Full structure/function analysis of all the pilin subunits in a type 4 pilus: a complex of minor pilins in Streptococcus sanguinis mediates binding to glycans

Full structure/function analysis of all the pilin subunits in a type 4 pilus: a complex of minor pilins in Streptococcus sanguinis mediates binding to glycans
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4 型菌毛中所有菌毛蛋白亚基的完整结构/功能分析:血链球菌中的次要菌毛蛋白复合物介导与聚糖的结合

DOI:
10.1101/2022.08.25.505150
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发表时间:
2022
期刊:
--
影响因子:
--
通讯作者:
Shahin M
Shahin M
中科院分区:
--
文献类型:
--
作者:
Shahin M

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4型丝(T4F)——其中4型毛(T4P)是原型——是丝状纳米机器的超家族,在原核生物中几乎无处不在。T4F是由一种主要支柱组成的聚合物,它还含有次要支柱,这些次要支柱的作用通常鲜为人知。在此,我们完成了机会致病菌血链球菌中全套T4P蛋白的结构/功能分析。我们确定了小柱状蛋白PilA的结构,它出乎意料地与T4F中广泛保守的四个小柱状蛋白顶端复合物的一个亚基相似。我们发现PilA相互作用并显著稳定了次要的PilC。我们确定了PilC的结构,表明它是一种模块化的pilin,具有凝集素模块,结合人类糖原中普遍存在的特定聚糖子集,即s的宿主。杂志。总之,我们的研究结果支持一个模型,即次要的支柱。sanguinisT4P形成一个位于尖端的复合体,促进与各种宿主受体的粘附。我们的研究结果对T4F中广泛保守的一组次要支柱具有一般意义。
Type 4 filaments (T4F) – of which type 4 pili (T4P) are the archetype – are a superfamily of filamentous nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin that 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 pathogenStreptococcus 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 stabilises the minor pilin PilC. We determined the structure of PilC, showing that it is a modular pilin with a lectin module binding a specific subset of glycans prevalent in the human glycome, the host ofS. sanguinis. Altogether, our findings support a model whereby the minor pilins inS. sanguinisT4P form a tip-located complex promoting adhesion to various host receptors. Our findings have general implications for a group of minor pilins widely conserved in T4F.
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