glycosylation pathways operating in A. viteae are discussed.

Animals↗
PubMed1997

Structural characterization of the N-glycans from Echinococcus granulosus hydatid cyst membrane and protoscoleces.

Infection by the tapeworm Echinococcus granulosus in the intermediate host results in the development of a hydatid cyst which contains the protoscoleces within a fluid-filled cavity enclosed by the bilayered cyst membrane. N-glycans were enzymatically released from crude extracts of homogenates of hydatid cyst membranes and protoscoleces and their structures were defined by high sensitivity fast atom bombardment mass spectrometry in conjunction with sequential exoglycosidase digestions. The major N-glycans from the cyst membrane were found to be non-charged structures having complex-type antennae and core fucosylation. The antennae are either truncated at the first N-acetylglucosamine or are extended with beta-galactose to form N-acetyllactosamine (lacNAc). A significant proportion of the lacNAc backbones are capped by alpha-galactose. The resulting Gal alpha-Gal beta-terminal structures may account for the earlier observation that antibodies against the blood group P1 epitope recognise components of hydatid cyst extracts. The complex-type N-glycans identified in the protoscoleces extracts were the same as the neutral structures found in the cyst membrane but a small proportion of high mannose structures and truncated di- and trimannosyl core structures were also identified. Sialylated N-glycans were identified as minor constituents of the cyst membrane preparation but were not observed in protoscoleces extracts. Whether the sialylated glycans are host derived or endogenously synthesized by the parasite remains to be established. This is the first reported structural analysis of N-glycans from cestodes and provides new insights into protein glycosylation in helminths.

Animals↗
PubMed1997

A novel geometry mass spectrometer, the Q-TOF, for low-femtomole/attomole-range biopolymer sequencing.

Ultra-high-sensitivity, biopolymer sequencing is a goal in many fields of molecular biology, and collisionally activated decomposition electrospray mass spectrometry (CAD ES MS/MS) using a triple quadrupole mass spectrometer has become a method of choice for work in the high- to mid-femtomole range. However, when the detection of ions becomes statistical, as it may in that range, the mass assignment of fragment ions is inaccurate and either sequencing becomes impossible or ambiguities result due, for example, to the closeness in amino acid residue masses (I/L, N or K/Q, E). Some ambiguities may be resolved by synthesizing possible sequences, but this is unsatisfactory. In considering the limitations of triple quadrupole MS/MS with respect to scanning ion detection, resolution, transmission, and mass accuracy, we reasoned that a novel geometry quadrupole orthogonal acceleration time-of-flight (Q-TOF) instrument would have special merit for ultra-high-sensitivity MS/MS sequencing, and suggested its construction for this purpose some three years ago. A prototype Q-TOF has now been built by Micromass [Morris et al. (1996), Rapid Commun. Mass Spectrom. 10, 889-896], and in the first research on the instrument, including MHC antigen and filarial nematode glycoprotein studies, we demonstrate low-femtomole- and attomole-range sequencing with mass accuracy of better than 0.1 Da throughout the daughter-ion spectrum, thus removing sequencing ambiguities in some of the most challenging work demanding the highest sensitivity.

Amino Acid Sequence↗
PubMed1997

Occurrence of terminal alpha 2-->8-linked disialylated poly-N-acetyllactosamine chains with Le(X) and I antigenic glycotopes in tetraantennary arms of an N-linked glycoprotein isolated from rainbow trout ovarian fluid.

The Pronase digestion of a 54K glycoprotein present in ovarian fluid of rainbow trout yielded a major glycopeptide. Carbohydrate compositional analysis revealed that this glycopeptide was likely to possess a single large N-glycan chain having low molecular weight oligomers of N-acetylneuraminic acid (oligoNeu5Ac). Structural studies of this glycopeptide revealed novel alpha 2-->8-linked disialylated poly-N-acetyllactosamine chains with Le(X) and I antigenic determinants on the N-linked tetraantennary core glycan. In our recent studies (Kitazume,S., Kitajima,K., Inoue,S., Inoue,Y. and Troy,F.A. (1994) J. Biol. Chem. 269, 10330-10340) we presented evidence that synthesis of alpha 2-->8-linked polysialic acid (polySia) chains is a two-step process in which chain initiation is catalyzed by an alpha 2-->8-sialyltransferase (alpha 2-->8-ST; initiase) that catalyzes synthesis of the first Sia alpha 2-->8-linkage, forming the disialic acid (diSia) unit, Sia alpha 2-->8-Sia alpha 2-->6-Gal-. Chain polymerization is then postulated to be catalyzed by a second enzyme, an alpha 2-->8-polyST ("polymerase") that converts the diSia units to polySia chains. The present structural studies leading to the discovery of alpha 2-->8-linked disialylated units that terminate poly-N-acetyllactosamine chains in an N-linked glycoprotein is further evidence in support of our hypothesis that more than one sialyltransferase activity is required for polySia chain synthesis and polymerization.

Animals↗
PubMed1997

Structural characterization of glycophingolipids from the eggs of Schistosoma mansoni and Schistosoma japonicum.

The granulomatous pathology in human intestinal schistosomiasis is induced primarily by the egg antigens of schistosome, a parasitic trematode. Glycolipids and glycoproteins were extracted from the eggs of the two major species which infect human, Schistosoma mansoni and Schistosoma japonicum, for structural characterization based on highly sensitive mass spectrometric analysis coupled with chemical derivatization. Here, we demonstrate that a series of uniquely multifucosylated glycosphingolipids constitute the major egg glycolipids of S. mansoni but not of S. japonicum. The S. mansoni glycosphingolipids were found to be extended by varying numbers of an unusual repeating unit, -->4(Fuc1-->2Fuc1-->3)GlcNAc1-->, and terminating as +/-Fuc1-->2Fuc1-->3GalNAc1--> at the nonreducing terminus. The similarity of these fucosylated structures, particularly the nonreducing terminal sequence, to the previously identified multifucosylated O-linked oligosaccharides of the cercarial glycocalyx, suggests that they may constitute the cross-reacting epitopes between the egg antigens and cercariae of S. mansoni. On the other hand, the difucosylated GalNAc terminal epitope was not found on the glycosphingolipids of S. japonicum. Thus, it qualifies for a possible role as a species-specific recognition glycan.

Animals↗
PubMed1997

Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: identification of novel core structures and terminal sequences.

The structural diversity of the glycans from Schistosoma mansoni and Schistosoma japonicum egg glycoproteins was investigated using high sensitivity fast atom bombardment mass spectrometric screening of glycan pools released enzymically or chemically from egg extracts. The egg glycoproteins from the two species carry a comparable range of high mannose and complex type N-glycans with both lacNAc and lacdiNAc constituting the backbones of the antennae in the latter class. Truncated N-glycans similar to those found on nematodes, insects, and plants were also identified. Sequential digestion with peptide N-glycosidase F and peptide N-glycosidase A afforded effective release and separation of N-glycans with nonfucosylated or alpha6-monofucosylated trimannosyl N,N'-diacetyl-chitobiose cores from those carrying core alpha3-, alpha6-difucosylation, all of which were found to be present in both species. Remarkably, a portion of the N-glycans from S. mansoni eggs was shown to be based on a xylosylated, alpha6-fucosylated trimannosyl core, whereas a portion of those from S. japonicum contains a xylosylated alpha3-, alpha6-difucosylated core which has not been previously described in any organism. O-Glycans were chemically released from the de-N-glycosylated glycopeptides and found to carry terminal sequences similar to those in the N-glycans. This study provides further evidence that multi-fucosylated terminal HexNAc units, previously identified on the cercarial glycocalyx O-glycans and egg glycosphingolipids, and now on the egg N- and O-glycans, are unique features of S. mansoni glycans. These multifucosylated terminal structures, which were not detected on the egg glycans of S. japonicum, are likely to constitute the cross-reacting epitopes between the eggs and cercariae of S. mansoni. Interestingly other HexNAc termini, including an unusual stretch of HexNAc3, were found to be common to both species. The mapping studies reported in this article provide an important foundation for further structural work in this challenging and important area of glycobiology.

Animals↗
PubMed1997

Viewing AIDS from a glycobiological perspective: potential linkages to the human fetoembryonic defence system hypothesis.

The primary molecular changes that lead to development of acquired immunodeficiency syndrome (AIDS) are very poorly understood, as are the mechanisms underlying the protection of the developing human from the maternal immune response. Recent data that the human immunodeficiency virus (HIV) may be using the glycosylation system of the T lymphocytes to acquire glycans for its glycoproteins that enable it to disrupt carbohydrate dependent immune cell interactions or induce aberrant immune reactions. Consistent with this hypothesis, gp120 from HIV infected human H9 lymphoblastoid cells expresses biantennary N-linked glycans with a bisecting GlcNAc sequence on 11% of their total oligosaccharides. This specific carbohydrate sequence has recently been shown to protect K562 erythroleukemic cells from natural killer (NK) cell responses when presented on the cell surface. We have recently demonstrated that bisecting biantennary type N-linked glycans are also expressed on the human zona pellucida (ZP); previous lectin binding studies indicate that is also expressed on human spermatozoa. Thus both the human gametes and HIV produced by H9 cells carry this same protective carbohydrate epitope on their outer surfaces. Human alpha-fetoprotein expressed in the developing human also carries the bisecting GlcNAc sequence, indicating that it may be suppressing the emerging fetal immune response by using its carbohydrate sequence as a functional group. We have suggested that the developing human and the gametes are also protected by soluble immunosuppressive glycoproteins found in the amniotic fluid and seminal plasma known as glycodelin-A (GdA) and glycodelin-S (GdS) respectively. Structural analysis of their N-linked oligosaccharides combined with other functional studies suggest that GdA and GdS employ their very unusual carbohydrate sequences as functional groups that enable them to manifest their immunosuppressive activities. GdA and GdS are significant components of our recently proposed model for the protection of the developing human and gametes designated the human fetoembryonic defence system hypothesis. A striking relationship now emerging is that the same unusual carbohydrate sequences associated with these immunosuppressive glycodelins are also specifically expressed on intravascular helminthic parasites, Helicobacter pylori, human tumour cells, and HIV infected T lymphocytes. The information presented in this review suggests that two new corollaries should be added to our recently proposed defence system hypothesis: (i) mimicry or acquisition of glycans that are used in this protective system by pathogens or tumour cells may enable them to either subvert or misdirect the human immune response, thereby greatly increasing their pathogenicity; and (ii) expression of glycoproteins used in this system by normal cells and tissues outside the reproductive system may protect them from immune responses, especially in those cases where major histocompatibility recognition is either absent or minimal. A better understanding of this hypothesis and its corollaries may enable us to address the molecular mechanisms underlying not only AIDS but also a host of other very serious pathological conditions in the human.

Acquired Immunodeficiency Syndrome↗
PubMed1997

Expression of glycans linked to natural killer cell inhibition on the human zona pellucida.

Protection of the gametes from potential immune responses is a primary function in human reproduction. The primary cell type responsible for the innate immune response in the uterus is the natural killer (NK) cell. NK cells normally recognize Class I major histocompatibility (MHC) molecules on potential target cells. Since both human spermatozoa and human oocytes do not express Class I MHC molecules on their surfaces, the appropriate cell surface signal that abrogates potential NK cell-mediated responses directed against these gametes is unknown. Recent evidence indicates that surface expression of bisecting-type N-linked glycans protects cells sensitive to NK cell-mediated lysis. We report that the zona pellucida of the human egg and plasma membranes of human spermatozoa potentially bind a lectin probe specific for bisecting type glycans in a carbohydrate-dependent manner. Since the innate immune response in the uterus is primarily mediated by NK cells, our results indicate that human gametes may be protected from this response by expressing bisecting type N-linked glycans on their surfaces.

Carbohydrate Conformation↗
PubMed1996

Characterization of the major core structures of the alpha2-->8-linked polysialic acid-containing glycan chains present in neural cell adhesion molecule in embryonic chick brains.

To gain more insight into the possible functional significance of the core glycan chain(s) on which polysialylation takes place in polysialic acid (poly-Sia)-containing glycoproteins, the structure of the core glycans in the embryonic form of chick brain neural cell adhesion molecule (N-CAM) were examined using chemical and instrumental techniques. The following new structural features, which had not been reported by the early pioneering study by Finne (Finne, J. (1982) J. Biol. Chem. 257, 11966-11970), were revealed (Structure I). (i) Two distinct types of multiantennary N-linked glycans, i.e. tri- and tetra-antennary structures, are present; (ii) an alpha1-->6-linked fucosyl residue is attached to the proximal GlcNAc residue of the di-N-acetylchitobiosyl unit; (iii) that the action of GlcNAc-transferase V, which catalyzes the attachment of the beta-(1-->6)-linked GlcNAc residue on the (1-->6)-alpha-linked mannose (Man) arm, appears to be essential for polysialylation to occur on the core glycan chain is suggested by the fact that the Man residue alpha1-->6-linked to the beta-linked Man residue is invariably 2,6-di-O-substituted by the GlcNAc residue; (iv) both type 1 (Galbeta1-->3GlcNAc) and type 2 (Galbeta1-->4 GlcNAc) sequences are present in the peripheral portion of the core glycan structure. An extended form of the type 2 chain, i.e. Galbeta1-->4GlcNAcbeta1-->3Galbeta1-->4GlcNAc, is also expressed on the (1-->3)- and (1-->6)-alpha-linked Man arms; (v) on average about 1.4 mol of sulfate is attached to the type 2 N-acetyllactosamine chain(s), where in the extended form the sulfate group is probably substituted at the O-3 position of the outmost GlcNAc residue, i.e. Galbeta1-->4(HSO3-->3)GlcNAcbeta1-->3Galbeta1--> 4GlcNAcbeta1-->Man. It is possible that the unusual structural features identified in this study might play a role in the initiation of polysialylation and our data should facilitate future research regarding the signals that control polysialylation.

Acetylation↗
PubMed1996

Gender-specific glycosylation of human glycodelin affects its contraceptive activity.

We have recently demonstrated that a human amniotic fluid-derived glycoprotein, glycodelin-A (GdA; previously known as PP14 or PAEP), potently inhibits gamete binding in an established sperm-egg binding system and expresses immunosuppressive activities directed against a variety of different immune cell types. GdA has high mannose-, hybrid-, and complex-type biantennary oligosaccharides including structures with fucosylated or sialylated N, N'-diacetyllactosediamine (GalNAcbeta1-4GlcNAc) sequences, which are rare in other human glycoproteins. We now report the characterization of glycodelin-S (GdS). This is a human seminal plasma glycoprotein that is immunologically indistinguishable from GdA, but unlike the latter, does not inhibit human sperm-zona pellucida binding under hemizona assay conditions. Analysis of the N-glycans of GdS by mass spectrometry revealed that all glycoforms of GdS are different from those of GdA. GdS glycans are unusually fucose-rich, and the major complex-type structures are biantennary glycans with Lewisx (Galbeta1-4(Fucalpha1-3)GlcNAc) and Lewisy (Fucalpha1-2Galbeta1-4(Fucalpha1-3)GlcNAc) antennae. It is probable that these highly fucosylated epitopes contribute to the immunosuppressive activity of human seminal plasma and to the low immunogenicity of sperm. This study provides the first evidence for gender-specific glycosylation that may serve to regulate key processes involved in human reproduction.

Contraceptive Agents↗