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Updated: Sep 22, 2025
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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
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Precision Structural Interpretation of Site-Specific N-Glycans in Seminal Plasma
Miaomiao Xin1,2, Yintai Xu1, Shanshan You1
1College of Life Science, Northwest University, Xi'an, Shaanxi Province 710069, PR China.
Journal of Proteome Research
|May 26, 2022
Summary
This study maps N-linked glycopeptides in human seminal plasma, revealing complex glycan structures. These findings enhance understanding of glycosylation
Area of Science:
- Proteomics
- Glycomics
- Reproductive Biology
Background:
- N-linked glycoproteins in seminal plasma are crucial for sperm function and fertilization.
- Detailed site-specific glycan structures in seminal plasma remain largely uncharacterized.
Purpose of the Study:
- To establish a precise site-specific N-glycoproteome map of human seminal plasma.
- To characterize the diversity and complexity of N-linked glycans in seminal plasma.
Main Methods:
- Utilized a site-specific glycoproteomic approach.
- Employed StrucGP software for glycan structure interpretation.
- Analyzed identified glycopeptides, glycans, N-glycosites, and glycoproteins.
Main Results:
- Identified 9567 unique glycopeptides, 773 N-linked glycan structures, and 1019 N-glycosites from 620 glycoproteins.
- Found glycans comprised of four core and 13 branch structures.
- Observed heavy fucosylation on glycoproteins involved in immune responses, similar to findings in human spermatozoa.
- Discovered more complex glycan structures in seminal plasma compared to spermatozoa, even for shared glycoproteins.
Conclusions:
- The study provides a comprehensive N-glycoproteome map of human seminal plasma.
- The findings reveal significant complexity in seminal plasma glycosylation.
- This data is valuable for future research on male reproductive system glycosylation and function.
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