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Methylation and in vivo expression of the surface-exposed Leptospira interrogans outer-membrane protein OmpL32

机译:甲基化和体内表达表面暴露的睑板瘤外膜蛋白OMPL32

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Recent studies have revealed that bacterial protein methylation is a widespread post-translational modification that is required for virulence in selected pathogenic bacteria. In particular, altered methylation of outer-membrane proteins has been shown to modulate the effectiveness of the host immune response. In this study, 2D gel electrophoresis combined with MALDI-TOF MS identified a Leptospira interrogans serovar Copenhageni strain Fiocruz L1-130 protein, corresponding to ORF LIC11848, which undergoes extensive and differential methylation of glutamic acid residues. Immunofluorescence microscopy implicated LIC11848 as a surface-exposed outer-membrane protein, prompting the designation OmpL32. Indirect immunofluorescence microscopy of golden Syrian hamster liver and kidney sections revealed expression of OmpL32 during colonization of these organs. Identification of methylated surface-exposed outer-membrane proteins, such as OmpL32, provides a foundation for delineating the role of this post-translational modification in leptospiral virulence.
机译:最近的研究表明,细菌蛋白甲基化是一种广泛的翻译后修饰,其在选定的致病细菌中所需的毒力。特别地,已经显示出外膜蛋白的改变的甲基化来调节宿主免疫应答的有效性。在本研究中,2D凝胶电泳与MALDI-TOF MS结合MS鉴定了一种leptospira interrogans Serovar Copenhageni菌株Fiocruz L1-130蛋白,其对应于ORF LIC11848,其经历了谷氨酸残基的广泛和差异甲基化。免疫荧光显微镜将LIC11848作为表面暴露的外膜蛋白,促使指定OMPL32。金叙利亚仓鼠肝脏和肾脏切片间接免疫荧光显微镜显示出在这些器官的定植过程中OMPL32的表达。甲基化的表面暴露的外膜蛋白如OMPL32的鉴定为描绘了这种翻译后修饰在钩端螺旋体毒力中的作用提供了基础。

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