Induction of Multiple Matrix Metalloproteinases in Human
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The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections
toxins Review The Role of Streptococcal and Staphylococcal Exotoxins and Proteases in Human Necrotizing Soft Tissue Infections Patience Shumba 1, Srikanth Mairpady Shambat 2 and Nikolai Siemens 1,* 1 Center for Functional Genomics of Microbes, Department of Molecular Genetics and Infection Biology, University of Greifswald, D-17489 Greifswald, Germany; [email protected] 2 Division of Infectious Diseases and Hospital Epidemiology, University Hospital Zurich, University of Zurich, CH-8091 Zurich, Switzerland; [email protected] * Correspondence: [email protected]; Tel.: +49-3834-420-5711 Received: 20 May 2019; Accepted: 10 June 2019; Published: 11 June 2019 Abstract: Necrotizing soft tissue infections (NSTIs) are critical clinical conditions characterized by extensive necrosis of any layer of the soft tissue and systemic toxicity. Group A streptococci (GAS) and Staphylococcus aureus are two major pathogens associated with monomicrobial NSTIs. In the tissue environment, both Gram-positive bacteria secrete a variety of molecules, including pore-forming exotoxins, superantigens, and proteases with cytolytic and immunomodulatory functions. The present review summarizes the current knowledge about streptococcal and staphylococcal toxins in NSTIs with a special focus on their contribution to disease progression, tissue pathology, and immune evasion strategies. Keywords: Streptococcus pyogenes; group A streptococcus; Staphylococcus aureus; skin infections; necrotizing soft tissue infections; pore-forming toxins; superantigens; immunomodulatory proteases; immune responses Key Contribution: Group A streptococcal and Staphylococcus aureus toxins manipulate host physiological and immunological responses to promote disease severity and progression. 1. Introduction Necrotizing soft tissue infections (NSTIs) are rare and represent a more severe rapidly progressing form of soft tissue infections that account for significant morbidity and mortality [1]. -
Role of Extracellular Proteases in Biofilm Disruption of Gram Positive
e Engine ym er z in n g E Mukherji, et al., Enz Eng 2015, 4:1 Enzyme Engineering DOI: 10.4172/2329-6674.1000126 ISSN: 2329-6674 Review Article Open Access Role of Extracellular Proteases in Biofilm Disruption of Gram Positive Bacteria with Special Emphasis on Staphylococcus aureus Biofilms Mukherji R, Patil A and Prabhune A* Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune, India *Corresponding author: Asmita Prabhune, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Pune 411008, India, Tel: 91-020-25902239; Fax: 91-020-25902648; E-mail: [email protected] Rec date: December 28, 2014, Acc date: January 12, 2015, Pub date: January 15, 2015 Copyright: © 2015 Mukherji R, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Abstract Bacterial biofilms are multicellular structures akin to citadels which have individual bacterial cells embedded within a matrix of a self-synthesized polymeric or proteinaceous material. Since biofilms can establish themselves on both biotic and abiotic surfaces and that bacteria residing in these complex molecular structures are much more resistant to antimicrobial agents than their planktonic equivalents, makes these entities a medical and economic nuisance. Of late, several strategies have been investigated that intend to provide a sustainable solution to treat this problem. More recently role of extracellular proteases in disruption of already established bacterial biofilms and in prevention of biofilm formation itself has been demonstrated. The present review aims to collectively highlight the role of bacterial extracellular proteases in biofilm disruption of Gram positive bacteria. -
Mediate Immune Evasion Aureolysin Cleaves Complement C3 To
Staphylococcus aureus Metalloprotease Aureolysin Cleaves Complement C3 To Mediate Immune Evasion This information is current as Alexander J. Laarman, Maartje Ruyken, Cheryl L. Malone, of September 29, 2021. Jos A. G. van Strijp, Alexander R. Horswill and Suzan H. M. Rooijakkers J Immunol 2011; 186:6445-6453; Prepublished online 18 April 2011; doi: 10.4049/jimmunol.1002948 Downloaded from http://www.jimmunol.org/content/186/11/6445 Supplementary http://www.jimmunol.org/content/suppl/2011/04/18/jimmunol.100294 Material 8.DC1 http://www.jimmunol.org/ References This article cites 56 articles, 13 of which you can access for free at: http://www.jimmunol.org/content/186/11/6445.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision by guest on September 29, 2021 • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2011 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Staphylococcus aureus Metalloprotease Aureolysin Cleaves Complement C3 To Mediate Immune Evasion Alexander J. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
S. Aureus-Serine Protease-Like Protein B (Splb) Activates PAR2 and Induces Endothelial Barrier Dysfunction
bioRxiv preprint doi: https://doi.org/10.1101/2020.12.30.424670; this version posted January 4, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. S. aureus-serine protease-like protein B (SplB) activates PAR2 and induces endothelial barrier dysfunction Arundhasa Chandrabalan1, Pierre E Thibeault1, Stefanie Deinhardt-Emmer2, Maria Nordengrün3, Jawad Iqbal3, Daniel M Mrochen3, Laura A Mittmann4, 5, Bishwas Chamling6, 7, Christoph A Reichel4, 5, Rithwik Ramachandran1, Barbara M Bröker3, Murty N Darisipudi3 1Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Ontario, Canada 2Section of Experimental Virology, Institute of Medical Microbiology, University Hospital Jena, Jena, Germany 3Department of Immunology, Institute of Immunology and Transfusion Medicine, University Medicine Greifswald, Greifswald, Germany 4Department of Otorhinolaryngology, University Hospital, Ludwig-Maximilians-University Munich, Munich, Germany 5Walter Brendel Centre of Experimental Medicine, University Hospital, Ludwig-Maximilians- University Munich, Munich, Germany 6Department of Cardiology, Internal Medicine B, University Medicine Greifswald, Greifswald, Germany 7DZHK (German Centre for Cardiovascular Research), Partner Site Greifswald, Germany *Correspondence: Dr. V.S. Narayana Murty Darisipudi [email protected] Address: Department of Immunology Institute of Immunology and Transfusion Medicine University Medicine Greifswald F. Sauerbruchstr. DZ 7 17475 Greifswald, Germany Keywords: Staphylococcus aureus, SplB, endothelial damage, proteinase-activated receptor 2, PAR2, G-protein-coupled receptors, cytokines Running title: SplB mediates endothelial inflammation via PAR2 bioRxiv preprint doi: https://doi.org/10.1101/2020.12.30.424670; this version posted January 4, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. -
Regulatory Rnas in Staphylococcus Aureus: Function and Mechanism
Regulatory RNAs in Staphylococcus aureus : Function and Mechanism Thao Nguyen Le Lam To cite this version: Thao Nguyen Le Lam. Regulatory RNAs in Staphylococcus aureus : Function and Mechanism. Agri- cultural sciences. Université Paris Sud - Paris XI, 2015. English. NNT : 2015PA112216. tel- 01424170 HAL Id: tel-01424170 https://tel.archives-ouvertes.fr/tel-01424170 Submitted on 2 Jan 2017 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. UNIVERSITÉ PARIS SACLAY - UNIVERSITÉ PARIS SUD UFR SCIENTIFIQUE D’ORSAY - ÉCOLE DOCTORALE STRUCTURE ET DYNAMIQUE DES SYSTÈMES VIVANTS Thèse Présentée pour obtenir le grade de DOCTEUR EN SCIENCES DE L’UNIVERSITÉ PARIS SUD Le 24 septembre 2015 Characterization of regulatory RNAs in Staphylococcus aureus Thao Nguyen LE LAM Directeur de thèse : Dr. Philippe BOULOC Laboratoire d’accueil : Signalisation et Réseaux de Régulations Bactériens Institute for Integrative Biology of the Cell (I2BC) CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, Orsay, France Composition du jury : Président du jury Pr. Nicolas BAYAN Rapporteur Dr. Maude GUILLIER Rapporteur Dr. Francis REPOILA Examinateur Pr. Brice FELDEN Examinateur Dr. Nara FIGUEROA-BOSSI Directeur de thèse Dr. Philippe BOULOC 1 2 TABLE OF CONTENTS FIGURES AND TABLES ......................................................................................................... -
Virulence Characteristics of Meca-Positive Multidrug-Resistant Clinical Coagulase-Negative Staphylococci
microorganisms Article Virulence Characteristics of mecA-Positive Multidrug-Resistant Clinical Coagulase-Negative Staphylococci Jung-Whan Chon 1, Un Jung Lee 2, Ryan Bensen 3, Stephanie West 4, Angel Paredes 5, Jinhee Lim 5, Saeed Khan 1, Mark E. Hart 1,6, K. Scott Phillips 7 and Kidon Sung 1,* 1 Division of Microbiology, National Center for Toxicological Research, US Food and Drug Administration, Jefferson, AR 72079, USA; [email protected] (J.-W.C.); [email protected] (S.K.); [email protected] (M.E.H.) 2 Division of Cardiology, Albert Einstein College of Medicine, Bronx, NY 10461, USA; [email protected] 3 Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA; [email protected] 4 Department of Animal Science, University of Arkansas, Fayetteville, AR 72701, USA; [email protected] 5 NCTR-ORA Nanotechnology Core Facility, US Food and Drug Administration, Jefferson, AR 72079, USA; [email protected] (A.P.); [email protected] (J.L.) 6 Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA 7 Division of Biology, Chemistry, and Materials Science, Office of Science and Engineering Laboratories, Center for Devices and Radiological Health, US Food and Drug Administration, Silver Spring, MD 20993, USA; [email protected] * Correspondence: [email protected]; Tel.: +1-(870)-543-7527 Received: 20 March 2020; Accepted: 29 April 2020; Published: 1 May 2020 Abstract: Coagulase-negative staphylococci (CoNS) are an important group of opportunistic pathogenic microorganisms that cause infections in hospital settings and are generally resistant to many antimicrobial agents. -
Development of a Vaccine Against
FEMS Microbiology Reviews, fuz030, 44, 2020, 123–153 doi: 10.1093/femsre/fuz030 Advance Access Publication Date: 16 December 2019 Review Article REVIEW ARTICLE Development of a vaccine against Staphylococcus Downloaded from https://academic.oup.com/femsre/article/44/1/123/5679032 by guest on 28 September 2021 aureus invasive infections: Evidence based on human immunity, genetics and bacterial evasion mechanisms Lloyd S. Miller1,2,3,4,5,*, Vance G. Fowler, Jr.6,7, Sanjay K. Shukla8,9,Warren E. Rose10,11 and Richard A. Proctor10,12 1Immunology, Janssen Research and Development, 1400 McKean Road, Spring House, PA, 19477, USA, 2Department of Dermatology, Johns Hopkins University School of Medicine, 1550 Orleans Street, Cancer Research Building 2, Suite 209, Baltimore, MD, 21231, USA, 3Department of Medicine, Division of Infectious Diseases, Johns Hopkins University School of Medicine, 1830 East Monument Street, Baltimore, MD, 21287, USA, 4Department of Orthopaedic Surgery, Johns Hopkins University School of Medicine, 601 North Caroline Street , Baltimore, MD, 21287, USA, 5Department of Materials Science and Engineering, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD, 21218, USA, 6Department of Medicine, Division of Infectious Diseases, Duke University Medical Center, 315 Trent Drive, Hanes House, Durham, NC, 27710, USA, 7Duke Clinical Research Institute, Duke University Medical Center, 40 Duke Medicine Circle, Durham, NC, 27710, USA, 8Center for Precision Medicine Research, Marshfield Clinic Research Institute, 1000 North -
Enzymes for Cell Dissociation and Lysis
Issue 2, 2006 FOR LIFE SCIENCE RESEARCH DETACHMENT OF CULTURED CELLS LYSIS AND PROTOPLAST PREPARATION OF: Yeast Bacteria Plant Cells PERMEABILIZATION OF MAMMALIAN CELLS MITOCHONDRIA ISOLATION Schematic representation of plant and bacterial cell wall structure. Foreground: Plant cell wall structure Background: Bacterial cell wall structure Enzymes for Cell Dissociation and Lysis sigma-aldrich.com The Sigma Aldrich Web site offers several new tools to help fuel your metabolomics and nutrition research FOR LIFE SCIENCE RESEARCH Issue 2, 2006 Sigma-Aldrich Corporation 3050 Spruce Avenue St. Louis, MO 63103 Table of Contents The new Metabolomics Resource Center at: Enzymes for Cell Dissociation and Lysis sigma-aldrich.com/metpath Sigma-Aldrich is proud of our continuing alliance with the Enzymes for Cell Detachment International Union of Biochemistry and Molecular Biology. Together and Tissue Dissociation Collagenase ..........................................................1 we produce, animate and publish the Nicholson Metabolic Pathway Hyaluronidase ...................................................... 7 Charts, created and continually updated by Dr. Donald Nicholson. DNase ................................................................. 8 These classic resources can be downloaded from the Sigma-Aldrich Elastase ............................................................... 9 Web site as PDF or GIF files at no charge. This site also features our Papain ................................................................10 Protease Type XIV -
The Genera Staphylococcus and Macrococcus
Prokaryotes (2006) 4:5–75 DOI: 10.1007/0-387-30744-3_1 CHAPTER 1.2.1 ehT areneG succocolyhpatS dna succocorcMa The Genera Staphylococcus and Macrococcus FRIEDRICH GÖTZ, TAMMY BANNERMAN AND KARL-HEINZ SCHLEIFER Introduction zolidone (Baker, 1984). Comparative immu- nochemical studies of catalases (Schleifer, 1986), The name Staphylococcus (staphyle, bunch of DNA-DNA hybridization studies, DNA-rRNA grapes) was introduced by Ogston (1883) for the hybridization studies (Schleifer et al., 1979; Kilp- group micrococci causing inflammation and per et al., 1980), and comparative oligonucle- suppuration. He was the first to differentiate otide cataloguing of 16S rRNA (Ludwig et al., two kinds of pyogenic cocci: one arranged in 1981) clearly demonstrated the epigenetic and groups or masses was called “Staphylococcus” genetic difference of staphylococci and micro- and another arranged in chains was named cocci. Members of the genus Staphylococcus “Billroth’s Streptococcus.” A formal description form a coherent and well-defined group of of the genus Staphylococcus was provided by related species that is widely divergent from Rosenbach (1884). He divided the genus into the those of the genus Micrococcus. Until the early two species Staphylococcus aureus and S. albus. 1970s, the genus Staphylococcus consisted of Zopf (1885) placed the mass-forming staphylo- three species: the coagulase-positive species S. cocci and tetrad-forming micrococci in the genus aureus and the coagulase-negative species S. epi- Micrococcus. In 1886, the genus Staphylococcus dermidis and S. saprophyticus, but a deeper look was separated from Micrococcus by Flügge into the chemotaxonomic and genotypic proper- (1886). He differentiated the two genera mainly ties of staphylococci led to the description of on the basis of their action on gelatin and on many new staphylococcal species. -
A Novel Abi-Domain Protein Controls Virulence Determinant Production
University of South Florida Scholar Commons Graduate Theses and Dissertations Graduate School 3-22-2017 A Novel Abi-domain Protein Controls Virulence Determinant Production in Staphylococcus aureus Stephanie Michelle Marroquin University of South Florida, [email protected] Follow this and additional works at: http://scholarcommons.usf.edu/etd Part of the Microbiology Commons, Molecular Biology Commons, and the Public Health Commons Scholar Commons Citation Marroquin, Stephanie Michelle, "A Novel Abi-domain Protein Controls Virulence Determinant Production in Staphylococcus aureus" (2017). Graduate Theses and Dissertations. http://scholarcommons.usf.edu/etd/6725 This Thesis is brought to you for free and open access by the Graduate School at Scholar Commons. It has been accepted for inclusion in Graduate Theses and Dissertations by an authorized administrator of Scholar Commons. For more information, please contact [email protected]. A Novel Abi-domain Protein Controls Virulence Determinant Production in Staphylococcus aureus by Stephanie M. Marroquin A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science in Public Health with a concentration in Global Communicable Diseases Department of Global Health College of Public Health University of South Florida Major Professor: Lindsey N. Shaw, Ph.D. Thomas R. Unnasch, Ph.D. John H. Adams, Ph.D. Date of Approval: March 16, 2017 Keywords: Pathogenesis, Blood Survival, Mass Spectrometry, Macrophage Infection, Site-Directed Mutagenesis, agr Quorum Sensing Copyright © 2017, Stephanie M. Marroquin Acknowledgments Many people deserve acknowledgements for the guidance and support they have provided throughout my master’s degree program. Firstly, I would like to thank my major professor Dr. -
Airway Microbiota Signals Anabolic and Catabolic Remodeling in the Transplanted Lung
Airway microbiota signals anabolic and catabolic remodeling in the transplanted lung Stephane Mouraux, MD,a* Eric Bernasconi, PhD,a*Celine Pattaroni, MSc,a Angela Koutsokera, MD, PhD,a John-David Aubert, MD,a Johanna Claustre, MD,b,c,d Christophe Pison, MD, PhD,b,c,d Pierre-Joseph Royer, PhD,e Antoine Magnan, MD,e Romain Kessler, MD, PhD,f Christian Benden, MD, FCCP,g Paola M. Soccal, MD,h Benjamin J. Marsland, PhD,aà and Laurent P. Nicod, MD,aà on behalf of the SysCLAD Consortium§ Lausanne, Zurich, and Geneva, Switzerland; and Grenoble, Saint Martin d’Heres, Nantes, and Strasbourg, France GRAPHICAL ABSTRACT Microbiota Impact on Airway Remodeling Microbiota: Prevotella, Streptococcus Veillonella, Neisseria Lung Bacterial transplant communities Staphylococcus, Pseudomonas Haemophilus, Corynebacterium Broncho- alveolar Host: M2 macrophage Myofibroblast lavage Cell differential M1 macrophage Neutrophil Fibroblast Gene Platelet-derived growth factor Thrombospondin expression Matrix metalloproteinases Osteopontin Pulmonary alveolus Capillary Extracellular Matrix Collagen Anabolic Fibronectin Remodeling Homeostasis Catabolic Remodeling Type I cell Type II cell Background: Homeostatic turnover of the extracellular matrix for a heterogeneous entity ultimately associated with conditions the structure and function of the healthy lung. In pathological airway and/or parenchyma remodeling. lung transplantation, long-term management remains limited Objective: This study assessed whether the local cross-talk by chronic lung allograft dysfunction, an umbrella term used between the pulmonary microbiota and host cells is a key From athe Service de Pneumologie, Centre Hospitalier Universitaire Vaudois, Lausanne; Thoracic Society for this work. E. Bernasconi’s institution received grant no. 305457, bthe Clinique Universitaire de Pneumologie, Pole^ Thorax et Vaisseaux, Centre Hospi- SysCLAD Consortium from European Commission FP7; grant no.