Spatial organization of the sperm cell glycoproteome

• Published in: Molecular & cellular proteomics 2024-12, p.100893, Article 100893
• Main Authors: Ji, Rensong, Chiozzi, Riccardo Zenezini, van den Toorn, Henk, Leung, Miguel, Zeev-Ben-Mordehai, Tzviya, Burke, Nathan D., Bromfield, Elizabeth G., Reiding, Karli R., Heck, Albert J.R.
• Format: Article
• Language: English
• ISSN: 1535-9476; 1535-9484; 1535-9484
• DOI: 10.1016/j.mcpro.2024.100893

Sperm cells are terminally differentiated cells that are essential for reproduction in sexually reproducing species. Consistent with their highly specialized function, sperm cells harbor a unique proteome containing many proteins not expressed in somatic cells. In contrast, the post-translational landscape of the sperm proteome remains largely unexplored, limiting our understanding of how modifications such as glycosylation impact sperm function and sperm-egg interactions. Here, we used glycopeptide-centric glycoproteomics to comprehensively characterize protein N-glycosylation in sperm from three mammalian species, revealing clear conservation of glycosylation profiles. We find that glycosylation patterns in sperm proteins are distinct from those in plasma, with as clear distinctive features less sialyation and more paucimannosylation in sperm. Moreover, based on their subcellular location, sperm protein glycosylation varies, with paucimannose species enriched in the acrosomal vesicle, oligomannose species in the sperm head membrane, and complex glycan species in the acrosomal membrane. [Display omitted] •The glycoproteome of human, bull and boar sperm are analyzed.•The sperm glycoproteome is very distinct from the plasma glycoproteome.•Sperm cells are highly compartmentalized and so are its glycan characteristics.•Paucimannose glycans are enriched in the acrosomal vesicle, oligomannose glycans in the head membrane, and complex glycans in the acrosomal membrane.•Glycoproteins and glycan characteristics, as well as their compartmentalization, are conserved between the studied organisms.