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原核淀粉样蛋白在种间相互作用中的生物学功能:事实和假设。

Biological Functions of Prokaryotic Amyloids in Interspecies Interactions: Facts and Assumptions.

机构信息

Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology (ARRIAM), 196608 St. Petersburg, Russia.

Faculty of Biology, St. Petersburg State University (SPbSU), 199034 St. Petersburg, Russia.

出版信息

Int J Mol Sci. 2020 Sep 30;21(19):7240. doi: 10.3390/ijms21197240.

DOI:10.3390/ijms21197240
PMID:33008049
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7582709/
Abstract

Amyloids are fibrillar protein aggregates with an ordered spatial structure called "cross-β". While some amyloids are associated with development of approximately 50 incurable diseases of humans and animals, the others perform various crucial physiological functions. The greatest diversity of amyloids functions is identified within prokaryotic species where they, being the components of the biofilm matrix, function as adhesins, regulate the activity of toxins and virulence factors, and compose extracellular protein layers. Amyloid state is widely used by different pathogenic bacterial species in their interactions with eukaryotic organisms. These amyloids, being functional for bacteria that produce them, are associated with various bacterial infections in humans and animals. Thus, the repertoire of the disease-associated amyloids includes not only dozens of pathological amyloids of mammalian origin but also numerous microbial amyloids. Although the ability of symbiotic microorganisms to produce amyloids has recently been demonstrated, functional roles of prokaryotic amyloids in host-symbiont interactions as well as in the interspecies interactions within the prokaryotic communities remain poorly studied. Here, we summarize the current findings in the field of prokaryotic amyloids, classify different interspecies interactions where these amyloids are involved, and hypothesize about their real occurrence in nature as well as their roles in pathogenesis and symbiosis.

摘要

淀粉样蛋白是具有称为“交叉-β”的有序空间结构的纤维状蛋白质聚集体。虽然一些淀粉样蛋白与大约 50 种人类和动物不可治愈疾病的发生有关,但其他淀粉样蛋白则执行各种关键的生理功能。在原核物种中,淀粉样蛋白的功能具有最大的多样性,它们作为生物膜基质的组成部分,作为黏附素发挥作用,调节毒素和毒力因子的活性,并构成细胞外蛋白质层。淀粉样蛋白状态被不同的致病性细菌物种广泛用于与真核生物的相互作用。这些淀粉样蛋白对产生它们的细菌具有功能,与人类和动物的各种细菌感染有关。因此,与疾病相关的淀粉样蛋白的种类不仅包括数十种哺乳动物来源的病理性淀粉样蛋白,还包括许多微生物淀粉样蛋白。尽管最近已经证明了共生微生物产生淀粉样蛋白的能力,但原核淀粉样蛋白在宿主-共生体相互作用以及原核群落内种间相互作用中的功能作用仍未得到充分研究。在这里,我们总结了原核淀粉样蛋白领域的现有发现,对涉及这些淀粉样蛋白的不同种间相互作用进行分类,并假设它们在自然界中的实际存在及其在发病机制和共生关系中的作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79b2/7582709/fa05e700057e/ijms-21-07240-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79b2/7582709/fa05e700057e/ijms-21-07240-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79b2/7582709/fa05e700057e/ijms-21-07240-g001.jpg

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