期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 100, 期 26, 页码 15631-15636出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2635507100
关键词
-
资金
- NICHD NIH HHS [R01 HD035652, HD 35652] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
Murine sperm initiate fertilization by binding to the outer covering of the egg known as the murine zona pellucida (mZP). This binding is thought to require the interaction of O-glycans linked to a specific mZP glycoprotein (mZP3) with egg-binding proteins coating the sperm plasma membrane. The precise molecular basis of this interaction remains to be resolved. In this study, we analyzed the O-glycosylation of the individual mZP glycoproteins by using ultrasensitive MS methods. We found that the majority of the O-glycans that are linked to mZP3 are core type 2 sequences terminated with sialic acid, lacNAc (Galbeta1-4GlcNAc), lacdiNAc (GalNAcbeta1-4GIcNAc), Galalpha1-31Gal, and NeuAcalpha2-3[GalNAcbeta1-4]Galbeta1-4 (Sd(a) antigen). Many of these terminal sequences have been implicated previously in murine sperm-egg binding. Core type 1 O-glycans are also present and are generally unmodified, although some are terminated with sialic acid, P-linked N-acetylhexosamine, or NeuAcalpha2-3[GalNAcbeta1-4]Galbeta1-4. Eggs expressing human ZP (huZP) glycoprotein huZP3, derived from transgenic mice, bind murine but not human sperm, implying that huZP3 acquires the same O-glycans as native mZP3. Sequencing of huZP3-associated O-glycans confirms that this implication is correct. The data obtained in this investigation may prove to be very useful for studies to determine the precise molecular basis of initial murine sperm-egg binding.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据