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Pathology User Guide
Whittington Health Version: 2021.1 MB 129 Microbiology Department Author: Service Managers Page 1 of 189 Print Date: 27 April 2021 Authorised by: DW Issue Date: 26 April 2021 PATHOLOGY USER GUIDE Version 2021.1 Document Number : MB 129 Approved By: David Whittington 1 The master document is controlled electronically. Printed copies of this document are not controlled. Document users are responsible for ensuring printed copies are valid prior to use. Whittington Health Version: 2021.1 MB 129 Microbiology Department Author: Service Managers Page 2 of 189 Print Date: 27 April 2021 Authorised by: DW Issue Date: 26 April 2021 CONTENTS GENERAL INFORMATION..................................................................................................................... 5 INTRODUCTION ................................................................................................................................. 5 ADDRESS ........................................................................................................................................... 5 LOCATION .......................................................................................................................................... 5 GENERAL ENQUIRIES ...................................................................................................................... 5 OPERATIONAL PATHOLOGY LABORATORY MANAGER ............................................................... 6 SERVICE AVAILABILITY ................................................................................................................... -
Bacterial Oxidases of the Cytochrome Bd Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets
Published in "Antioxidants & Redox Signaling doi: 10.1089/ars.2020.8039, 2020" which should be cited to refer to this work. Bacterial Oxidases of the Cytochrome bd Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets Vitaliy B. Borisov,1 Sergey A. Siletsky,1 Alessandro Paiardini,2 David Hoogewijs,3 Elena Forte,2 Alessandro Giuffre`,4 and Robert K. Poole5 Abstract Significance: Cytochrome bd is a ubiquinol:oxygen oxidoreductase of many prokaryotic respiratory chains with a unique structure and functional characteristics. Its primary role is to couple the reduction of molecular oxygen, even at submicromolar concentrations, to water with the generation of a proton motive force used for adenosine triphosphate production. Cytochrome bd is found in many bacterial pathogens and, surprisingly, in bacteria for- mally denoted as anaerobes. It endows bacteria with resistance to various stressors and is a potential drug target. Recent Advances: We summarize recent advances in the biochemistry, structure, and physiological functions of cytochrome bd in the light of exciting new three-dimensional structures of the oxidase. The newly discovered roles of cytochrome bd in contributing to bacterial protection against hydrogen peroxide, nitric oxide, perox- ynitrite, and hydrogen sulfide are assessed. Critical Issues: Fundamental questions remain regarding the precise delineation of electron flow within this multihaem oxidase and how the extraordinarily high affinity for oxygen is accomplished, while endowing bacteria with resistance to other small ligands. Future Directions: It is clear that cytochrome bd is unique in its ability to confer resistance to toxic small molecules, a property that is significant for understanding the propensity of pathogens to possess this oxidase. -
Reconstitution of Active Transport in Proteoliposomes Containing Cytochrome O Oxidase and Lac Carrier Protein Purified from Esch
Proc. Natl Acad. Sci. USA Vol. 80, pp. 4889-4893, August 1983 Biochemistry Reconstitution of active transport in proteoliposomes containing cytochrome o oxidase and lac carrier protein purified from Escherichia coli (chemiosmotic hypothesis/proton electrochemical gradient/carbocyanine/octyl glucoside/detergent dilution) KAZUNOBU MATSUSHITA*, LEKHA PATEL*, ROBERT B. GENNISt, AND H. RONALD KABACK*t *Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110; and tDepartment of Chemistry, University of Illinois, Urbana, Illinois 61801 Communicated by B. L. Horecker, April 29, 1983 ABSTRACT Most active transport across the bacterial cell flux with appropriately directed lactose concentration gra- membrane is driven by a proton electrochemical gradient dients, and accumulate lactose against a concentration gradient (AJAH+, interior negative and alkaline) generated via electron when AOH+ (interior negative or alkaline or both) is imposed transfer through a membrane-bound respiratory chain. This phe- (2-5). Furthermore, the turnover number of purified lac car- nomenon is now reproduced in vitro with proteoliposomes con- rier in proteoliposomes is similar to that observed in right-side- taining only two proteins purified from the membrane of Esch- out membrane vesicles, as is the Km for lactose (1). In addition, erichia coli. An o-type cytochrome oxidase was extracted from a secondary structure model for the lac carrier protein has been membranes of a cytochrome d terminal oxidase mutant with octyl proposed (6), monoclonal antibodies against the purified pro- 8-D-glucopyranoside after sequential treatment with urea and tein have been prepared and characterized (7), and it has been cholate and was purified to homogeneity by ion-exchange chro- the matography. -
Multi-Omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities
Washington University in St. Louis Washington University Open Scholarship Arts & Sciences Electronic Theses and Dissertations Arts & Sciences Summer 8-15-2019 Multi-omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities Tayte Paul Campbell Washington University in St. Louis Follow this and additional works at: https://openscholarship.wustl.edu/art_sci_etds Part of the Bioinformatics Commons, Biology Commons, and the Microbiology Commons Recommended Citation Campbell, Tayte Paul, "Multi-omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities" (2019). Arts & Sciences Electronic Theses and Dissertations. 1888. https://openscholarship.wustl.edu/art_sci_etds/1888 This Dissertation is brought to you for free and open access by the Arts & Sciences at Washington University Open Scholarship. It has been accepted for inclusion in Arts & Sciences Electronic Theses and Dissertations by an authorized administrator of Washington University Open Scholarship. For more information, please contact [email protected]. WASHINGTON UNIVERSITY IN ST. LOUIS Division of Biology and Biomedical Sciences Plant and Microbial Biosciences Dissertation Examination Committee: Gautam Dantas, Chair Arpita Bose Andrew Kau Audrey Odom-John Himadri Pakrasi Fuzhong Zhang Multi-omic Understanding of the Evolution of Xenobiotic Tolerance in Bacterial Isolates and Communities by Tayte P. Campbell A dissertation presented to The Graduate School of Washington University in partial fulfillment -
In-Vitro Synthesis and Reconstitution of Cytochrome Bo3 Ubiquinol Oxidase in Artificial Membranes
In-vitro Synthesis and Reconstitution of Cytochrome bo3 Ubiquinol Oxidase in Artificial Membranes Dissertation Zur Erlangung des Grades Doktor der Naturwissenschaften Am Fachbereich Biologie Der Johannes Gutenberg-Universität Mainz Ahu ARSLAN YILDIZ geboren am 20.12.1980 in Turkey Mainz, 2010 Dekan: Prof. Dr. Erwin Schmidt 1. Berichterstatter: Prof. Dr. Eva K. Sinner 2. Berichterstatter: Prof. Dr. Harald Paulsen 3. Prüfer: Prof. Dr. Wolfgang Knoll 4. Prüfer: Prof. Dr. Elmar Jaenicke Tag der mündlichen Prüfung: 29.01.2010 Abbreviations ATP Adenosine triphosphate PD Parkinson’s Disease Cyt-bo3 Cytochrome bo3 ubiquinol oxidase NADH Nicotinamide adenine dinucleotide UQ Ubiquinone UQH2 Ubiquinol Cyt-c Cytochrome c E.coli Escherichia coli Heme Heme or Haem molecule Cyt-bd Cytochrome bd ubiquinol oxidase cyo Cytochrome encoding operon CuA Copper site in subunit II CuB Copper of binuclear site CFPS Cell-free protein synthesis tRNA Transfer RNA GTP Guanidine triphosphate BLMs Black lipid membranes sBLM Supported bilayer lipid membrane tBLM Tethered lipid bilayer membrane SPR Surface Plasmon Resonance Spectroscopy SPFS Surface Plasmon Enhanced Fluorescence Spectroscopy θc Critical angle θm Minimum angle TIR Total internal reflection εd Dielectric constant n Refractive index CA Contact angle pJRHisA Subunit II histidine tagged enzyme with natural promoter pRCO3 Fused subunit II-I-III enzyme with natural promoter pETcyo Subunit II histidine tagged enzyme with T7 promoter LB Luria Bertani media ii KOH Potassium hydroxide PES Polyethylene sulfonate -
Metabolic and Regulatory Rearrangements Underlying Glycerol Metabolism in 3 Pseudomonas Putida KT2440 4 5 by 6 7 Pablo I
1 1 2 Metabolic and regulatory rearrangements underlying glycerol metabolism in 3 Pseudomonas putida KT2440 4 5 by 6 7 Pablo I. Nikel, Juhyun Kim, and Víctor de Lorenzo* 8 9 Systems and Synthetic Biology Program, Centro Nacional de Biotecnología (CNB-CSIC), 10 Madrid 28049, Spain 11 12 13 14 Running Title: Glycerol metabolism in P. putida 15 Keywords: Glycerol, Pseudomonas putida, central metabolism, Entner-Doudoroff pathway, redox 16 homeostasis, transcriptional regulation 17 18 19 20 _________________________________________________________________________________ 21 22 * Corresponding author V. de Lorenzo 23 Systems and Synthetic Biology Program 24 Centro Nacional de Biotecnología (CNB-CSIC) 25 Darwin 3, Campus de Cantoblanco 26 Madrid 28049, Spain 27 Phone: +34 91 585 4536 28 Fax: +34 91 585 4506 29 E-mail: [email protected] 30 2 1 SUMMARY 2 3 While the natural niches of the soil bacterium Pseudomonas putida are unlikely to include significant 4 amounts of free glycerol as a growth substrate, this bacterium is genetically equipped with the functions 5 required for its metabolism. We have resorted to deep sequencing of the transcripts in glycerol-grown 6 P. putida KT2440 cells to gain an insight into the biochemical and regulatory components involved in 7 the shift between customary C sources (e.g., glucose or succinate) to the polyol. Transcriptomic results 8 were contrasted with key enzymatic activities under the same culture conditions. Cognate expression 9 profiles revealed that genes encoding enzymes of the Entner-Doudoroff route and other catabolic 10 pathways, e.g., the gluconate and 2-ketogluconate loops, were significantly down-regulated on glycerol. -
Differential Effects of Epinephrine, Norepinephrine, and Indole
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Texas A&M University INFECTION AND IMMUNITY, Sept. 2007, p. 4597–4607 Vol. 75, No. 9 0019-9567/07/$08.00ϩ0 doi:10.1128/IAI.00630-07 Copyright © 2007, American Society for Microbiology. All Rights Reserved. Differential Effects of Epinephrine, Norepinephrine, and Indole on Escherichia coli O157:H7 Chemotaxis, Colonization, and Gene Expressionᰔ Tarun Bansal, Derek Englert, Jintae Lee, Manjunath Hegde, Thomas K. Wood, and Arul Jayaraman* Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843-3122 Received 3 May 2007/Returned for modification 4 June 2007/Accepted 13 June 2007 During infection in the gastrointestinal tract, enterohemorrhagic Escherichia coli (EHEC) O157:H7 is exposed to a wide range of signaling molecules, including the eukaryotic hormones epinephrine and norepi- nephrine, and bacterial signal molecules such as indole. Since these signaling molecules have been shown to be involved in the regulation of phenotypes such as motility and virulence that are crucial for EHEC infections, we hypothesized that these molecules also govern the initial recognition of the large intestine environment and attachment to the host cell surface. Here, we report that, compared to indole, epinephrine and norepinephrine exert divergent effects on EHEC chemotaxis, motility, biofilm formation, gene expression, and colonization of HeLa cells. Using a novel two-fluorophore chemotaxis assay, it was found that EHEC is attracted to epineph- rine and norepinephrine while it is repelled by indole. In addition, epinephrine and norepinephrine also increased EHEC motility and biofilm formation while indole attenuated these phenotypes. -
Davidge JBC Supplementary.Pdf
promoting access to White Rose research papers Universities of Leeds, Sheffield and York http://eprints.whiterose.ac.uk/ White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/7923/ (includes links to Main Article, Supplementary Material and Figures) Published paper Davidge, K.S., Sanguinetti, G., Yee, C.H., Cox, A.G., McLeod, C.W., Monk, C.E., Mann, B.E., Motterlini, R. and Poole, R.K. (2009) Carbon monoxide-releasing antibacterial molecules target respiration and global transcriptional regulators. Journal of Biological Chemistry, 284 (7). pp. 4516-4524. http://dx.doi.org/10.1074/jbc.M808210200 Supplementary Material White Rose Research Online [email protected] Supplementary Material Carbon monoxide-releasing antibacterial molecules target respiration and global transcriptional regulators Kelly S Davidge, Guido Sanguinetti, Chu Hoi Yee, Alan G Cox, Cameron W McLeod, Claire E Monk, Brian E Mann, Roberto Motterlini and Robert K Poole Contents Page Number Supplementary Figure S1 3 Inhibition by CORM-3 of E. coli cultures grown in defined medium anaerobically and aerobically Supplementary Figure S2 4 Viability assays showing survival of anaerobically and aerobically E. coli in defined growth medium Supplementary Figure S3 5 Reaction of terminal oxidases in vivo on addition of RuCl2(DMSO)4 to intact cells in a dual-wavelength spectrophotometer Supplementary Figure S4 6 CORM-3 generates carbonmonoxycytochrome bd in vivo and depresses synthesis of cytochrome bo' Supplementary Figure S5 7 Expression of spy-lacZ activity -
Letters to Nature
letters to nature Received 7 July; accepted 21 September 1998. 26. Tronrud, D. E. Conjugate-direction minimization: an improved method for the re®nement of macromolecules. Acta Crystallogr. A 48, 912±916 (1992). 1. Dalbey, R. E., Lively, M. O., Bron, S. & van Dijl, J. M. The chemistry and enzymology of the type 1 27. Wolfe, P. B., Wickner, W. & Goodman, J. M. Sequence of the leader peptidase gene of Escherichia coli signal peptidases. Protein Sci. 6, 1129±1138 (1997). and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258, 12073±12080 2. Kuo, D. W. et al. Escherichia coli leader peptidase: production of an active form lacking a requirement (1983). for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274±280 (1993). 28. Kraulis, P.G. Molscript: a program to produce both detailed and schematic plots of protein structures. 3. Tschantz, W. R. et al. Characterization of a soluble, catalytically active form of Escherichia coli leader J. Appl. Crystallogr. 24, 946±950 (1991). peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34, 3935±3941 29. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and (1995). the thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281±296 (1991). 4. Allsop, A. E. et al.inAnti-Infectives, Recent Advances in Chemistry and Structure-Activity Relationships 30. Meritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505± (eds Bently, P. H. & O'Hanlon, P. J.) 61±72 (R. Soc. Chem., Cambridge, 1997). -
C12) United States Patent (IO) Patent No.: US 9,441,253 B2 San Et Al
IIIIII IIIIIIII Ill lllll lllll lllll lllll lllll lllll lllll lllll 111111111111111111 US009441253B2 c12) United States Patent (IO) Patent No.: US 9,441,253 B2 San et al. (45) Date of Patent: Sep.13,2016 (54) METABOLIC TRANSISTOR IN BACTERIA 114/13027 (2013.01); C12Y 205/01001 (2013.01); C12Y 205/01032 (2013.01); C12Y (71) Applicant: William Marsh Rice University, 205/01093 (2013.01); C12Y 305/01022 Houston, TX (US) (2013.01); C12Y 305/99002 (2013.01); C12Y 401/01024 (2013.01); C12Y 602/01011 (72) Inventors: Ka-Yiu San, Houston, TX (US); (2013.01); Y02E 50/17 (2013.01); Y02P 20/52 George N. Bennett, Houston, TX (US); (2015.11) Hui Wu, Houston, TX (US) (58) Field of Classification Search CPC .................................. C12P 7/56; C12N 15/70 (73) Assignee: William Marsh Rice University, Houston, TX (US) USPC .................... 435/108, 111, 115, 116, 252.33 See application file for complete search history. ( *) Notice: Subject to any disclaimer, the term ofthis patent is extended or adjusted under 35 (56) References Cited U.S.C. 154(b) by 130 days. U.S. PATENT DOCUMENTS (21) Appl. No.: 14/176,008 2004/0152159 Al 8/2004 Causey (22) Filed: Feb. 7, 2014 OTHER PUBLICATIONS (65) Prior Publication Data Wu et al. Biotechnology and bioengineering, (Aug. 2015) vol. 112, US 2014/0227745 Al Aug. 14, 2014 No. 8, pp. 1720-1726.* Alper H., Miyaoku K., Stephanopoulos G., (2005) Construction of Related U.S. Application Data lycopene overproducing E. coli strains by combining systematic and combinatorial gene knockout targets. Nat. Biotechnol. 23,612-616. -
Distribution of Cytochromes in Bacteria: Relationship to General Physiology DAVID J
INTERNATIONAL JOURNAL of SYSTEMATIC BACTERIOLOGY Vol. 23, No. 4 October 1973, p. 459-467 Prin ted in U.S.A. Copyright 0 1973 International Association of Microbiological Societies Distribution of Cytochromes in Bacteria: Relationship to General Physiology DAVID J. MEYER' and COLIN W. JONES Department of Biochemistry, The University of Leicester, England A review of cytochrome occurrence in bacteria is presented which gives the taxonomic distribution of cytochromes and which relates this to general physiological characteristics. Data obtained from published research and recent experimental studies on a total of 169 species of bacteria suggested the existence of four major groupings: (i) the aerobic and facultatively anaerobic, heterotrophic gram positives (cytochrome pattern aa3.0. b.c); (ii) the aerobic and facultatively anaerobic, heterotrophic gram negatives (cytochrome pattern either al.d.o.b.c, a1.o.b.c or aa3.o.b.c); (iii) anaerobic and microaerophilic hetero- trophs (cytochrome pattern b sometimes with al /d/o), and (iv) the ch'emo- and photo-autotrophs (cytochrome pattern c plus czl /aa3/o/b). The absence or minor presence of cytochrome c in facultatively anaerobic and anaerobic heterotrophs was confirmed and was also observed in plant and animal pathogens. Cytochrome d was confined in occurrence mainly to a small taxonomic group of organisms characterized by a high degree of adaptability to unstable habitats. This group was considered for further subdivision dependent upon the conditions causing the production of cytochrome d. As part of an investigation into the occur- ilated on organisms in the three major bacterial orders: rence of more than one spectral type of (i) the taxonomic status of the species according to cytochrome oxidase in many bacteria, a survey Bergey 's Manual of Determinative Bacteriology (13) of published data was carried out. -
JOURNAL of BACTERIOLOGY VOLUME 169 DECEMBER 1987 NUMBER 12 Samuel Kaplan, Editor in Chief (1992) Kenneth N
JOURNAL OF BACTERIOLOGY VOLUME 169 DECEMBER 1987 NUMBER 12 Samuel Kaplan, Editor in Chief (1992) Kenneth N. Timmis, Editor (1992) University of Illinois, Urbana Richard M. Losick, Editor (1988) Centre Medical Universitaire, James D. Friesen, Editor (1992) Harvard University, Cambridge, Mass. Geneva, Switzerland University of Toronto, L. Nicholas Ornston, Editor (1992) Graham C. Walker, Editor (1990) Toronto, Canada Yale University, New Haven, Conn. Massachusetts Institute of Stanley C. Holt, Editor (1987) Robert H. Rownd, Editor (1990) Technology, Cambridge, Mass. The University of Texas Health Northwestern Medical School, Robert A. Weisberg, Editor (1990) Science Center, San Antonio Chicago, Ill. National Institute of Child June J. Lascelles, Editor (1989) Health and Human University of California, Los Angeles Development, Bethesda, Md. EDITORIAL BOARD David Apirion (1988) James G. Ferry (1989) Eva R. Kashket (1987) Palmer Rogers (1987) Stuart J. Austin (1987) David Figurski (1987) David E. Kennell (1988) Barry P. Rosen (1989) Frederick M. Ausubel (1989) Timothy J. Foster (1989) Wil N. Konings (1987) Lucia B. Rothman-Denes (1989) Barbara Bachmann (1987) Robert T. Fraley (1988) Jordan Konisky (1987) Rudiger Schmitt (1989) Manfred E. Bayer (1988) David I. Friedman (1989) Dennis J. Kopecko (1987) June R. Scott (1987) Margret H. Bayer (1989) Masamitsu Futai (1988) Viji Krishnapillai (1988) Jane K. Setlow (1987) Claire M. Berg (1989) Robert Gennis (1988) Terry Krulwich (1987) Peter Setlow (1987) Helmut Bertrand (1988) Jane Gibson (1988) Lasse Lindahl (1987) James A. Shapiro (1988) Terry J. Beveridge (1988) Robert D. Goldman (1988) Jack London (1987) Louis A. Sherman (1988) Donald A. Bryant (1988) Susan Gottesman (1989) Sharon Long (1989) Howard A.