• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>RSC Advances >O-GlcNAcylation confers protection against Staphylococcus aureus infection in Caenorhabditis elegans through ubiquitination
【24h】

O-GlcNAcylation confers protection against Staphylococcus aureus infection in Caenorhabditis elegans through ubiquitination

机译：o-glcnacylation通过泛素化赋予Caenorhabdise elegans的金黄色葡萄球菌感染保护

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Glycosylation is one of the most prevalent post-translational modifications in biological systems. In Caenorhabditis elegans, O-GlcNAcylation has been shown to be actively involved in the regulation of dauer formation and detoxification of toxins secreted by invading pathogens. On this backdrop, the present study is focused on understanding the role of O-GlcNAcylation in C. elegans during Staphylococcus aureus infection using a gel based proteomic approach. Results of time course killing assays with wild-type and mutants of glycosylation and comparison of results revealed an increase in the survival of the C. elegans oga-1 mutant when compared to wild-type N2 and the ogt-1 mutant. Increased survival of C. elegans N2 upon S. aureus infection in the presence of O-(2-acetamido-2-deoxy-d-glucopyranosylidenamino) N-phenylcarbamate (PUGNAc-an OGA inhibitor) further confirmed the involvement of O-GlcNAcylation in protecting C. elegans from infection. The two-dimensional gel-based proteomic analysis of the control and S. aureus infected C. elegans oga-1 mutant followed by mass spectrometric identification of differentially expressed proteins has been carried out. The results revealed that key proteins involved in ubiquitination such as Cullin-1 (CUL-1), Cullin-3 (CUL-3), BTB and MATH domain-containing protein 15 (BATH-15), ubiquitin-conjugating enzyme E2 variant 3 (UEV-3) and probable ubiquitin-conjugating enzyme E2 7 (UBC-7) are upregulated. Real-time PCR analysis further confirms the upregulation of genes encoding the above-mentioned proteins which are involved in the ubiquitin-mediated pathways in C. elegans. In addition, treatment of C. elegans wild-type N2 and the oga-1 mutant with PUGNAc + suramin and suramin (an ubiquitination inhibitor), respectively has resulted in increased sensitivity to S. aureus infection. Hence, it is presumed that upregulation of proteins involved in the ubiquitination pathway could be the key regulatory mechanism responsible for the enhanced survival of the oga-1 mutant during S. aureus infection.
机译：糖基化是生物系统中最普遍的翻译后修饰之一。在Caenorhabditis的秀丽隐杆线上，已经表明O-Glcnacylation积极参与通过入侵病原体分泌的Dauer形成和毒素的解毒。在这种背景上，本研究重点是在使用基于凝胶的蛋白质组学方法的葡萄球菌感染期间理解O-Glcnacylation在C.杆状乐菌中的作用。与糖基化的野生型和突变体杀死测定的时间路径结果和结果的比较显示，与野生型N 2和OGT-1突变体相比，秀丽隐杆线虫oga-1突变体的存活率增加。在O-（2-乙酰氨基-2-脱氧-3-d-glucopyranosylidenamino）N-苯基氨基甲酸酯（PUGNAC-的OGA抑制剂）的存在下在金黄色葡萄球菌感染增加线虫N2的生存进一步证实O型GlcNAc糖基中的参与保护杆状杆菌免受感染。进行了对照的二维凝胶的蛋白质组学分析，对照感染的C.秀丽杆菌OGA-1突变体，随后进行了差异表达蛋白质的质谱鉴定。结果表明，泛素化的关键蛋白如Cullin-1（CUL-1），Cullin-3（CUL-3），BTB和含数学域蛋白15（浴-15），泛素缀合酶E2变体3 （UEV-3）和可能的泛素缀合酶E2 7（UBC-7）被上调。实时PCR分析进一步证实编码涉及乌比杆菌的泛素介导的途径中上述蛋白质的基因的上调。此外，分别处理C.秀丽隐杆线虫野生型N2和oga-1突变体，分别导致对金黄色葡萄球菌感染的敏感性增加。因此，推测遍及泛素化途径中涉及的蛋白质的上调可能是负责在核桃感染期间增强OGA-1突变体的存活的关键调节机制。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号