Spermadhesins of the AQN and AWN families, DQH sperm surface protein and HNK protein in the heparin-binding fraction of boar seminal plasma

Jonáková, Věra; Kraus, Michal; Veselský, L; Cechová, D; Bezouška, Karel; Tichá, Marie

doi:10.1530/jrf.0.1140025

Cited by 55 publications

(58 citation statements)

References 22 publications

(34 reference statements)

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“…N-terminal sequence of DQH protein matches exactly the determined N-terminal sequence~32 amino acid residues! of pAIF-1~Hadjisavas et al, 1994;Jonáková et al, 1998!. On the other hand, it is obvious that the DQH protein described here and the pB1 protein described previously belong to the same family of seminal plasma proteins as bovine BSP A1, BSP A3 Seidah et al, 1987!, andstallion HSP-1~Calvete et al, 1995!. These proteins are all members of the large family of cell and matrix adhesion proteins, which includes seminal plasma proteins, colagenases, fibronectins, blood coagulation factors, and large cell surface receptors such as the macrophage mannose receptor, and the cation independent mannose-6-phosphate receptors~Hadjisa-vas et al, 1994!. Unlike in seminal plasma proteins, where the tandemly arranged fibronectin type II repeats encompass most of the protein sequence, in the other proteins of this family, this repeat represents only a small portion of the entire protein sequence.…”

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confidence: 61%

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Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin‐resistant boar seminal plasma O‐glycoprotein related to pB1 protein

et al. 1999

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Abstract:The complete covalent structure of a novel boar DQH sperm surface protein resistant to many classical procedures of enzymatic fragmentation was determined. The relative molecular mass of the major form of this protein determined by ESI-MS and MALDI-MS was 13,065.2 6 1.0 and 13,065.1, respectively. However, additional peaks differing by 162 Da~i.e., minus hexose!, 365 Da~i.e., minus hexose and N-acetylhexosamine!, 146 Da~i.e., plus deoxyhexose!, and 291 Da~i.e., plus sialic acid! indicated the heterogeneity due to differences in glycosylation. The complete covalent structure of the protein was determined using automated Edman degradation, MALDI-MS, and post-source decay~PSD! MALDI-MS, and shown to consist of N-terminal O-glycosylated peptide followed by two fibronectin type II repeats. The carbohydrates are O-glycosidically linked to threonine 10, as confirmed by PSD MALDI-MS of the isolated N-terminal glycopeptide. Eight cysteine residues of the protein form four disulfide bridges, the positions of which were assigned from MALDI-MS and Edman degradation data. We conclude that mass spectral techniques provide an indispensable tool for the detailed analysis of the covalent structure of proteins, especially those that are refractory to standard approaches of protein chemistry.

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mentioning

confidence: 61%

“…It has been shown that boar seminal plasma contains proteins that are not members of AQN and AWN families~Fernlund et al, 1994;Hadjisavas et al, 1994;Jonáková et al, 1998!. One of them, the phosphorylcholine-binding protein pB1, has been recently characterized~Calvete et al, 1997!.…”

mentioning

confidence: 99%

Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin‐resistant boar seminal plasma O‐glycoprotein related to pB1 protein

et al. 1999

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“…Mannose-binding sites and AQN-1 molecules (Jonakova et al, 1998) are localized over the acosomal region of the sperm. GNA-binding proteins of the oviductal membrane bind to the same region of the sperm surface when tested by fluorescence microscopy after treatment of a sperm suspension with the biotinylated protein fraction (Fig.…”

Section: Candidate Molecules Involved In Sperm-oviduct Interactionsmentioning

confidence: 99%

Glycobiology of fertilization in the pig

Töpfer‐Petersen¹,

Ekhlasi-Hundrieser²,

Tsolova³

2008

Int. J. Dev. Biol.

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By adopting internal fertilization, the meeting of both gametes -the sperm and the egg -and thus the highly coordinated sequence of interactions leading to fertilization, occur in the female reproductive tract. In mammals, the oviduct has been shown to translate the requirements of the female, coordinating sperm activation (capacitation) and sperm transport with the arrival of the ovulated egg. A hierarchy of carbohydrate-based interactions accompanies these events ranging from the binding of uncapacitated sperm to the oviductal epithelium (establishment of the female sperm reservoir), to the primary and secondary binding processes contributing to gamete recognition and sperm penetration of the oocyte zona pellucida. The current perspective will focus on the carbohydrate-recognition systems in the binding events during fertilization in the pig. The roles of the major carbohydrate-binding proteins, the spermadhesins and the acrosomal serine proteinase, pro/acrosin are discussed under consideration of recent structural data. The glycans and the glycoproteins of the porcine oviduct with a focus on the candidate sperm receptors as well as the zona pellucida N-glycans of prepuberal pigs have been characterized by a mass spectrometric approach. Furthermore, some preliminary data supporting the hypothesis that the zona pellucida has to undergo a maturation process during oocyte development are presented. KEY WORDS: gamete interaction, spermadhesin, acrosin, zona pellucida, glycoprotein, glycan A short review of mammalian fertilizationThe fertilization of an egg by a sperm is the fundamental event in life, as it culminates in the creation of a new individual. In mammals, the meeting of the fertilizing competent sperm and the ovulated egg is the beginning of a highly coordinated sequence of cellular interactions between the haploid gametes, which leads to the formation of the diploid zygote and initiates embryonic development.The first contact between sperm and egg takes place at the outer surface of the surrounding extracellular matrix of the egg, the zona pellucida (ZP). By binding to distinct oligosaccharides of the ZP glycoproteins, the fertilizing sperm recognizes the egg. Upon anchoring the sperm to the egg through the ZP carbohydrates the signaling cascade leading to acrosomal exocytosis of the sperm is activated allowing the sperm to pass through the zona pellucida. The acrosome-reacted sperm in the end interacts and fuses with the egg plasma membrane, which in turn enables the egg to complete meiosis, to initiate the mechanisms to prevent Int.

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“…These fractions were subjected to CE. Individual protein components of these fractions were obtained using RP-HPLC separation as described previously [14]. These individual proteins were used as standards for CE.…”

Section: Samplesmentioning

confidence: 99%

“…Among the ligands used, immobilized heparin is often applied to separate H+ and heparin-nonbinding fraction of seminal plasma (H -) proteins [7,13,14]. Affinity techniques not only are useful for the protein isolation but also represent a valuable and essential tool for the study and analysis of binding properties of protein components that participate in the fertilization process.…”

Section: Introductionmentioning

confidence: 99%

Affinity liquid chromatography and capillary electrophoresis of seminal plasma proteins

Varilova

Semenkova

Horák

et al. 2006

J of Separation Science

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Interactions of boar, bull, and human seminal plasma proteins with heparin and phosphorylcholine were studied by affinity LC using heparin immobilized to a Toyopearl support. A step gradient elution from 0.15 to 1.50 M NaCl was employed to elute the seminal plasma proteins. Relative amounts of the heparin-binding fraction of seminal plasma proteins (H+) in seminal plasma of three species were determined. Further on, the fraction of seminal plasma proteins interacting with phosphorylcholine-binding proteins (P+) was evaluated. P+ proteins were not found in human seminal plasma and their highest amount was present in bull seminal plasma. A CE method was developed for separation of seminal plasma proteins. Various capillaries and separation conditions were tested; the best resolution was obtained in a bare-silica capillary, with a micellar system consisting of a 0.02 M borate buffer and 0.05 M SDS pH 10.0. The optimized conditions were applied to the identification of the components in boar plasma.

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Spermadhesins of the AQN and AWN families, DQH sperm surface protein and HNK protein in the heparin-binding fraction of boar seminal plasma

Cited by 55 publications

References 22 publications

Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin‐resistant boar seminal plasma O‐glycoprotein related to pB1 protein

Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin‐resistant boar seminal plasma O‐glycoprotein related to pB1 protein

Glycobiology of fertilization in the pig

Affinity liquid chromatography and capillary electrophoresis of seminal plasma proteins

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