Abstract
The impact of seminal plasma components on the fertilization outcomes in humans is still under question. The increasing number of couples facing problems with conception raises the need for predictive biomarkers. Detailed understanding of the molecular mechanisms accompanying fertilization remains another challenge. Carbohydrate–protein recognition may be of key importance in this complex field. In this study, we analyzed the unique glycosylation pattern of seminal plasma proteins, the display of high-mannose and hybrid-type oligosaccharides, by means of their reactivity with mannose-specific Galanthus nivalis lectin. Normozoospermic infertile subjects presented decreased amounts of lectin-reactive glycoepitopes compared to fertile donors and infertile patients with abnormal semen parameters. Glycoproteins containing unveiled mannose were isolated in affinity chromatography, and 17 glycoproteins were identified in liquid chromatography-tandem mass spectrometry with electrospray ionization. The N-glycome of the isolated glycoproteins was examined in matrix-assisted laser desorption ionization mass spectrometry. Eleven out of 27 identified oligosaccharides expressed terminal mannose residues, responsible for lectin binding. We suggest that lowered content of high-mannose and hybrid type glycans in normozoospermic infertile patients may be associated with impaired sperm protection from preterm capacitation and should be considered in the search for new infertility markers.
Highlights
Gamete fusion and some regulatory processes in the fertilization cascade require specific carbohydrate structures [1,2,3]
In this study we aimed to screen seminal plasma (SP) of subfertile/infertile men for the presence of glycoproteins decorated with glycans containing at least one antenna terminated with unveiled mannose, and compare the profile of this mannose expression to fertile subjects, in order to find possible markers of impaired fertility
In the gel region
Summary
Gamete fusion and some regulatory processes in the fertilization cascade require specific carbohydrate structures [1,2,3] This is not surprising, as sugar epitopes are known to provide a system of biological information transfer, and they are fundamental in mediation of a great number of cellular communication events [4,5]. The oligosaccharide is hydrolyzed to the 5-monosaccharide core that is further rebuilt with complex-type antennae, containing GlcNAc, galactose and sialic acid instead of six Man residues. Glycans of this type are considered as a “passport”, enabling secretion of the glycoprotein outside the cell. High-mannose type glycans are absent (or detectable only in trace amounts) in human secretory glycoproteins [8]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
