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Global characterization of mouse testis O-glycoproteome landscape during spermatogenesis

Author

Listed:
  • Qiannan Liu

    (Shanghai Jiao Tong University)

  • Xiaoyan Lu

    (Shanghai Jiao Tong University)

  • Yao Deng

    (Shanghai Jiao Tong University)

  • Han Zhang

    (Shanghai Jiao Tong University)

  • Rumeng Wei

    (Shanghai Jiao Tong University)

  • Hongrui Li

    (Shanghai Jiao Tong University)

  • Ying Feng

    (Sichuan University)

  • Juan Wei

    (Shanghai Jiao Tong University)

  • Fang Ma

    (Sichuan University)

  • Yan Zhang

    (Shanghai Jiao Tong University)

  • Xia Zou

    (Shanghai Jiao Tong University)

Abstract

Protein O-glycosylation plays critical roles in sperm formation and maturation. However, detailed knowledge on the mechanisms involved is limited due to lacking characterization of O-glycoproteome of testicular germ cells. Here, we performed a systematic analysis of site-specific O-glycosylation in mouse testis, and established an O-glycoproteome map with 349 O-glycoproteins and 799 unambiguous O-glycosites. Moreover, we comprehensively investigated the distribution properties of O-glycosylation in testis and identified a region near the N-terminal of peptidase S1 domain that is susceptible to O-glycosylation. Interestingly, we found dynamic changes with an increase Tn and a decrease T structure from early to mature developmental stages. Notably, the importance of O-glycosylation was supported by its effects on the stability, cleavage, and interaction of acrosomal proteins. Collectively, these data illustrate the global properties of O-glycosylation in testis, providing insights and resources for future functional studies targeting O-glycosylation dysregulation in male infertility.

Suggested Citation

  • Qiannan Liu & Xiaoyan Lu & Yao Deng & Han Zhang & Rumeng Wei & Hongrui Li & Ying Feng & Juan Wei & Fang Ma & Yan Zhang & Xia Zou, 2025. "Global characterization of mouse testis O-glycoproteome landscape during spermatogenesis," Nature Communications, Nature, vol. 16(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57980-7
    DOI: 10.1038/s41467-025-57980-7
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