Characterization of a glycan-binding complex of minor pilins completes the analysis of Streptococcus sanguinis type 4 pili subunits.

Characterization of a glycan-binding complex of minor pilins completes the analysis of Streptococcus sanguinis type 4 pili subunits.
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DOI:
10.1073/pnas.2216237120
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发表时间:
2023-01-17
影响因子:
11.1
通讯作者:
Pelicic, Vladimir
Pelicic, Vladimir
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Shahin, Meriam;Sheppard, Devon;Raynaud, Claire;Berry, Jamie-Lee;Gurung, Ishwori;Silva, Lisete M.;Feizi, Ten;Liu, Yan;Pelicic, Vladimir

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4型皮利(T4 P)-在细菌病原体中很重要-是由一个特征明确的主要菌毛蛋白和几个次要菌毛蛋白组成的细丝,其作用通常知之甚少。血链球菌T4 P由五种菌毛蛋白组成,这使得它成为详细确定每个菌毛蛋白亚基的作用的良好模型。在这里,我们描述了PilA和PilC的特征,展示了它们如何相互作用以及它们如何发挥作用。结合我们以前的研究结果,这提供了一个完整的观点,在S。血吸虫T4 P PilE 1/PilE 2是形成丝状体骨架的主要菌毛蛋白,而三种次要菌毛蛋白(PilA、PilB和PilC)形成促进与各种宿主受体粘附的尖端定位复合物。4型丝(T4 F)-其中4型皮利(T4 P)是原型-是几乎普遍存在于原核生物中的纳米机器的超家族。T4 F是一种主要菌毛蛋白的聚合物,其还含有次要菌毛蛋白,其作用通常知之甚少。在这里,我们完成了一套完整的T4 P菌毛蛋白的结构/功能分析的机会致病菌血链球菌。我们确定了次要菌毛蛋白PilA的结构,这是出乎意料的类似于一个尖端定位的复杂的四个次要菌毛蛋白,广泛保守的T4 F的亚基之一。我们发现,PilA相互作用,并显着稳定的次要菌毛蛋白PilC。我们确定了PilC的结构,表明它是一种模块化的菌毛蛋白,其凝集素模块结合人糖组中普遍存在的聚糖子集,S。吸血鬼总之,我们的研究结果支持了一个模型,即在S。血T4 P形成尖端定位复合物,促进与各种宿主受体的粘附。这对T4 F具有普遍意义。
Type 4 pili (T4P)—important in bacterial pathogens—are filaments composed of one well-characterized major pilin, and several minor pilins whose roles are often poorly understood. Streptococcus sanguinis T4P are composed of five pilins, which makes it a good model to determine the role of each pilin subunit in detail. Here, we characterize PilA and PilC, showing how they interact and how they function. Together with our previous findings, this provides an integrated view of the role of the five pilin subunits in S. sanguinis T4P. PilE1/PilE2 are the major pilins forming the backbone of the filament, while the three minor pilins (PilA, PilB, and PilC) form a tip-located complex promoting adhesion to various host receptors. Type 4 filaments (T4F)—of which type 4 pili (T4P) are the archetype—are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we complete the structure/function analysis of the full set of T4P pilins in the opportunistic bacterial pathogen Streptococcus sanguinis. We determined the structure of the minor pilin PilA, which is unexpectedly similar to one of the subunits of a tip-located complex of four minor pilins, widely conserved in T4F. We found that PilA interacts and dramatically stabilizes the minor pilin PilC. We determined the structure of PilC, showing that it is a modular pilin with a lectin module binding a subset of glycans prevalent in the human glycome, the host of S. sanguinis. Altogether, our findings support a model whereby the minor pilins in S. sanguinis T4P form a tip-located complex promoting adhesion to various host receptors. This has general implications for T4F.
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发表时间: 2016-03-11
期刊: Science (New York, N.Y.)
影响因子: --
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发表时间: 2013-02-19
影响因子: 11.1
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DOI: 10.1107/s0907444909042073
发表时间: 2010-01
期刊: Acta crystallographica. Section D, Biological crystallography
影响因子: --
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