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首页> 外文期刊>RSC Advances >O-GlcNAcylation confers protection against Staphylococcus aureus infection in Caenorhabditis elegans through ubiquitination
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O-GlcNAcylation confers protection against Staphylococcus aureus infection in Caenorhabditis elegans through ubiquitination

机译：O-GlcNAcylation通过泛素化赋予秀丽隐杆线虫抗金黄色葡萄球菌感染的保护

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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。在秀丽隐杆线虫中，已证明O-GlcNAcylation积极参与了dauer形成和入侵病原体分泌的毒素排毒的调节。在这种背景下，本研究着重于使用基于凝胶的蛋白质组学方法了解O-GlcNAcylation在秀丽隐杆线虫感染金黄色葡萄球菌期间的作用。用野生型和糖基化突变体进行时程杀灭测定的结果以及结果的比较表明，与野生型N2和ogt-1突变体相比，秀丽隐杆线虫oga-1突变体的存活率提高了。在存在O-（2-乙酰氨基-2-脱氧-D-吡喃葡萄糖基乙二酰胺）N-苯基氨基甲酸酯（PUGNAc-OGA抑制剂）的情况下，金黄色葡萄球菌感染后秀丽隐杆线虫N2的存活增加，进一步证实了O-GlcNAcylation参与了保护线虫免受感染。已对对照和金黄色葡萄球菌感染的秀丽隐杆线虫oga-1突变体进行了基于凝胶的二维蛋白质组分析，然后通过质谱鉴定了差异表达的蛋白质。结果显示，涉及泛素化的关键蛋白如Cullin-1（CUL-1），Cullin-3（CUL-3），BTB和含MATH结构域的蛋白15（BATH-15），泛素结合酶E2变体3 （UEV-3）和可能的泛素结合酶E2 7（UBC-7）被上调。实时PCR分析进一步证实了编码上述蛋白的基因的上调，这些蛋白与秀丽隐杆线虫的遍在蛋白介导的途径有关。另外，用PUGNAc +苏拉明和苏拉明（泛素化抑制剂）分别处理秀丽隐杆线虫野生型N2和oga-1突变体对金黄色葡萄球菌感染的敏感性增加。因此，可以推测参与泛素化途径的蛋白质的上调可能是导致金黄色葡萄球菌感染期间oga-1突变体存活时间延长的关键调控机制。

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