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首页> 外文期刊>Journal of bacteriology >Characterization of a Mycoplasma pneumoniae hmw3 Mutant: Implications for Attachment Organelle Assembly
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Characterization of a Mycoplasma pneumoniae hmw3 Mutant: Implications for Attachment Organelle Assembly

机译：肺炎支原体hmw3突变体的表征：对附件细胞器大会的影响。

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The proteins required for adherence of the pathogen Mycoplasma pneumoniae to host respiratory epithelial cells are localized to a polar structure, the attachment organelle. A number of these proteins have been characterized functionally by analysis of noncytadhering mutants, and many are components of the mycoplasma cytoskeleton. Mutations in some cytadherence-associated proteins have pleiotropic effects, including decreased stability of other proteins, loss of adherence and motility, and abnormal morphology. The function of protein HMW3, a component of the attachment organelle, has been difficult to discern due to lack of an appropriate mutant. In this paper, we report that loss of HMW3 resulted in decreased levels and more diffuse localization of cytoskeletal protein P65, subtle changes in morphology, inability to cluster the adhesin P1 consistently at the terminal organelle, reduced cytadherence, and, in some cells, an atypical electron-dense core in the attachment organelle. This phenotype suggests a role for HMW3 in the architecture and stability of the attachment organelle.
机译：病原体肺炎支原体粘附于宿主呼吸道上皮细胞所需的蛋白质位于一个极性结构，即附着细胞器。这些蛋白质中的许多已经通过非细胞粘附突变体的分析进行了功能鉴定，其中许多是支原体细胞骨架的组成部分。某些与细胞粘附相关的蛋白质中的突变具有多效性，包括其他蛋白质的稳定性下降，粘附性和运动性丧失以及形态异常。由于缺乏合适的突变体，难以识别蛋白质HMW3（附着细胞器的一个组成部分）的功能。在本文中，我们报道了HMW3的缺失导致细胞骨架蛋白P65的水平降低和扩散更加分散，形态上的细微变化，无法在终末细胞器上一致地粘附粘附素P1，减少了细胞黏附，并且在某些细胞中，附着细胞器中的非典型电子致密核。该表型表明HMW3在附着细胞器的结构和稳定性中的作用。

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