O-linked protein glycosylation in Mycoplasma.
O-linked protein glycosylation in Mycoplasma.
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DOI：
10.1111/mmi.12415
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发表时间：
2013-12
影响因子：
3.6
通讯作者：
Dybvig K
中科院分区：
文献类型：
--
作者：
Jordan DS;Daubenspeck JM;Laube AH;Renfrow MB;Dybvig K
虽然支原体缺乏生物信息学可识别的糖基转移酶和核苷酸转移酶，但已知这些细菌可以产生多糖和糖脂。我们在这里表明，支原体也产生糖蛋白，因此糖蛋白比以前认识到的更复杂。几种支原体的蛋白质与糖蛋白染色反应，并选择小鼠病原体关节炎支原体进行进一步研究。高分辨率质谱法证实了关节炎支原体糖蛋白的存在。在丝氨酸和苏氨酸残基上都清楚地发现了o链糖基化。糖蛋白的糖基化位点没有一致的氨基酸序列。单个己糖被鉴定为o链修饰，葡萄糖通过13C标记推断为几个糖基化位点的己糖。这是第一个最终确定任何分子中蛋白质糖基化位点的研究。
Although mycoplasmas have a paucity of glycosyltransferases and nucleotidyltransferases recognizable by bioinformatics, these bacteria are known to produce polysaccharides and glycolipids. We show here that mycoplasmas also produce glycoproteins and hence have glycomes more complex than previously realized. Proteins from several species of Mycoplasma reacted with a glycoprotein stain, and the murine pathogen Mycoplasma arthritidis was chosen for further study. The presence of M. arthritidis glycoproteins was confirmed by high-resolution mass spectrometry. O-linked glycosylation was clearly identified at both serine and threonine residues. No consensus amino acid sequence was evident for the glycosylation sites of the glycoproteins. A single hexose was identified as the O-linked modification, and glucose was inferred by 13C labeling to be the hexose at several of the glycosylation sites. This is the first study to conclusively identify sites of protein glycosylation in any of the mollicutes.