The adhesive property of the type IV pilus-associated component PilC1 of pathogenic Neisseria is supported by the conformational structure of the N-terminal part of the molecule
The adhesive property of the type IV pilus-associated component PilC1 of pathogenic Neisseria is supported by the conformational structure of the N-terminal part of the molecule
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DOI：
10.1046/j.1365-2958.2001.02452.x
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发表时间：
2001-05-01
影响因子：
3.6
通讯作者：
Nassif, X
中科院分区：
文献类型：
--
作者：
Morand, PC;Tattevin, P;Nassif, X
Neisserial PilC蛋白是IV型毛的生物发生和粘附的关键因子。两个pilC等位基因通常存在于脑膜炎奈瑟菌中，至少一个pilC蛋白是菌毛组装和转化能力所必需的。此外，脑膜炎球菌的PilC1而不是PilC2调节粘附性，而在淋病奈瑟菌中，两个等位基因都具有粘附性。脑膜炎球菌的pilC基因受到不同的调控，研究表明，细菌与细胞接触会短暂诱导pilC1的表达，而不是pilC2的表达。这项工作的目的是确定，除了调节外，pilc1介导的粘附是否由脑膜炎球菌PilC2蛋白中不存在的某些特定蛋白模式赋予。我们首先证明了脑膜炎球菌PilC1和PilC2初级序列的差异导致了不同的粘附表型，从而消除了转录调控是PilC1粘附表型的唯一原因。为了确定PilC1负责粘附的区域，我们设计了在PilC1位点表达各种PilC1- pilc2杂交的脑膜炎球菌菌株。我们的数据表明，特定的PilC1粘附促进区域位于分子的氨基末端部分，并且该区域内的几个结构域可能相互作用以促进对人体细胞的粘附。
Neisserial PilC proteins are key elements in type IV pili biogenesis and adhesion. Two pilC alleles are usually present in Neisseria meningitidis, At least one of the PilC proteins is required for pilus assembly and competence for transformation. In addition, meningococcal PilC1, but not PilC2, modulates adhesiveness, whereas, in N. gonorrhoeae, both alleles are adhesive. The meningococcal pilC genes are differently regulated, and it was shown that the expression of pilC1, but not that of pilC2, Is transiently induced by bacteria-cell contact. The aim of this work was to determine whether, besides regulation, PilC1-mediated adhesion was conferred by some specific protein pattern not present in the meningococcal PilC2 protein. We demonstrate first that differences within the primary sequence of the meningococcal PilC1 and PilC2 are responsible for different adhesion phenotypes, thus eliminating the regulation of transcription being solely responsible for the adhesive phenotype of PilC1. To identify the regions of PilC1 responsible for adhesion, we engineered meningococcal strains expressing various PilC1-PilC2 hybrids at the pilC1 locus. Our data demonstrate that the specific PilC1 adhesion-promoting regions are located in the amino-terminal part of the molecule and that several domains within this region probably interact with each other to promote adhesion to human cells.