Structural Basis for Tuning Activity and Membrane Specificity of Bacterial
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(12) United States Patent (10) Patent No.: US 8,585,627 B2 Dacey, Jr
US008585627B2 (12) United States Patent (10) Patent No.: US 8,585,627 B2 Dacey, Jr. et al. (45) Date of Patent: Nov. 19, 2013 (54) SYSTEMS, DEVICES, AND METHODS (51) Int. Cl. INCLUDING CATHETERS CONFIGURED TO A6B 9/00 (2006.01) MONITOR BOFILMI FORMATION HAVING (52) U.S. Cl. BOFILMI SPECTRAL INFORMATION USPC ................................... 604/8; 604/6.08; 604/9 CONFIGURED ASA DATASTRUCTURE (58) Field of Classification Search USPC ........................................... 604/6.08, 8, 9, 20 (75) Inventors: Ralph G. Dacey, Jr., St. Louis,MO See application file for complete search history. (US); Roderick A. Hyde, Redmond, WA (US); Muriel Y. Ishikawa, Livermore, CA (US); Jordin T. Kare, Seattle, WA (56) References Cited (US); Eric C. Leuthardt, St. Louis,MO U.S. PATENT DOCUMENTS (US); Nathan P. Myhrvold, Bellevue, WA (US); Dennis J. Rivet, Chesapeake, 3,274.406 A 9/1966 Sommers, Jr. VA (US); Michael A. Smith, Phoenix, 3,825,016 A 7, 1974 Lale et al. AZ (US); Elizabeth A. Sweeney, Seattle, (Continued) WA (US); Clarence T. Tegreene, Bellevue, WA (US); Lowell L. Wood, FOREIGN PATENT DOCUMENTS Jr., Bellevue, WA (US); Victoria Y. H. EP 1614 442 A2 1, 2006 Wood, Livermore, CA (US) WO WO91,06855 A2 5, 1991 (73) Assignee: The Invention Science Fund I, LLC (Continued) (*) Notice: Subject to any disclaimer, the term of this OTHER PUBLICATIONS patent is extended or adjusted under 35 PCT International Search Report; International App. No. PCT/ U.S.C. 154(b) by 291 days. US2010/003088; Apr. 1, 2011; pp. 1-4. (21) Appl. No.: 12/927,294 (Continued) (22) Filed: Nov. -
Role of Perforin-2 in Regulating Type I Interferon Signaling
https://www.scientificarchives.com/journal/journal-of-cellular-immunology Journal of Cellular Immunology Review Article Role of Perforin-2 in Regulating Type I Interferon Signaling Gregory V Plano, Noula Shembade* Department of Microbiology and Immunology, Sylvester Comprehensive Cancer Center Miller School of Medicine, University of Miami, Miami, FL 33136, USA *Correspondence should be addressed to Noula Shembade; [email protected] Received date: November 21, 2020, Accepted date: February 02, 2021 Copyright: © 2021 Plano G, 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 Sepsis is a systemic inflammatory response caused by a harmful host immune reaction that is activated in response to microbial infections. Infection-induced type I interferons (IFNs) play critical roles during septic shock. Type I IFNs initiate their biological effects by binding to their transmembrane interferon receptors and initiating the phosphorylation and activation of tyrosine kinases TYK2 and JAK1, which promote phosphorylation and activation of STAT molecules. Type I IFN-induced activation of JAK/STAT pathways is a complex process and not well understood. Improper regulation of type I IFN responses can lead to the development of infectious and inflammation-related diseases, including septic shock, autoimmune diseases, and inflammatory syndromes. This review is mainly focused on the possible mechanistic roles of the transmembrane Perforin-2 molecule in the regulation of type I IFN- induced signaling. Keywords: JAK/STAT, Interferons, TYK2, STATs, Perforin-2, IFNAR1, IFNAR2 and Signaling Introduction and activator of transcription 2), respectively, under normal physiological conditions [4,5]. -
Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins
Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins. Robert Frangež, Dušan Šuput, Jordi Molgó, Evelyne Benoit To cite this version: Robert Frangež, Dušan Šuput, Jordi Molgó, Evelyne Benoit. Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins.. Toxins, MDPI, 2017, 9 (4), 10.3390/toxins9040128. hal-01572247 HAL Id: hal-01572247 https://hal.archives-ouvertes.fr/hal-01572247 Submitted on 20 May 2020 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. toxins Review Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins Robert Frangež 1, Dušan Šuput 2, Jordi Molgó 3 and Evelyne Benoit 3,* 1 Institute of Preclinical Sciences, Veterinary Faculty, University of Ljubljana; 1115-Ljubljana, Slovenia; [email protected] 2 Laboratory for Cell Physiology and Toxinology, Institute of Pathophysiology, School of Medicine, University of Ljubljana, P.O. Box 11, 1105-Ljubljana, Slovenia; [email protected] 3 DRF/Institut de Sciences de la Vie Frédéric Joliot/SIMOPRO, CEA de Saclay, and Institut des Neurosciences Paris-Saclay (Neuro-PSI), UMR 9197 CNRS/Université Paris-Sud, 91190 Gif-sur-Yvette, France; [email protected] * Correspondence: [email protected]; Tel.: +33-169-085-685 Academic Editor: Michel R. -
Le Fonctionnement Du Transporteur ABC De Streptococcus Pneumoniae Impliqué Dans La Résistance Contre Les Peptides Antimicrobiens Jaroslav Vorac
Le fonctionnement du transporteur ABC de Streptococcus pneumoniae impliqué dans la résistance contre les peptides antimicrobiens Jaroslav Vorac To cite this version: Jaroslav Vorac. Le fonctionnement du transporteur ABC de Streptococcus pneumoniae impliqué dans la résistance contre les peptides antimicrobiens. Biologie moléculaire. Université Grenoble Alpes, 2016. Français. NNT : 2016GREAV009. tel-01503129 HAL Id: tel-01503129 https://tel.archives-ouvertes.fr/tel-01503129 Submitted on 6 Apr 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. THÈSE Pour obtenir le grade de DOCTEUR DE L’UNIVERSITÉ GRENOBLE ALPES Spécialité : Biologie Structurale et Nanobiologie Arrêté ministériel : 7 août 2006 Présentée par Jaroslav VORÁ! Thèse dirigée par Dr. Jean-Michel JAULT et codirigée par Dr. Claire DURMORT préparée au sein d e l’ Institut de Biologie Structurale dans l'École Doctorale Chimie et Sciences d u Vivant Le fonctionnement du transporteur ABC de Streptococcus pneumoniae impliqué dans la résistance contre les peptides antimicrobiens 7KqVHVRXWHQXHSXEOLTXHPHQWOHDYULO Jury composé de : Prof. Tino KRELL Rapporteur Dr. Marc PRUDHOMME Rapporteur Dr. Guillaume LENOIR Examinateur Prof. Dominique SCHNEIDER 3UpVLGHQW Dr. Jean-Michel Jault Directeur de th qse Dr. Claire Durmort Co-directrice de th qse THESIS To obtain the degree of DOCTOR of PHILOSOPHY of the UNIVERSITY GRENOBLE ALPES Speciality : Structural Biology and Nanobiology Arrêté ministériel : 7 août 2006 Presented by Jaroslav VORÁ! Thesis directed by Dr. -
Response of Cellular Innate Immunity to Cnidarian Pore-Forming Toxins
Review Response of Cellular Innate Immunity to Cnidarian Pore-Forming Toxins Wei Yuen Yap 1 and Jung Shan Hwang 2,* 1 Department of Biological Sciences, School of Science and Technology, Sunway University, No. 5 Jalan Universiti, Bandar Sunway, Selangor Darul Ehsan 47500, Malaysia; [email protected] 2 Department of Medical Sciences, School of Healthcare and Medical Sciences, Sunway University, No. 5 Jalan Universiti, Bandar Sunway, Selangor Darul Ehsan 47500, Malaysia * Correspondence: [email protected]; Tel.: +603-7491-8622 (ext. 7414) Academic Editor: Jean-Marc Sabatier Received: 23 August 2018; Accepted: 28 September 2018; Published: 4 October 2018 Abstract: A group of stable, water-soluble and membrane-bound proteins constitute the pore forming toxins (PFTs) in cnidarians. They interact with membranes to physically alter the membrane structure and permeability, resulting in the formation of pores. These lesions on the plasma membrane causes an imbalance of cellular ionic gradients, resulting in swelling of the cell and eventually its rupture. Of all cnidarian PFTs, actinoporins are by far the best studied subgroup with established knowledge of their molecular structure and their mode of pore-forming action. However, the current view of necrotic action by actinoporins may not be the only mechanism that induces cell death since there is increasing evidence showing that pore-forming toxins can induce either necrosis or apoptosis in a cell-type, receptor and dose-dependent manner. In this review, we focus on the response of the cellular immune system to the cnidarian pore-forming toxins and the signaling pathways that might be involved in these cellular responses. -
Stonefish Toxin Defines an Ancient Branch of the Perforin-Like Superfamily
Stonefish toxin defines an ancient branch of the perforin-like superfamily Andrew M. Ellisdona,b, Cyril F. Reboula,b, Santosh Panjikara,c, Kitmun Huynha, Christine A. Oelliga, Kelly L. Wintera,d, Michelle A. Dunstonea,b,e, Wayne C. Hodgsond, Jamie Seymourf, Peter K. Deardeng, Rodney K. Twetenh, James C. Whisstocka,b,1,2, and Sheena McGowane,1,2 aBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; bAustralian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, 3800, Australia; cAustralian Synchrotron, Macromolecular Crystallography, Melbourne, VIC, 3168, Australia; dBiomedicine Discovery Institute and Department of Pharmacology, Monash University, Melbourne, VIC, 3800, Australia; eBiomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia; fCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD, 4870, Australia; gDepartment of Biochemistry and Genetics Otago, University of Otago, Dunedin, 9054 Aotearoa–New Zealand; and hDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104 Edited by Brenda A. Schulman, St. Jude Children’s Research Hospital, Memphis, TN, and approved November 3, 2015 (received for review April 19, 2015) The lethal factor in stonefish venom is stonustoxin (SNTX), a parallel interface along their entire 115-Å length (2,908 Å2 heterodimeric cytolytic protein that induces cardiovascular collapse buried surface area) (Fig. 1 A–D and Fig. S1). Fold recognition in humans and native predators. Here, using X-ray crystallography, searches reveal that each SNTX protein comprises four do- we make the unexpected finding that SNTX is a pore-forming mains (Fig. -
Measuring Kinetic Drivers of Pneumolysin Pore Structure
Eur Biophys J (2016) 45:365–376 DOI 10.1007/s00249-015-1106-x ORIGINAL ARTICLE Measuring kinetic drivers of pneumolysin pore structure Robert J. C. Gilbert1 · Andreas F.-P. Sonnen2 Received: 7 October 2015 / Revised: 1 December 2015 / Accepted: 7 December 2015 / Published online: 23 February 2016 © The Author(s) 2016. This article is published with open access at Springerlink.com Abstract Most membrane attack complex-perforin/ Keywords Pore formation · Kinetics · MACPF/CDC · cholesterol-dependent cytolysin (MACPF/CDC) proteins Toroidal pore · Oligomerization · Membrane structure are thought to form pores in target membranes by assem- bling into pre-pore oligomers before undergoing a pre-pore to pore transition. Assembly during pore formation is into Introduction both full rings of subunits and incomplete rings (arcs). The balance between arcs and full rings is determined by The membrane attack complex-perforin/cholesterol- a mechanism dependent on protein concentration in which dependent cytolysin (MACPF/CDC) family is the largest- arc pores arise due to kinetic trapping of the pre-pore forms known group of pore-forming proteins (Anderluh and by the depletion of free protein subunits during oligomeri- Gilbert 2014; Gilbert et al. 2013). Members have been zation. Here we describe the use of a kinetic assay to study identified in every kind of cellular life form apart from the pore formation in red blood cells by the MACPF/CDC Archaebacteria, and within their producing organisms they pneumolysin from Streptococcus pneumoniae. We show enact a plethora of different biological functions (Ander- that cell lysis displays two kinds of dependence on pro- luh et al. -
Innate Immunology, Lecture 5: Barrier Epithelia and Antimicrobial Peptides
Stanford Microbiology and Immunology 104/204: Innate Immunology, Lecture 5: Barrier epithelia and antimicrobial peptides Structure of a lung Trachea lead to bronchi to bronchioles to alveoli It is a dead-end structure that must deal with inhaled particles which would otherwise accumulate in the alveolae Mucus escalator In the bronchioles the mucus escalator moves material up to the throat. This escalator functions in the eustachian tubes, nose and lungs Think of the escalator as moving flypaper that traps particles and moves them out of the lung. The bronchiolar epithelia are composed of epithelia cells with many cilia, goblet cells that secrete mucus and mucus glands In an uninfected state the mucus glands produce most of the mucus but during an infection the goblet cells are induced to produce large amounts of mucus resulting in the production of phlegm. Alveoli This is the location where oxygen and carbon dioxide are exchanged. A thin epithelium is in close contact with capillaries, allowing rapid gas exchange. Alveolar lumen contains Macrophages Complement Antibodies- IgA Surfactant – also an opsonizing lectin Alveolus is a dead end – it contains no cilia and cannot cough things out; Particles must be removed by macrophages Infection and biowarfare considerations Particles above a certain size (~10 um) will contact the mucus-lined walls of the bronchioles and be swept from the lungs. Inhaled pathogens that survive in the alveolae must be smaller than this – in the 1-5 µm range we remember from the anthrax mail case. How do you defeat -
Structural Basis for Tuning Activity and Membrane Specificity of Bacterial
bioRxiv preprint doi: https://doi.org/10.1101/2020.06.16.154724; this version posted June 17, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. 1 Structural basis for tuning activity and membrane specificity of bacterial 2 cytolysins 3 4 5 Authors: Nita R. Shah1, Tomas B. Voisin1, Edward S. Parsons2, Courtney M. Boyd1, Bart W. 6 Hoogenboom2,3, Doryen Bubeck1* 7 8 Affiliations: 9 1 Department of Life Sciences, Sir Ernst Chain Building, Imperial College London, London, SW7 10 2AZ, UK 11 2 London Centre for Nanotechnology, University College London, London, WC1H 0AH, UK 12 3 Department of Physics and Astronomy, University College London, Gower Street, London, 13 WC1E 6BT, UK 14 15 16 *Contact Information: [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.06.16.154724; this version posted June 17, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. 17 ABSTRACT 18 Cholesterol-dependent cytolysins (CDCs) form protein nanopores to lyse cells. They target 19 eukaryotic cells using different mechanisms, but all require the presence of cholesterol to pierce 20 lipid bilayers. How CDCs use cholesterol to selectively lyse cells is essential for understanding 21 virulence strategies of several pathogenic bacteria, and for repurposing CDCs to kill new cellular 22 targets. -
Mammalian Neuropeptides As Modulators of Microbial Infections: Their Dual Role in Defense Versus Virulence and Pathogenesis
International Journal of Molecular Sciences Review Mammalian Neuropeptides as Modulators of Microbial Infections: Their Dual Role in Defense versus Virulence and Pathogenesis Daria Augustyniak 1,* , Eliza Kramarska 1,2, Paweł Mackiewicz 3, Magdalena Orczyk-Pawiłowicz 4 and Fionnuala T. Lundy 5 1 Department of Pathogen Biology and Immunology, Faculty of Biology, University of Wroclaw, 51-148 Wroclaw, Poland; [email protected] 2 Institute of Biostructures and Bioimaging, Consiglio Nazionale delle Ricerche, 80134 Napoli, Italy 3 Department of Bioinformatics and Genomics, Faculty of Biotechnology, University of Wroclaw, 50-383 Wroclaw, Poland; pamac@smorfland.uni.wroc.pl 4 Department of Chemistry and Immunochemistry, Wroclaw Medical University, 50-369 Wroclaw, Poland; [email protected] 5 Wellcome-Wolfson Institute for Experimental Medicine, School of Medicine, Dentistry and Biomedical Sciences, Queen’s University Belfast, Belfast BT9 7BL, UK; [email protected] * Correspondence: [email protected]; Tel.: +48-71-375-6296 Abstract: The regulation of infection and inflammation by a variety of host peptides may represent an evolutionary failsafe in terms of functional degeneracy and it emphasizes the significance of host defense in survival. Neuropeptides have been demonstrated to have similar antimicrobial activities to conventional antimicrobial peptides with broad-spectrum action against a variety of microorganisms. Citation: Augustyniak, D.; Neuropeptides display indirect anti-infective capacity via -
Pore-Forming Proteins and Adaptation of Living Organisms to Environmental Conditions
ISSN 0006-2979, Biochemistry (Moscow), 2008, Vol. 73, No. 13, pp. 1473-1492. © Pleiades Publishing, Ltd., 2008. Original Russian Text © Zh. I. Andreeva-Kovalevskaya, A. S. Solonin, E. V. Sineva, V. I. Ternovsky, 2008, published in Uspekhi Biologicheskoi Khimii, 2008, Vol. 48, pp. 267-318. REVIEW Pore-Forming Proteins and Adaptation of Living Organisms to Environmental Conditions Zh. I. Andreeva-Kovalevskaya1, A. S. Solonin1*, E. V. Sineva1, and V. I. Ternovsky2* 1Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: [email protected] 2Institute of Cell Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: [email protected] Received July 16, 2008 Revision received August 4, 2008 Abstract—Pore-forming proteins are powerful “tools” for adaptation of living organisms to environmental conditions. A wide range of these proteins isolated from various sources, from viruses to mammals, has been used for the analysis of their role in the processes of intra- and inter-species competition, defense, attack, and signaling. Here we review a large number of pore-forming proteins from the perspective of their functions, structures, and mechanisms of membrane penetration. Various mechanisms of cell damage, executed by these proteins in the course of formation of a pore and after its passing to conducting state, have been considered: endo- and exocytosis, lysis, necrosis, apoptosis, etc. The role of pore-forming pro- teins in evolution is discussed. The relevance of practical application of pore formers has been shown, including application in nanotechnological constructions. DOI: 10.1134/S0006297908130087 Key words: pore-forming proteins, adaptation, pore structure, apoptosis, nanotechnology The cell membrane is the primary barrier in contacts branes more permeable for ions by shifting osmotic equi- of a living organism with the environment or other librium of the cell, thereby causing its swelling followed species. -
The Cholesterol-Dependent Cytolysins Family of Gram-Positive Bacterial Toxins
Chapter 20 Submitted July 2009 The cholesterol-dependent cytolysins family of Gram-positive bacterial toxins Alejandro P. Heuck, Paul C. Moe, and Benjamin B. Johnson Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, U.S.A. [email protected] Abstract The cholesterol-dependent cytolysins (CDC) are a family of β-barrel pore- forming toxins secreted by Gram-positive bacteria. These toxins are produced as water- soluble monomeric proteins that after binding to the target cell oligomerize on the membrane surface forming a ring-like pre-pore complex, and finally insert a large β-barrel into the membrane (about 250 Å in diameter). Formation of such a large transmembrane structure requires multiple and coordinated conformational changes. The presence of cholesterol in the target membrane is absolutely required for pore-formation, and therefore it was long thought that cholesterol was the cellular receptor for these toxins. However, not all the CDC require cholesterol for binding. Intermedilysin, secreted by Streptoccocus intermedius only binds to membranes containing a protein receptor, but forms pores only if the membrane contains sufficient cholesterol. In contrast, perfringolysin O, secreted by Clostridium perfringens, only binds to membranes containing substantial amounts of cholesterol. The mechanisms by which cholesterol regulates the cytolytic activity of the CDC are not understood at the molecular level. The C-terminus of perfringolysin O is involved in cholesterol recognition, and changes in the conformation of the loops located at the distal tip of this domain affect the 1 toxin-membrane interactions. At the same time, the distribution of cholesterol in the membrane can modulate toxin binding.