Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization
Deletion of the Cytophaga hutchinsonii type IX secretion system gene sprP results in defects in gliding motility and cellulose utilization
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DOI：
10.1007/s00253-013-5355-2
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发表时间：
2013-11
影响因子：
5
通讯作者：
Yongtao Zhu;M. McBride
中科院分区：
文献类型：
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作者：
Yongtao Zhu;M. McBride
噬细胞菌 hutchinsoniiglaga 在表面快速滑动，并采用细胞相关蛋白的新型集合来消化结晶纤维素。HimarEm1 转座子诱变用于分离带有 CHU_0170(sprP) 插入的突变体，该突变体部分缺乏滑动运动性，无法消化滤纸纤维素。 SprP 与牙龈卟啉单胞菌 IX 型分泌系统 (T9SS) 蛋白 PorP（参与牙龈蛋白酶毒力因子的分泌）和约氏黄杆菌 T9SS 蛋白 SprF（将滑动运动机制的成分递送至细胞表面所需）相似。我们开发了一种有效的方法来构建 C 中的靶向非极性突变。哈钦森和删除的 prP。缺失突变体存在滑动缺陷并且不能消化纤维素，与sprPon质粒的互补恢复了这两种能力。序列分析预测CHU_3105是由T9SS分泌的，spr的缺失导致胞外CHU_3105水平下降。结果表明SprP可能在蛋白质分泌中发挥作用。 T9SS 可能是运动和纤维素利用所必需的，因为预计参与这两个过程的细胞表面蛋白具有 C 末端结构域，这些结构域被认为将它们靶向该分泌系统。现在可用于 C 的有效遗传工具。哈钦森应该能够对这种常见但知之甚少的细菌的纤维素分解、滑动运动和蛋白质分泌机制进行详细分析。
Cytophaga hutchinsoniiglides rapidly over surfaces and employs a novel collection of cell-associated proteins to digest crystalline cellulose.HimarEm1transposon mutagenesis was used to isolate a mutant with an insertion inCHU_0170(sprP) that was partially deficient in gliding motility and was unable to digest filter paper cellulose. SprP is similar in sequence to thePorphyromonas gingivalistype IX secretion system (T9SS) protein PorP that is involved in the secretion of gingipain protease virulence factors and to theFlavobacterium johnsoniaeT9SS protein SprF that is needed to deliver components of the gliding motility machinery to the cell surface. We developed an efficient method to construct targeted nonpolar mutations inC. hutchinsoniiand deletedsprP. The deletion mutant was defective in gliding and failed to digest cellulose, and complementation withsprPon a plasmid restored both abilities. Sequence analysis predicted that CHU_3105 is secreted by the T9SS, and deletion ofsprPresulted in decreased levels of extracellular CHU_3105. The results suggest that SprP may function in protein secretion. The T9SS may be required for motility and cellulose utilization because cell surface proteins predicted to be involved in both processes have C-terminal domains that are thought to target them to this secretion system. The efficient genetic tools now available forC. hutchinsoniishould allow a detailed analysis of the cellulolytic, gliding motility, and protein secretion machineries of this common but poorly understood bacterium.