Nanobdellati(原 DPANN)古菌及其宿主中的 N-连接的蛋白质糖基化。

IF 2.7 3区 生物学 Q3 MICROBIOLOGY
Journal of Bacteriology Pub Date : 2024-09-19 Epub Date: 2024-08-28 DOI:10.1128/jb.00205-24
Satoshi Nakagawa, Hiroyuki D Sakai, Shigeru Shimamura, Yoshiki Takamatsu, Shingo Kato, Hirokazu Yagi, Saeko Yanaka, Maho Yagi-Utsumi, Norio Kurosawa, Moriya Ohkuma, Koichi Kato, Ken Takai
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引用次数: 0

摘要

Nanobdellati 王国的成员以前被称为 DPANN 古菌,其特点是细胞体积超小,基因组缩小。它们主要通过在不同环境中与特定宿主的外共生相互作用而繁衍生息。最近的成功培养强调了与宿主细胞的粘附对于了解纳米贝氏菌生态生理学的重要性。细胞粘附通常由细胞表面碳水化合物介导,而在古细菌中,细胞表面通常包裹的糖基化 S 层蛋白可能会促进细胞粘附。在本研究中,我们对两种共培养的纳米贝藻及其宿主古细菌以及宿主和非宿主古细菌的纯培养物进行了糖蛋白组学分析。Nanobdellati 表现出各种糖蛋白,包括古细菌蛋白和假定蛋白,其糖蛋白的结构与宿主的不同。这表明,尽管能量成本很高,但纳诺贝拉蒂可能利用宿主衍生的底物自主合成用于修饰蛋白质的聚糖。Nanobdellati蛋白质上的糖修饰始终发生在N-X-S/T序列内的天冬酰胺残基上,这与在古生菌、细菌和真核生物中观察到的模式一致。在宿主和非宿主古细菌中,S 层蛋白质通常由己糖、N-乙酰己糖胺和磺化脱氧己糖修饰。然而,宿主古细菌的 N-糖结构具有不同的糖,如脱氧己糖、壬磺酸糖和非还原末端的戊糖,这与 Nanobdellati 能够区分宿主和非宿主细胞有关。有趣的是,当宿主古生菌与纳米贝氏菌共培养时,N-聚糖中的特定糖类木糖被消除了。这些发现加深了我们对蛋白质糖基化在古细菌相互作用中的作用的理解。重要意义纳米虫古细菌以前被称为 DPANN,在系统发育上具有多样性,分布广泛,而且是强制性外共生的。Nanobdellati 识别和粘附其特定宿主的分子机制在很大程度上仍未得到探索。蛋白质糖基化是贯穿生命各个领域的基本生物学机制,通常对各种细胞-细胞相互作用至关重要。本研究首次揭示了水蚤及其宿主和非宿主古菌的糖蛋白组。我们发现,纳诺贝拉蒂可能利用来自宿主的底物,自主合成用于修饰蛋白质的聚糖。此外,我们还发现了独特的糖基化模式,这表明了纳米虫区分宿主细胞和非宿主细胞的机制。这项研究极大地推动了我们对极端环境中微生物相互作用的分子基础的理解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
N-linked protein glycosylation in Nanobdellati (formerly DPANN) archaea and their hosts.

Members of the kingdom Nanobdellati, previously known as DPANN archaea, are characterized by ultrasmall cell sizes and reduced genomes. They primarily thrive through ectosymbiotic interactions with specific hosts in diverse environments. Recent successful cultivations have emphasized the importance of adhesion to host cells for understanding the ecophysiology of Nanobdellati. Cell adhesion is often mediated by cell surface carbohydrates, and in archaea, this may be facilitated by the glycosylated S-layer protein that typically coats their cell surface. In this study, we conducted glycoproteomic analyses on two co-cultures of Nanobdellati with their host archaea, as well as on pure cultures of both host and non-host archaea. Nanobdellati exhibited various glycoproteins, including archaellins and hypothetical proteins, with glycans that were structurally distinct from those of their hosts. This indicated that Nanobdellati autonomously synthesize their glycans for protein modifications probably using host-derived substrates, despite the high energy cost. Glycan modifications on Nanobdellati proteins consistently occurred on asparagine residues within the N-X-S/T sequon, consistent with patterns observed across archaea, bacteria, and eukaryotes. In both host and non-host archaea, S-layer proteins were commonly modified with hexose, N-acetylhexosamine, and sulfonated deoxyhexose. However, the N-glycan structures of host archaea, characterized by distinct sugars such as deoxyhexose, nonulosonate sugar, and pentose at the nonreducing ends, were implicated in enabling Nanobdellati to differentiate between host and non-host cells. Interestingly, the specific sugar, xylose, was eliminated from the N-glycan in a host archaeon when co-cultured with Nanobdella. These findings enhance our understanding of the role of protein glycosylation in archaeal interactions.IMPORTANCENanobdellati archaea, formerly known as DPANN, are phylogenetically diverse, widely distributed, and obligately ectosymbiotic. The molecular mechanisms by which Nanobdellati recognize and adhere to their specific hosts remain largely unexplored. Protein glycosylation, a fundamental biological mechanism observed across all domains of life, is often crucial for various cell-cell interactions. This study provides the first insights into the glycoproteome of Nanobdellati and their host and non-host archaea. We discovered that Nanobdellati autonomously synthesize glycans for protein modifications, probably utilizing substrates derived from their hosts. Additionally, we identified distinctive glycosylation patterns that suggest mechanisms through which Nanobdellati differentiate between host and non-host cells. This research significantly advances our understanding of the molecular basis of microbial interactions in extreme environments.

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来源期刊
Journal of Bacteriology
Journal of Bacteriology 生物-微生物学
CiteScore
6.10
自引率
9.40%
发文量
324
审稿时长
1.3 months
期刊介绍: The Journal of Bacteriology (JB) publishes research articles that probe fundamental processes in bacteria, archaea and their viruses, and the molecular mechanisms by which they interact with each other and with their hosts and their environments.
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