PilB from Streptococcus sanguinis is a bimodular type IV pilin with a direct role in adhesion.
PilB from Streptococcus sanguinis is a bimodular type IV pilin with a direct role in adhesion.
复制标题
来自Sanguinis链球菌的PILB是一种双性异的IV型PILIN，在粘附中具有直接作用。
DOI：
10.1073/pnas.2102092118
复制
发表时间：
2021-06-01
影响因子：
11.1
通讯作者：
Pelicic V
中科院分区：
文献类型：
--
作者：
Raynaud C;Sheppard D;Berry JL;Gurung I;Pelicic V
IV型皮利（T4 P）是广泛存在于原核生物中的功能多样的丝状体，由IV型菌毛蛋白组成，并通过保守的多蛋白机制组装。目前尚不清楚这种相当简单的细丝如何如此多才多艺。我们对血链球菌T4 P的一种次要菌毛蛋白PilB的结构/功能分析为这一悖论提供了一个优雅的解释。我们发现PilB是一个模块化的菌毛蛋白，一个大的模块“嫁接”到一个小的菌毛蛋白模块上，它直接介导S。sanguinis宿主细胞/蛋白质。这种进化的修补策略似乎在细菌中很普遍，因为全球分析显示，模块化菌毛蛋白广泛存在，并表现出惊人的各种架构。IV型皮利（T4 P）是功能多样的丝状纳米机器，在原核生物中几乎普遍存在。它们主要是一种主要菌毛蛋白的聚合物，但也含有功能通常不明确且可能多种多样的次要菌毛蛋白。在这里，我们表明，次要的菌毛PilB从血链球菌的T4 P显示一个不寻常的双模块的三维结构与庞大的冯维勒布兰德因子A样（vWA）模块“嫁接”到一个小的菌毛模块通过一个短循环。结构建模表明PilB仅与T4 P尖端的定位相容。通过详细的功能分析，我们发现1）vWA模块包含一个典型的金属离子依赖性粘附位点，优先结合Mg ~（2+）和Mn ~（2+），2）取消金属结合对PilB结构或纤毛没有影响，3）金属结合对S.血T4 P介导的抽搐运动性和对真核细胞的粘附，以及4）vWA模块显示出对几种宿主蛋白质的内在结合能力。这些发现揭示了一种优雅而简单的进化修补策略，通过将功能模块嫁接到菌毛蛋白上由细丝呈现来增加T4 P功能的多样性。这种策略似乎已被细菌广泛使用，其中模块化菌毛蛋白广泛存在，并表现出惊人的各种架构。
Type IV pili (T4P) are functionally versatile filaments widespread in prokaryotes, composed of type IV pilins and assembled by conserved multiprotein machineries. It remains unclear how such rather simple filaments can be so versatile. Our structure/function analysis of PilB, a minor pilin of Streptococcus sanguinis T4P, offers an elegant explanation for this paradox. We show that PilB is a modular pilin with a bulky module “grafted” onto a small pilin module, which directly mediates adhesion of S. sanguinis to host cells/proteins. This evolutionary tinkering strategy appears to be prevalent in bacteria since a global analysis reveals that modular pilins are widespread and exhibit an astonishing variety of architectures. Type IV pili (T4P) are functionally versatile filamentous nanomachines, nearly ubiquitous in prokaryotes. They are predominantly polymers of one major pilin but also contain minor pilins whose functions are often poorly defined and likely to be diverse. Here, we show that the minor pilin PilB from the T4P of Streptococcus sanguinis displays an unusual bimodular three-dimensional structure with a bulky von Willebrand factor A–like (vWA) module “grafted” onto a small pilin module via a short loop. Structural modeling suggests that PilB is only compatible with a localization at the tip of T4P. By performing a detailed functional analysis, we found that 1) the vWA module contains a canonical metal ion–dependent adhesion site, preferentially binding Mg2+ and Mn2+, 2) abolishing metal binding has no impact on the structure of PilB or piliation, 3) metal binding is important for S. sanguinis T4P–mediated twitching motility and adhesion to eukaryotic cells, and 4) the vWA module shows an intrinsic binding ability to several host proteins. These findings reveal an elegant yet simple evolutionary tinkering strategy to increase T4P functional versatility by grafting a functional module onto a pilin for presentation by the filaments. This strategy appears to have been extensively used by bacteria, in which modular pilins are widespread and exhibit an astonishing variety of architectures.
登录
查看更多内容
DOI：
10.1126/science.aad2001
发表时间：
2016-03-11
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Chang YW;Rettberg LA;Treuner-Lange A;Iwasa J;Søgaard-Andersen L;Jensen GJ
通讯作者：
Jensen GJ
影响因子：
6.7
作者：
Hilleringmann M;Giusti F;Baudner BC;Masignani V;Covacci A;Rappuoli R;Barocchi MA;Ferlenghi I
通讯作者：
Ferlenghi I
影响因子：
5.7
作者：
Izore, Thierry;Contreras-Martel, Carlos;Dessen, Andrea
通讯作者：
Dessen, Andrea
影响因子：
5.6
作者：
Kawahara, Kazuki;Oki, Hiroya;Nakamura, Shota
通讯作者：
Nakamura, Shota
影响因子：
3.7
作者：
Johnson MD;Garrett CK;Bond JE;Coggan KA;Wolfgang MC;Redinbo MR
通讯作者：
Redinbo MR