Functional role of surface layer proteins of Lactobacillus acidophilus L-92 in stress tolerance and binding to host cell proteins.

IF 3.1 4区 医学 Q2 Agricultural and Biological Sciences
Bioscience of Microbiota, Food and Health Pub Date : 2021-01-01 Epub Date: 2020-09-17 DOI:10.12938/bmfh.2020-005
Taketo Wakai, Chie Kano, Harma Karsens, Jan Kok, Naoyuki Yamamoto
{"title":"Functional role of surface layer proteins of <i>Lactobacillus acidophilus</i> L-92 in stress tolerance and binding to host cell proteins.","authors":"Taketo Wakai,&nbsp;Chie Kano,&nbsp;Harma Karsens,&nbsp;Jan Kok,&nbsp;Naoyuki Yamamoto","doi":"10.12938/bmfh.2020-005","DOIUrl":null,"url":null,"abstract":"<p><p><i>Lactobacillus acidophilus</i> surface layer proteins (SLPs) self-assemble into a monolayer that is non-covalently bound to the outer surface of the cells. There they are in direct contact with the environment, environmental stressors and gut components of the host in which the organism resides. The role of <i>L. acidophilus</i> SLPs is not entirely understood, although SLPs seem to be essential for bacterial growth. We constructed three <i>L. acidophilus</i> L-92 strains, each expressing a mutant of the most abundant SLP, SlpA. Each carried a 12-amino acid c-myc epitope substitution at a different position in the protein. A strain was also obtained that expressed the SlpA paralog SlpB from an originally silent <i>slpB</i> gene. All four strains behaved differently with respect to growth under various stress conditions, such as the presence of salt, ox gall or ethanol, suggesting that SlpA affects stress tolerance in <i>L. acidophilus</i> L-92. Also, the four mutants showed differential <i>in vitro</i> binding ability to human host cell proteins such as uromodulin or dendritic cell (DC)-specific intercellular adhesion molecule-3 grabbing non-integrin (DC-SIGN). Furthermore, co-culture of murine immature DCs with a mutant strain expressing one of the recombinant SlpA proteins changed the concentrations of the cytokines IL-10 and IL-12. Our data suggest that SlpA and SlpB of <i>L. acidophilus</i> participate in bacterial stress tolerance and binding to uromodulin or DC-SIGN, possibly leading to effective immune-modification.</p>","PeriodicalId":8867,"journal":{"name":"Bioscience of Microbiota, Food and Health","volume":null,"pages":null},"PeriodicalIF":3.1000,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b1/24/bmfh-40-033.PMC7817507.pdf","citationCount":"7","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioscience of Microbiota, Food and Health","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.12938/bmfh.2020-005","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2020/9/17 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"Agricultural and Biological Sciences","Score":null,"Total":0}
引用次数: 7

Abstract

Lactobacillus acidophilus surface layer proteins (SLPs) self-assemble into a monolayer that is non-covalently bound to the outer surface of the cells. There they are in direct contact with the environment, environmental stressors and gut components of the host in which the organism resides. The role of L. acidophilus SLPs is not entirely understood, although SLPs seem to be essential for bacterial growth. We constructed three L. acidophilus L-92 strains, each expressing a mutant of the most abundant SLP, SlpA. Each carried a 12-amino acid c-myc epitope substitution at a different position in the protein. A strain was also obtained that expressed the SlpA paralog SlpB from an originally silent slpB gene. All four strains behaved differently with respect to growth under various stress conditions, such as the presence of salt, ox gall or ethanol, suggesting that SlpA affects stress tolerance in L. acidophilus L-92. Also, the four mutants showed differential in vitro binding ability to human host cell proteins such as uromodulin or dendritic cell (DC)-specific intercellular adhesion molecule-3 grabbing non-integrin (DC-SIGN). Furthermore, co-culture of murine immature DCs with a mutant strain expressing one of the recombinant SlpA proteins changed the concentrations of the cytokines IL-10 and IL-12. Our data suggest that SlpA and SlpB of L. acidophilus participate in bacterial stress tolerance and binding to uromodulin or DC-SIGN, possibly leading to effective immune-modification.

Abstract Image

Abstract Image

Abstract Image

嗜酸乳杆菌L-92表层蛋白在胁迫耐受和与宿主细胞蛋白结合中的功能作用。
嗜酸乳杆菌表面层蛋白(SLPs)自组装成一层,与细胞外表面非共价结合。在那里,它们与环境、环境压力源和生物体所在宿主的肠道成分直接接触。嗜酸乳杆菌SLPs的作用尚不完全清楚,尽管SLPs似乎是细菌生长所必需的。我们构建了三个嗜酸乳杆菌L-92菌株,每个菌株都表达了最丰富的SLP突变体SlpA。每个都在蛋白质的不同位置携带一个12个氨基酸的c-myc表位替代。从原沉默的SlpB基因中获得了表达SlpA平行SlpB的菌株。在不同的胁迫条件下,如盐、牛胆或乙醇的存在,这四种菌株的生长表现不同,表明SlpA影响了嗜酸乳杆菌L-92的逆境耐受性。此外,这四种突变体对人类宿主细胞蛋白(如尿调素或树突状细胞(DC)特异性细胞间粘附分子-3捕获非整合素(DC- sign))的体外结合能力也存在差异。此外,将小鼠未成熟dc与表达重组SlpA蛋白之一的突变株共培养,可以改变细胞因子IL-10和IL-12的浓度。我们的数据表明嗜酸乳杆菌的SlpA和SlpB参与细菌的应激耐受并与尿调蛋白或DC-SIGN结合,可能导致有效的免疫修饰。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Bioscience of Microbiota, Food and Health
Bioscience of Microbiota, Food and Health Immunology and Microbiology-Applied Microbiology and Biotechnology
CiteScore
5.50
自引率
3.20%
发文量
24
期刊介绍: Bioscience of Microbiota, Food and Health (BMFH) is a peer-reviewed scientific journal with a specific area of focus: intestinal microbiota of human and animals, lactic acid bacteria (LAB) and food immunology and food function. BMFH contains Full papers, Notes, Reviews and Letters to the editor in all areas dealing with intestinal microbiota, LAB and food immunology and food function. BMFH takes a multidisciplinary approach and focuses on a broad spectrum of issues.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信