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计算机模拟分析突显了具有类胶原蛋白结构域的新型粘附素复合体成员的存在。

In-Silico Analysis Highlights the Existence in Members of Complex of a New Class of Adhesins Possessing Collagen-like Domains.

作者信息

Estevens Ricardo, Mil-Homens Dalila, Fialho Arsenio M

机构信息

Department of Bioengineering, Instituto Superior Técnico, University of Lisbon, Av. Rovisco Pais, 1049-001 Lisbon, Portugal.

Institute for Bioengineering and Biosciences (iBB), Instituto Superior Técnico, University of Lisbon, Av. Rovisco Pais, 1049-001 Lisbon, Portugal.

出版信息

Microorganisms. 2023 Apr 25;11(5):1118. doi: 10.3390/microorganisms11051118.

DOI:10.3390/microorganisms11051118
PMID:37317093
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10224339/
Abstract

is a multi-drug-resistant lung pathogen. This species synthesizes various virulence factors, among which cell-surface components (adhesins) are critical for establishing the contact with host cells. This work in the first part focuses on the current knowledge about the adhesion molecules described in this species. In the second part, through in silico approaches, we perform a comprehensive analysis of a group of unique bacterial proteins possessing collagen-like domains (CLDs) that are strikingly overrepresented in the species, representing a new putative class of adhesins. We identified 75 CLD-containing proteins in complex (Bcc) members (Bcc-CLPs). The phylogenetic analysis of Bcc-CLPs revealed the evolution of the core domain denominated "Bacterial collagen-like, middle region". Our analysis remarkably shows that these proteins are formed by extensive sets of compositionally biased residues located within intrinsically disordered regions (IDR). Here, we discuss how IDR functions may increase their efficiency as adhesion factors. Finally, we provided an analysis of a set of five homologs identified in J2315. Thus, we propose the existence in Bcc of a new type of adhesion factors distinct from the described collagen-like proteins (CLPs) found in Gram-positive bacteria.

摘要

是一种多重耐药性肺部病原体。该物种合成多种毒力因子,其中细胞表面成分(粘附素)对于与宿主细胞建立接触至关重要。这项工作的第一部分聚焦于关于该物种中描述的粘附分子的现有知识。在第二部分中,我们通过计算机方法,对一组在该物种中显著富集的具有胶原样结构域(CLDs)的独特细菌蛋白进行了全面分析,这些蛋白代表了一类新的假定粘附素。我们在复杂(Bcc)成员(Bcc-CLPs)中鉴定出75种含CLD的蛋白。对Bcc-CLPs的系统发育分析揭示了名为“细菌胶原样,中间区域”的核心结构域的进化。我们的分析显著表明,这些蛋白由位于内在无序区域(IDR)内的大量成分偏向性残基组成。在此,我们讨论IDR功能如何可能提高它们作为粘附因子的效率。最后,我们对在J2315中鉴定出的一组五个同源物进行了分析。因此,我们提出在Bcc中存在一种新型粘附因子,它不同于革兰氏阳性细菌中发现的所述胶原样蛋白(CLPs)。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/37a844d4da16/microorganisms-11-01118-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/d5a7f08be2f5/microorganisms-11-01118-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/fc6fa25bf0c0/microorganisms-11-01118-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/beafe23189f8/microorganisms-11-01118-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/8d21fe9d4b3d/microorganisms-11-01118-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/063bcc201a27/microorganisms-11-01118-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/37a844d4da16/microorganisms-11-01118-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/d5a7f08be2f5/microorganisms-11-01118-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/fc6fa25bf0c0/microorganisms-11-01118-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/beafe23189f8/microorganisms-11-01118-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/8d21fe9d4b3d/microorganisms-11-01118-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/063bcc201a27/microorganisms-11-01118-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a2e8/10224339/37a844d4da16/microorganisms-11-01118-g006.jpg

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AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models.AlphaFold 蛋白质结构数据库:用高精度模型极大地扩展蛋白质序列空间的结构覆盖范围。
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flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions.
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Current Insights on the Diverse Structures and Functions in Bacterial Collagen-like Proteins.当前对细菌胶原蛋白样蛋白的多种结构和功能的深入了解。
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