Structure/function analysis of Neisseria meningitidis PilW, a conserved protein that plays multiple roles in type IV pilus biology.
Structure/function analysis of Neisseria meningitidis PilW, a conserved protein that plays multiple roles in type IV pilus biology.
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脑膜炎奈瑟菌 PilW 的结构/功能分析，这是一种在 IV 型菌毛生物学中发挥多种作用的保守蛋白。
DOI：
10.1128/iai.05313-11
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发表时间：
2011
影响因子：
3.1
通讯作者：
Szeto TH
中科院分区：
文献类型：
--
作者：
Szeto TH
IV型皮利（Tfp）是广泛存在的丝状细菌细胞器，其介导多种功能，并在包括脑膜炎奈瑟氏菌在内的几种重要人类病原体的发病机制中发挥关键作用。Tfp生物学在分子水平上仍然知之甚少，因为参与其中的许多蛋白质的作用仍然大多不清楚。根据我们最近报道的N.脑膜炎球菌PilW是一种广泛保守的Tfp生物合成所必需的蛋白质，我们通过定点诱变靶向一系列关键残基并使用一系列表型测定分析相应的变体来进行结构/功能分析。在这里，我们表明，PilW的参与功能的TFP可以从遗传上解偶联其并行的作用，通过该TFP出现在细菌表面上的分泌素通道的组装/稳定。这些发现表明PilW是一种多功能蛋白。
Type IV pili (Tfp) are widespread filamentous bacterial organelles that mediate multiple functions and play a key role in pathogenesis in several important human pathogens, including Neisseria meningitidis. Tfp biology remains poorly understood at a molecular level because the roles of the numerous proteins that are involved remain mostly obscure. Guided by the high-resolution crystal structure we recently reported for N. meningitidis PilW, a widely conserved protein essential for Tfp biogenesis, we have performed a structure/function analysis by targeting a series of key residues through site-directed mutagenesis and analyzing the corresponding variants using an array of phenotypic assays. Here we show that PilW's involvement in the functionality of Tfp can be genetically uncoupled from its concurrent role in the assembly/stabilization of the secretin channels through which Tfp emerge on the bacterial surface. These findings suggest that PilW is a multifunctional protein.