Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen
Heavy fucosylation (fucose residues ≥ 6 per glycan) has been previously reported in human semen with unclear precise site-specific glycan structures. In current study, we characterized heavily fucosylated glycoproteins as a distinctive feature of human spermatozoa (HS) and seminal plasma (HSP), with...
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2025-09-01
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| Series: | Carbohydrate Polymer Technologies and Applications |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666893925002828 |
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| author | Miaomiao Xin Yintai Xu Shanshan You Cheng Li Jiechen Shen Bojing Zhu Qiaohong Zhao Juanzi Shi Shisheng Sun |
| author_facet | Miaomiao Xin Yintai Xu Shanshan You Cheng Li Jiechen Shen Bojing Zhu Qiaohong Zhao Juanzi Shi Shisheng Sun |
| author_sort | Miaomiao Xin |
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| description | Heavy fucosylation (fucose residues ≥ 6 per glycan) has been previously reported in human semen with unclear precise site-specific glycan structures. In current study, we characterized heavily fucosylated glycoproteins as a distinctive feature of human spermatozoa (HS) and seminal plasma (HSP), with a precise definition of glycan structural features at the glycosite-specific level. There were 49 unique heavily fucosylated intact glycopeptides (IGPs) at 15 N-glycosites from 12 glycoproteins identified in HS, and 188 unique heavily fucosylated IGPs at 58 N-glycosites from 37 glycoproteins in HSP. Among these heavily fucosylated glycoproteins, 10 were shared in HS and HSP, 2 were detected only in HS and 17 only in HSP. Almost all heavily fucosylated glycans were complex N-glycans with core fucosylation and Lewis antennary, among which CLU were glycosylated by ten and nine fucoses per glycan in HS and HSP, respectively. Moreover, these heavily fucosylated glycans varied from tri- to hexa-antennas. Notably, the N-glycan structures on shared heavily fucosylated glycoproteins were more complex in HSP than in HS. These heavily fucosylated glycoproteins identified in human semen represent a valuable and distinctive resource for glycopeptide studies, offering significant potential for advancing glycoproteomic methodologies and clinical research into male infertility. |
| format | Article |
| id | doaj-art-36c69d438a734e2cb52bf5a882b84aba |
| institution | Kabale University |
| issn | 2666-8939 |
| language | English |
| publishDate | 2025-09-01 |
| publisher | Elsevier |
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| series | Carbohydrate Polymer Technologies and Applications |
| spelling | doaj-art-36c69d438a734e2cb52bf5a882b84aba2025-08-20T03:50:58ZengElsevierCarbohydrate Polymer Technologies and Applications2666-89392025-09-011110094110.1016/j.carpta.2025.100941Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semenMiaomiao Xin0Yintai Xu1Shanshan You2Cheng Li3Jiechen Shen4Bojing Zhu5Qiaohong Zhao6Juanzi Shi7Shisheng Sun8The Assisted Reproduction Center, Northwest Women’s and Children’s Hospital, Xi’an, Shaanxi 710003, PR China; Laboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi 710069, PR China; Faculty of Fisheries and Protection of Waters, University of South Bohemia in Ceske Budejovice, Vodnany, 38925, Czech RepublicLaboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi 710069, PR ChinaResearch Center for the Qinling Giant Panda (Shaanxi Rare Wildlife Rescue Base), Shaanxi Academy of Forestry Sciences, Xi’an, Shaanxi 710402, PR ChinaLaboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi 710069, PR ChinaLaboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi 710069, PR ChinaLaboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi 710069, PR ChinaThe Assisted Reproduction Center, Northwest Women’s and Children’s Hospital, Xi’an, Shaanxi 710003, PR ChinaThe Assisted Reproduction Center, Northwest Women’s and Children’s Hospital, Xi’an, Shaanxi 710003, PR China; Corresponding authors.Laboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi’an, Shaanxi 710069, PR China; Corresponding authors.Heavy fucosylation (fucose residues ≥ 6 per glycan) has been previously reported in human semen with unclear precise site-specific glycan structures. In current study, we characterized heavily fucosylated glycoproteins as a distinctive feature of human spermatozoa (HS) and seminal plasma (HSP), with a precise definition of glycan structural features at the glycosite-specific level. There were 49 unique heavily fucosylated intact glycopeptides (IGPs) at 15 N-glycosites from 12 glycoproteins identified in HS, and 188 unique heavily fucosylated IGPs at 58 N-glycosites from 37 glycoproteins in HSP. Among these heavily fucosylated glycoproteins, 10 were shared in HS and HSP, 2 were detected only in HS and 17 only in HSP. Almost all heavily fucosylated glycans were complex N-glycans with core fucosylation and Lewis antennary, among which CLU were glycosylated by ten and nine fucoses per glycan in HS and HSP, respectively. Moreover, these heavily fucosylated glycans varied from tri- to hexa-antennas. Notably, the N-glycan structures on shared heavily fucosylated glycoproteins were more complex in HSP than in HS. These heavily fucosylated glycoproteins identified in human semen represent a valuable and distinctive resource for glycopeptide studies, offering significant potential for advancing glycoproteomic methodologies and clinical research into male infertility.http://www.sciencedirect.com/science/article/pii/S2666893925002828Heavy fucosylationSite-specific glycan structuresSpermatozoaSeminal plasmaMass spectrometry |
| spellingShingle | Miaomiao Xin Yintai Xu Shanshan You Cheng Li Jiechen Shen Bojing Zhu Qiaohong Zhao Juanzi Shi Shisheng Sun Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen Carbohydrate Polymer Technologies and Applications Heavy fucosylation Site-specific glycan structures Spermatozoa Seminal plasma Mass spectrometry |
| title | Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen |
| title_full | Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen |
| title_fullStr | Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen |
| title_full_unstemmed | Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen |
| title_short | Structural and site-specific characterization of distinctive N-glycans with heavy fucosylation in human semen |
| title_sort | structural and site specific characterization of distinctive n glycans with heavy fucosylation in human semen |
| topic | Heavy fucosylation Site-specific glycan structures Spermatozoa Seminal plasma Mass spectrometry |
| url | http://www.sciencedirect.com/science/article/pii/S2666893925002828 |
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