Investigating E. coli cell envelope proteins and processes through colicin intoxication
通过大肠菌素中毒研究大肠杆菌细胞包膜蛋白和过程
基本信息
- 批准号:BB/G020671/2
- 负责人:
- 金额:$ 127.88万
- 依托单位:
- 依托单位国家:英国
- 项目类别:Research Grant
- 财政年份:2012
- 资助国家:英国
- 起止时间:2012 至 无数据
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
Gram-negative bacteria have evolved to survive in diverse ecological niches. Many species are pathogenic while others are not, for example serving a symbiotic role in the mammalian gut helping to digest food. The major distinguishing feature of Gram-negative organisms compared to their Gram-positive counterparts is the existence of an additional membrane barrier, the outer membrane (OM), which is also responsible for the absence of staining with Gram dye in bacteriological procedures. Although serving an important barrier function for the organism, the OM is not an energised system. This presents significant problems for processes that require an energy source, such as the bringing in of essential nutrients that are too big to pass through the protein-pores that naturally exist in the OM. This is in contrast to the inner membrane (IM) of the bacterium which is an energised system by virtue of the organism's metabolism. An essential element of an energised IM is the flow of protons from the space between the OM and IM (the periplasm) back across the IM into the cell's cytoplasm, which is called the proton motive force (pmf). The pmf is a powersource for many energy-dependent processes in all organisms. In Gram-negative bacteria it is also responsible for the way in which the organism energises biochemical events at the OM, using long proteins that are embedded in the IM and which point towards the OM where they meet partner proteins. Two of the most important proteins that perform this type of energy linkage are TonB and TolA, each of which is part of larger protein assemblies usually referred to as the Ton and Tol systems. Ton is involved in bringing essential nutrients into the cell while Tol is involved in maintaining the barrier functions of the OM although how it does this is not clear. What is also not clear, even though this has been heavily studied for many years, is how these systems respond to pmf in a way that promotes their specific functions at the OM. This LOLA application aims to exploit the behaviour of a family of protein antibiotics called colicins to probe energy-dependent processes at the Gram-negative OM, focusing on Escherichia coli. Colicins are made by E. coli to kill neighbouring bacteria during times of competition and are very potent antibacterials; a single molecule entering the bacterium is sufficient to elicit cell death. Colicins begin their journey into an E. coli cell by binding to a nutrient receptor in the OM. Subsequent interactions with either the Ton or Tol systems catalyse their entry into the cell (a process called translocation) which is thought to be dependent on the pmf across the IM, but this has yet to be proven. We propose exploiting colicins as probes of OM processes using biochemical, biophysical and structural approaches. We will measure the forces that are exerted on colicins bound to the external surface of a cell and determine whether these forces are wholly pmf-dependent. We will establish how these potent antimicrobials use their associations with Tol proteins in the periplasm to penetrate the cells' OM defences, which may point the way toward new antibiotics. We will also capitalise on a remarkable series of observations that have for the first time visualised single colicin molecules bound to receptor proteins diffusing on the external surface of an E. coli cell. These observations highlight a property of the OM that contradicts standard biochemical and microbiological textbooks, where the motion of protein molecules embedded in the OM is assumed to be free and unrestricted, as is the case for the IM. In contrast, we find that movement is not unrestricted but rather demarcated into compartments. We will investigate the reason for such compartmentalisation and determine whether it plays a role in colicin translocation. Ultimately, this LOLA will provide fundamental new insight into the Gram-negative OM and its organisation.
革兰氏阴性菌已经进化到可以在不同的生态环境中生存。许多物种是致病的,而其他物种则不是,例如在哺乳动物肠道中发挥共生作用,帮助消化食物。与革兰氏阳性微生物相比,革兰氏阴性微生物的主要区别特征是存在额外的膜屏障,即外膜(OM),这也是细菌学程序中不存在革兰氏染料染色的原因。虽然OM对生物体起着重要的屏障作用,但它不是一个能量系统。这对于需要能量源的过程提出了重大问题,例如引入太大而不能通过OM中天然存在的蛋白质孔的必需营养素。这与细菌的内膜(IM)形成对比,细菌的内膜是一个通过生物体代谢的能量系统。能量化IM的一个基本要素是质子从OM和IM之间的空间(周质)穿过IM返回细胞的细胞质,这被称为质子动力(pmf)。pmf是所有生物体中许多依赖能量的过程的动力源。在革兰氏阴性细菌中,它也负责生物体在OM处激发生化事件的方式,使用嵌入IM中的长蛋白质,并指向OM,在那里它们遇到伴侣蛋白质。执行这种类型的能量连接的两个最重要的蛋白质是TonB和托拉,它们中的每一个都是通常被称为Ton和Tol系统的较大蛋白质组装体的一部分。Ton参与将必需营养素带入细胞,而Tol参与维持OM的屏障功能,尽管它如何做到这一点尚不清楚。尽管多年来已经对此进行了大量研究,但目前还不清楚的是,这些系统如何以促进其在OM中的特定功能的方式对pmf做出反应。该LOLA应用旨在利用称为大肠杆菌素的蛋白质抗生素家族的行为来探测革兰氏阴性OM的能量依赖性过程,重点是大肠杆菌。大肠杆菌素是由大肠杆菌E.在竞争期间,大肠杆菌能够杀死邻近的细菌,并且是非常有效的抗菌剂;单个分子进入细菌就足以引起细胞死亡。大肠杆菌素开始它们进入E.大肠杆菌细胞中的营养受体结合的OM。随后与Ton或Tol系统的相互作用催化它们进入细胞(称为易位的过程),这被认为取决于穿过IM的pmf,但这尚未得到证实。我们建议利用大肠杆菌素作为探针的OM过程中使用的生物化学,生物物理和结构的方法。我们将测量施加在与细胞外表面结合的大肠杆菌素上的力,并确定这些力是否完全依赖于pmf。我们将确定这些有效的抗菌剂如何利用它们与周质中的Tol蛋白的结合来穿透细胞的OM防御,这可能为新的抗生素指明方向。我们还将利用一系列引人注目的观察结果,这些观察结果首次可视化了单个大肠杆菌素分子与在大肠杆菌外表面扩散的受体蛋白结合。coli细胞。这些观察结果突出了OM的一个属性,这与标准的生物化学和微生物学教科书相矛盾,其中嵌入OM中的蛋白质分子的运动被假定为是自由和不受限制的,就像IM的情况一样。与此相反,我们发现,运动不是不受限制的,而是划分成隔间。我们将调查这种区室化的原因,并确定它是否在大肠杆菌素易位中发挥作用。最终,该LOLA将为革兰氏阴性OM及其组织提供基本的新见解。
项目成果
期刊论文数量(10)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Structural and biophysical analysis of nuclease protein antibiotics.
核酸酶蛋白抗生素的结构和生物物理分析。
- DOI:10.1042/bcj20160544
- 发表时间:2016-09-15
- 期刊:
- 影响因子:0
- 作者:Klein A;Wojdyla JA;Joshi A;Josts I;McCaughey LC;Housden NG;Kaminska R;Byron O;Walker D;Kleanthous C
- 通讯作者:Kleanthous C
Supramolecular assemblies underpin turnover of outer membrane proteins in bacteria.
- DOI:10.1038/nature14461
- 发表时间:2015-07-16
- 期刊:
- 影响因子:64.8
- 作者:Rassam P;Copeland NA;Birkholz O;Tóth C;Chavent M;Duncan AL;Cross SJ;Housden NG;Kaminska R;Seger U;Quinn DM;Garrod TJ;Sansom MS;Piehler J;Baumann CG;Kleanthous C
- 通讯作者:Kleanthous C
Blind prediction of interfacial water positions in CAPRI.
- DOI:10.1002/prot.24439
- 发表时间:2014-04
- 期刊:
- 影响因子:2.9
- 作者:Lensink MF;Moal IH;Bates PA;Kastritis PL;Melquiond AS;Karaca E;Schmitz C;van Dijk M;Bonvin AM;Eisenstein M;Jiménez-García B;Grosdidier S;Solernou A;Pérez-Cano L;Pallara C;Fernández-Recio J;Xu J;Muthu P;Praneeth Kilambi K;Gray JJ;Grudinin S;Derevyanko G;Mitchell JC;Wieting J;Kanamori E;Tsuchiya Y;Murakami Y;Sarmiento J;Standley DM;Shirota M;Kinoshita K;Nakamura H;Chavent M;Ritchie DW;Park H;Ko J;Lee H;Seok C;Shen Y;Kozakov D;Vajda S;Kundrotas PJ;Vakser IA;Pierce BG;Hwang H;Vreven T;Weng Z;Buch I;Farkash E;Wolfson HJ;Zacharias M;Qin S;Zhou HX;Huang SY;Zou X;Wojdyla JA;Kleanthous C;Wodak SJ
- 通讯作者:Wodak SJ
Structures of the Ultra-High-Affinity Protein-Protein Complexes of Pyocins S2 and AP41 and Their Cognate Immunity Proteins from Pseudomonas aeruginosa.
- DOI:10.1016/j.jmb.2015.07.014
- 发表时间:2015-08-28
- 期刊:
- 影响因子:5.6
- 作者:Joshi A;Grinter R;Josts I;Chen S;Wojdyla JA;Lowe ED;Kaminska R;Sharp C;McCaughey L;Roszak AW;Cogdell RJ;Byron O;Walker D;Kleanthous C
- 通讯作者:Kleanthous C
Protein-protein interactions and the spatiotemporal dynamics of bacterial outer membrane proteins.
- DOI:10.1016/j.sbi.2015.10.007
- 发表时间:2015-12
- 期刊:
- 影响因子:6.8
- 作者:Kleanthous C;Rassam P;Baumann CG
- 通讯作者:Baumann CG
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Colin Kleanthous其他文献
Nanoscale Protein Interactions Determine the Mesoscale Dynamic Organisation of Biomembranes
- DOI:
10.1016/j.bpj.2017.11.2163 - 发表时间:
2018-02-02 - 期刊:
- 影响因子:
- 作者:
Anna L. Duncan;Matthieu Chavent;Patrice Rassam;Jean Hélie;Tyler Reddy;Oliver Birkholz;Dmitry Belyaev;Ben Hambly;Jacob Piehler;Colin Kleanthous;Mark S.P. Sansom - 通讯作者:
Mark S.P. Sansom
Force Triggered Dissociation of the Highly Avid E9:Im9 Complex
- DOI:
10.1016/j.bpj.2012.11.3174 - 发表时间:
2013-01-29 - 期刊:
- 影响因子:
- 作者:
David Brockwell;Oliver Farrance;Renata Kaminska;Sasha Derrington;Colin Kleanthous;Sheena Radford - 通讯作者:
Sheena Radford
MPSA abstracts
- DOI:
10.1007/bf01898856 - 发表时间:
1994-07-01 - 期刊:
- 影响因子:1.400
- 作者:
Mahmoud Aminlari;Thomas Asquith;Katherine Sarlo;Jerome M. Bailey;Oanh Tu;Gilbert Issai;Alice Ha;John E. Shively;Alexander W. Bell;Nicole C. Baur;John J. M. Bergeron;Wei -Jia Ou;David Y. Thomas;Katherine Cianflone;Allain Baldo;Maxwell T. Hincke;Richard L. Momparler;Josée Laliberté;David M. P. Thomson;M. Sutherland;Vladimir Besada;Javier Gonzalez;Gabriel Padron;Hilda Garay;Osvaldo Reyes;Toshifumi Takao;Yasutsugu Shimonishi;Rainer Bischoff;Dominique Roecklin;Bernadette Bouchon;Klaus Klarskov;Alain Van Dorsselaer;Patricia G. Brake;Anne Pacitti;Terry Higgins;Panos Stevis;John Malinowski;Sue McElhiney;Janes Huang;Christine Vestal;Scott D. Buckel;Tracy Stevenson;Joseph A. Loo;Martin Caffrey;Jin Wang;Carmichael J. A. Wallace;Ian Clark-Lewis;C. A. Carothers Carraway;J. Huang;Y. Li;S. -H. Juang;A. Gallo;B. J. Mayer;K. L. Carraway;Patrick L. Coleman;Daniel Sarpong;David W. Deerfield;Amanda Holland-Minkley;John D. Hempel;Hugh B. Nicholas;Nancy D. Denslow;Leroy C. Folmar;Craig V. Sullivan;James D. Dixon;Jonathan P. Mark;Christopher P. Elicone;Simin D. Maleknia;Brian F. McGuinness;Fred E. Regnier;Noubar B. Afeyan;Julia M. Dolence;C. Dale Poulter;Tsezi Egorov;Alexander Musolyamov;Yves Popineau;Jens Andersen;Peter Roepstorff;Roberto J. Falkenstein;Mirtha J. Biscoglio de Jiménez Bonino;Clara Peña;D. L. Gauggel;T. N. Asquith;R. J. Isfort;N. S. Miller;D. B. Cody;Michael F. Giblin;Tuck C. Wong;Thomas P. Quinn;Gregory A. Grant;Mark W. Crankshaw;Scott Griffith;Steve Schroeder;Thomas Quinn;F. Guinet;Y. Petillot;J. M. Chapsal;J. Dubayle;F. Greco;O. Barge;E. Forest;C. Valentin;Frederick M Hahn;Jonathan A. Baker;C. Dale Poulter;Mitsuru Haniu;William C. Kenney;Michael F. Rohde;James G. Harman;Eun Ju Lee;Joel Glasgow;Sew Fen Lew;Ali O. Belduz;Reed J. Harris;Michael S. Molony;Lene H. Keyt;Shiaw -Lin Wu;David H. Hawke;Jaqueline Tso;Sherrell Early;Chad G. Miller;G. Thomas Hayman;Jan A. Miernyk;Ulf Hellman;Christer Wernstedt;Jorge Góñez;Daniel Hess;Ralph Studer;Peter E. Hunziker;Hisashi Hirano;Yoshihiro Watanabe;Sergei F. Barbashov;Setsuko Komatsu;Andrew M. Hemmings;Masaru Miyagi;Susumu Tsunasawa;Reuben E. Huber;Nathan J. Roth;Michael T. Gaunt;Paul Jenö;Thierry Mini;Suzette Moes;Martin Horst;Kenji Jinnai;Tetsuo Ashizawa;M. Zouhair Atassi;Anders H. Johnsen;Hanne Jensen;Jens F. Rehfeld;Masaharu Kamo;Takao Kawakami;Norifumi Miyatake;Akira Tsugita;JN Keen;PF Zagalsky;JBC Findlay;Regine Kraft;Susanne Kostka;Enno Hartmann;Henry C. Krutzsch;John K. Inman;Claudia Machalinski;Mirtha Biscoglio de Jiménez Bonino;Donald K. McRorie;Gregg R. Dieckmann;Susan Heilman;William F. DeGrado;Vincent L. Pecoraro;James Kenny;Julie Sahakian;Jacqueline Tso;Mary B. Moyer;William A. Burkhart;Tatyana Muranova;Lubov Makova;Hugh Nicholas;John Hempel;Amy Hinich;David Deerfield;Joseph Behrmann;Alex Ropelewski;Lori Nixon;Leonard Maneri;Kerry Nugent;Ken Stoney;John Wieser;Hiroshi Ohguro;Krzysztof Palczewski;Kenneth A. Walsh;Richard S. Johnson;Leonard C Packman;Carl Webster;John Gray;G. Padrón;V. Morera;L. J. González;Y. Támbara;V. Besada;R. Villalonga;G. Chinea;O. Reyes;H. Garay R. Bringas;C. Nazábal;Bruce P. Parkinson;Kent A. Yamada;Anne Randolph;Anthony Pisano;Nicole H. Packer;John W. Redmond;Keith L. Williams;Andrew A. Gooley;Hanne H. Rasmussen;Ejvind Mørtz;Matthias Mann;Julio E. Celis;Lone K. Rasmussen;Esben S. Sørensen;Torben E. Petersen;Jørgen Gliemann;Poul Henning Jensen;Staffan Renlund;Henrik Wadensten;Annika Persson;Per Persson;Agneta Johansson;Per -Olof Edlund;Donald J. Rose;Ragna Sack;Alex Apffel;Chad Miller;Rodney L. Levine;Kazuyasu Sakaguchi;Nicola Zambrano;Marc S. Lewis;Eric T. Baldwin;Bruce A. Shapiro;John W Erickson;James G. Omichinski;G. Marius Clore;Angela M. Gronenborn;Ettore Appella;Werner Schröder;Irmgard Moser;Werner Pansegrau;Erich Lanka;Richard J. Simpson;James Eddes;Hong Ji;Gavin E. Reid;Robert L. Moritz;Peter Højrup;David W. Speicher;David F. Reim;Kaye D. Speicher;B. R. Srinivasa;S. P. Barde;William G. Stirtan;Alyona Sukhanova;Sergey Vorob'ev;Alexander Gabibov;Igor Bronstein;Kenji Tanaka;Kuniko Einaga;Minoru Tsukada;Jonathan F. Tait;Kazuo Fujikawa;Keiji Takamoto;Kazuo Satake;Ilya A. Vakser;V. V. Velikodvorskaia;A. G. Gabibov;A. G. Rabinkov;Tennie Videler;Michael Osborne;Geoffrey Moore;Richard James;Colin Kleanthous;Jane H. Walent;Richard Bessen;Dick Marsh;G. Marius Clore;Ronald L. Niece;Francis H. C. Tsao;Hong Wang;Scot R. Weinberger;Lynn M. Chakel;Ewald M. Wondrak;Alan R. Kimmel;John M. Louis - 通讯作者:
John M. Louis
How Nanoscale Protein Interactions Determine the Mesoscale Dynamic Organisation of Membrane Proteins
- DOI:
10.1016/j.bpj.2018.11.1984 - 发表时间:
2019-02-15 - 期刊:
- 影响因子:
- 作者:
Anna L. Duncan;Maximilian A.R. Bandurka;Matthieu G. Chavent;Patrice Rassam;Wanling Song;Oliver Birkholz;Jean Helie;Tyler Reddy;Dmitry Beliaev;Ben Hambly;Jacob Piehler;Colin Kleanthous;Mark S.P. Sansom - 通讯作者:
Mark S.P. Sansom
Letter to the Editor: Assignment of 1H,13C and 15N signals of the DNase domain of colicin E9
- DOI:
10.1023/a:1008394407597 - 发表时间:
1999-06-01 - 期刊:
- 影响因子:1.900
- 作者:
Sara B.-M. Whittaker;Ruth Boetzel;Colin MacDonald;Lu-Yun Lian;Richard James;Colin Kleanthous;Geoffrey R. Moore - 通讯作者:
Geoffrey R. Moore
Colin Kleanthous的其他文献
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{{ truncateString('Colin Kleanthous', 18)}}的其他基金
Pushing the envelope: atomic force microscopy imaging of the bacterial outer membrane during growth and division
挑战极限:生长和分裂过程中细菌外膜的原子力显微镜成像
- 批准号:
BB/X007669/1 - 财政年份:2024
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Exploiting protein import to interrogate energy transduction through the bacterial cell envelope
利用蛋白质输入来询问通过细菌细胞包膜的能量转导
- 批准号:
BB/X016366/1 - 财政年份:2024
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Molecular basis of outer membrane stabilisation by the energised Tol-Pal system in Gram-negative bacteria
革兰氏阴性菌通电 Tol-Pal 系统外膜稳定的分子基础
- 批准号:
BB/V008056/1 - 财政年份:2021
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Protein import through the E. coli cell envelope
通过大肠杆菌细胞膜输入蛋白质
- 批准号:
BB/P009948/1 - 财政年份:2017
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Molecular basis of protein translocation through outer membrane porins
蛋白质通过外膜孔蛋白易位的分子基础
- 批准号:
BB/L021234/1 - 财政年份:2015
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Molecular mechanism of environmental stress sensing by bacterial Zinc-containing Anti-Sigma factors
细菌含锌Anti-Sigma因子感知环境应激的分子机制
- 批准号:
BB/I008691/2 - 财政年份:2012
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Molecular mechanism of environmental stress sensing by bacterial Zinc-containing Anti-Sigma factors
细菌含锌Anti-Sigma因子感知环境应激的分子机制
- 批准号:
BB/I008691/1 - 财政年份:2011
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Investigating E. coli cell envelope proteins and processes through colicin intoxication
通过大肠菌素中毒研究大肠杆菌细胞包膜蛋白和过程
- 批准号:
BB/G020671/1 - 财政年份:2009
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
Biophysical and structural analysis of protein-protein interactions: from encounter complexes to computational design and directed evolution
蛋白质-蛋白质相互作用的生物物理和结构分析:从相遇复合物到计算设计和定向进化
- 批准号:
BB/E011306/1 - 财政年份:2007
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant
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相似海外基金
Defining E. coli Diversity in Complex Samples: Methods for Surveillance & Transmission
定义复杂样品中的大肠杆菌多样性:监测方法
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Mechanisms underlying diarrhea and gut inflammation mediated by Enterotoxigenic and Enteropathogenic E. coli
产肠毒素和致病性大肠杆菌介导的腹泻和肠道炎症的机制
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$ 127.88万 - 项目类别:
SBIR Phase I: Point-of-Care Diagnostic Tool for Identifying Extended Spectrum β-Lactamase E. Coli in Urinary Tract Infection
SBIR 第一阶段:用于识别尿路感染中的超广谱 β-内酰胺酶大肠杆菌的即时诊断工具
- 批准号:
2233653 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Standard Grant
Utilizing the power of synthetic biology and De Novo design for the overexpression and biochemical stabilization of KCNA6 or Kv1.6 potassium channels in the E. coli expression system
利用合成生物学和 De Novo 设计的力量,实现大肠杆菌表达系统中 KCNA6 或 Kv1.6 钾通道的过度表达和生化稳定
- 批准号:
10666856 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Identification of coexistence relationships and phenotypic traits of virulence and resistance genes by large-scale E. coli genome analysis
通过大规模大肠杆菌基因组分析鉴定毒力和抗性基因的共存关系和表型特征
- 批准号:
23K07947 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Molecular Pathogenesis of enterotoxigenic E. coli associated enteropathy
产肠毒素大肠杆菌相关性肠病的分子发病机制
- 批准号:
10656056 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Characterization of the RRS: a new chromosomal structural element in E. coli
RRS 的表征:大肠杆菌中的一种新染色体结构元件
- 批准号:
10752809 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Examining the mechanisms of epoxytigliane induced biofilm disruption in antibiotic resistant E coli
检查环氧替利亚烷诱导抗生素耐药性大肠杆菌生物膜破坏的机制
- 批准号:
BB/Y51276X/1 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Training Grant
Microfluidic Impedance Biosensor for the Detection of E. coli in Waterways
用于检测水道中大肠杆菌的微流控阻抗生物传感器
- 批准号:
2882939 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Studentship
Defining the physiology of E. coli O157:H7 in cattle to develop phage-based interventions
定义牛体内大肠杆菌 O157:H7 的生理学以开发基于噬菌体的干预措施
- 批准号:
BB/X007022/1 - 财政年份:2023
- 资助金额:
$ 127.88万 - 项目类别:
Research Grant