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
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomic Center, Utrecht, The Netherlands.
Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Utrecht, The Netherlands; Netherlands Proteomic Center, Utrecht, The Netherlands; Division of Biosciences, Institute of Structural and Molecular Biology, University College London, London, United Kingdom; Division of Biosciences, University College London Mass Spectrometry Science Technology Platform, University College London, London, United Kingdom.
Mol Cell Proteomics. 2025 Jan;24(1):100893. doi: 10.1016/j.mcpro.2024.100893. Epub 2024 Dec 12.
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.
精子细胞是终末分化细胞，对于有性生殖物种的繁殖至关重要。与其高度专业化的功能相一致，精子细胞拥有独特的蛋白质组，包含许多在体细胞中不表达的蛋白质。相比之下，精子蛋白质组的翻译后格局在很大程度上仍未得到探索，这限制了我们对糖基化等修饰如何影响精子功能和精卵相互作用的理解。在此，我们使用以糖肽为中心的糖蛋白质组学全面表征了三种哺乳动物精子中的蛋白质N-糖基化，揭示了糖基化谱的明显保守性。我们发现精子蛋白质中的糖基化模式与血浆中的不同，精子中唾液酸化较少而高甘露糖基化较多，具有明显的独特特征。此外，根据其亚细胞定位，精子蛋白质糖基化有所不同，高甘露糖型糖在顶体小泡中富集，寡甘露糖型糖在精子头部膜中，而复杂聚糖型糖在顶体膜中。
