Archaeal bundling pili of Pyrobaculum calidifontis reveal similarities between archaeal and bacterial biofilms.

Archaeal bundling pili of Pyrobaculum calidifontis reveal similarities between archaeal and bacterial biofilms.
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DOI:
10.1073/pnas.2207037119
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发表时间:
2022-06-28
影响因子:
11.1
通讯作者:
--
中科院分区:
综合性期刊1区
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--
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生物膜是微生物的群落,其中细胞彼此附着以及附着到各种表面。细菌生物膜由于其在许多感染中的重要性而得到了深入的研究,而对生命的第三个领域--细菌生物膜的了解却少得多。使用低温电子显微镜,我们已经确定了表面丝,形成双极束连接古细菌细胞的原子结构。我们发现,这些捆绑皮利的主要蛋白质与已知是细菌生物膜的重要组成部分的蛋白质具有共同的祖先。这增加了我们对细菌和古细菌之间进化关系的理解,并可能为细菌生物膜提供新的见解。细菌形成的生物膜因其在致病机制中的重要性而受到广泛关注,但对古细菌形成的生物膜的研究较少。已知古细菌中的细胞外细丝,如IV型皮利、绳和套管,在古细菌生物膜的形成中起作用。我们已经使用低温电子显微镜,以确定原子结构的一个以前未知的类的古菌表面丝超嗜热Pyrobaculum calidifontis。这些纤维,我们称之为古菌束皮利(ABP),组装成高度有序的双极束。这些纤维束的双极性质很可能是由至少两个不同细胞的纤维丝联合而成的。组分蛋白AbpA在序列和结构水平上均与细菌蛋白TasA(细菌生物膜中细胞外基质的主要组分)具有同源性,有助于生物膜稳定性。我们发现,AbpA形成非常稳定的细丝的方式类似于细菌TasA纤维和伴侣引导途径皮利的供体链交换,其中一个亚基的β-链被纳入下一个亚基的β-折叠。我们的研究结果揭示了细菌和古细菌生物膜之间可能的机械相似性和进化联系,并表明可能存在许多其他尚未表征的古细菌表面细丝。
Biofilms are communities of microbes where cells attach to each other as well as to various surfaces. Bacterial biofilms have been intensively studied due to their importance in many infections, whereas much less is known about biofilms in Archaea, the third domain of life. Using cryo-electron microscopy, we have determined the atomic structure of a surface filament that forms bi-polar bundles connecting archaeal cells. We show that the major protein of these bundling pili has common ancestry with a protein known to be an important component of bacterial biofilms. This adds to our understanding of the evolutionary relationship between bacteria and archaea and may provide new insights into bacterial biofilms. While biofilms formed by bacteria have received great attention due to their importance in pathogenesis, much less research has been focused on the biofilms formed by archaea. It has been known that extracellular filaments in archaea, such as type IV pili, hami, and cannulae, play a part in the formation of archaeal biofilms. We have used cryo-electron microscopy to determine the atomic structure of a previously uncharacterized class of archaeal surface filaments from hyperthermophilic Pyrobaculum calidifontis. These filaments, which we call archaeal bundling pili (ABP), assemble into highly ordered bipolar bundles. The bipolar nature of these bundles most likely arises from the association of filaments from at least two different cells. The component protein, AbpA, shows homology, both at the sequence and structural level, to the bacterial protein TasA, a major component of the extracellular matrix in bacterial biofilms, contributing to biofilm stability. We show that AbpA forms very stable filaments in a manner similar to the donor-strand exchange of bacterial TasA fibers and chaperone-usher pathway pili where a β-strand from one subunit is incorporated into a β-sheet of the next subunit. Our results reveal likely mechanistic similarities and evolutionary connection between bacterial and archaeal biofilms, and suggest that there could be many other archaeal surface filaments that are as yet uncharacterized.
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