The Variable Internal Structure of the Mycoplasma Penetrans
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Universidade Federal Do Rio Grande Do Sul Centro De Biotecnologia Programa De Pós-Graduação Em Biologia Celular E Molecular
UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL CENTRO DE BIOTECNOLOGIA PROGRAMA DE PÓS-GRADUAÇÃO EM BIOLOGIA CELULAR E MOLECULAR Caracterização Molecular do Microbioma Hospitalar por Sequenciamento de Alto Desempenho Tese de Doutorado Pabulo Henrique Rampelotto Porto Alegre 2019 UNIVERSIDADE FEDERAL DO RIO GRANDE DO SUL CENTRO DE BIOTECNOLOGIA PROGRAMA DE PÓS-GRADUAÇÃO EM BIOLOGIA CELULAR E MOLECULAR Caracterização Molecular do Microbioma Hospitalar por Sequenciamento de Alto Desempenho Tese submetida ao Programa de Pós-Graduação em Biologia Celular e Molecular da UFRGS, como requisito parcial para a obtenção do grau de Doutor em Ciências Pabulo Henrique Rampelotto Orientador: Dr. Rogério Margis Porto Alegre, Abril de 2019 Instituições e fontes financiadoras: Instituições: Laboratório de Genomas e Populações de Plantas (LGPP), Departamento de Biofísica, UFRGS – Porto Alegre/RS, Brasil. Neoprospecta Microbiome Technologies SA – Florianópolis/SC, Brasil. Hospital Universitário Polydoro Ernani de São Thiago, Universidade Federal de Santa Catarina (UFSC) – Florianópolis/SC, Brasil. Fontes financiadoras: Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), Brasil. Agradecimentos Aos meus familiares, pelo suporte incondicional em todos os momentos de minha vida. Ao meu orientador Prof. Rogério Margis, pela oportunidade e confiança. Aos colegas de laboratório, pelo apoio e amizade. Ao Programa de Pós-Graduação em Biologia Celular e Molecular, por todo o suporte. Aos inúmeros autores e co-autores que participaram dos meus diversos projetos editoriais, pelas brilhantes discussões em temas tão fascinantes. Enfim, a todos que, de alguma forma, contribuíram para a realização deste trabalho. “A tarefa não é tanto ver aquilo que ninguém viu, mas pensar o que ninguém ainda pensou sobre aquilo que todo mundo vê” (Arthur Schopenhauer) SUMÁRIO LISTA DE ABREVIATURAS .......................................................................................... -
Movements of Mycoplasma Mobile Gliding Machinery Detected by High
bioRxiv preprint doi: https://doi.org/10.1101/2021.01.28.428740; this version posted January 29, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.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 4.0 International license. 1 mBio (Research Article) 2 3 Movements of Mycoplasma mobile gliding machinery detected by 4 high-speed atomic force microscopy 5 Kohei Kobayashia*, Noriyuki Koderab*, Taishi Kasaia, Yuhei O Taharaa,c, Takuma 6 Toyonagaa, Masaki Mizutania, Ikuko Fujiwaraa, Toshio Andob, Makoto Miyataa,c,# 7 8 aGraduate School of Science, Osaka City University, 3-3-138 Sugimoto, 9 Sumiyoshi-ku, Osaka 558-8585, Japan. 10 bNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-chou, 11 Kanazawa, Ishikawa 920-1192, Japan. 12 cThe OCU Advanced Research Institute for Natural Science and Technology 13 (OCARINA), Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 14 558-8585, Japan. 15 16 Address correspondence to Makoto Miyata, [email protected] 17 *These authors contributed equally to this work. 18 Present address: Taishi Kasai: Department of Life Science, Rikkyo University, 19 3-34-1 Nishiikebukuro, Toshima-ku, Tokyo 171-8501, Japan. 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.01.28.428740; this version posted January 29, 2021. 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 4.0 International license. -
The Mysterious Orphans of Mycoplasmataceae
The mysterious orphans of Mycoplasmataceae Tatiana V. Tatarinova1,2*, Inna Lysnyansky3, Yuri V. Nikolsky4,5,6, and Alexander Bolshoy7* 1 Children’s Hospital Los Angeles, Keck School of Medicine, University of Southern California, Los Angeles, 90027, California, USA 2 Spatial Science Institute, University of Southern California, Los Angeles, 90089, California, USA 3 Mycoplasma Unit, Division of Avian and Aquatic Diseases, Kimron Veterinary Institute, POB 12, Beit Dagan, 50250, Israel 4 School of Systems Biology, George Mason University, 10900 University Blvd, MSN 5B3, Manassas, VA 20110, USA 5 Biomedical Cluster, Skolkovo Foundation, 4 Lugovaya str., Skolkovo Innovation Centre, Mozhajskij region, Moscow, 143026, Russian Federation 6 Vavilov Institute of General Genetics, Moscow, Russian Federation 7 Department of Evolutionary and Environmental Biology and Institute of Evolution, University of Haifa, Israel 1,2 [email protected] 3 [email protected] 4-6 [email protected] 7 [email protected] 1 Abstract Background: The length of a protein sequence is largely determined by its function, i.e. each functional group is associated with an optimal size. However, comparative genomics revealed that proteins’ length may be affected by additional factors. In 2002 it was shown that in bacterium Escherichia coli and the archaeon Archaeoglobus fulgidus, protein sequences with no homologs are, on average, shorter than those with homologs [1]. Most experts now agree that the length distributions are distinctly different between protein sequences with and without homologs in bacterial and archaeal genomes. In this study, we examine this postulate by a comprehensive analysis of all annotated prokaryotic genomes and focusing on certain exceptions. -
Role of Protein Phosphorylation in Mycoplasma Pneumoniae
Pathogenicity of a minimal organism: Role of protein phosphorylation in Mycoplasma pneumoniae Dissertation zur Erlangung des mathematisch-naturwissenschaftlichen Doktorgrades „Doctor rerum naturalium“ der Georg-August-Universität Göttingen vorgelegt von Sebastian Schmidl aus Bad Hersfeld Göttingen 2010 Mitglieder des Betreuungsausschusses: Referent: Prof. Dr. Jörg Stülke Koreferent: PD Dr. Michael Hoppert Tag der mündlichen Prüfung: 02.11.2010 “Everything should be made as simple as possible, but not simpler.” (Albert Einstein) Danksagung Zunächst möchte ich mich bei Prof. Dr. Jörg Stülke für die Ermöglichung dieser Doktorarbeit bedanken. Nicht zuletzt durch seine freundliche und engagierte Betreuung hat mir die Zeit viel Freude bereitet. Des Weiteren hat er mir alle Freiheiten zur Verwirklichung meiner eigenen Ideen gelassen, was ich sehr zu schätzen weiß. Für die Übernahme des Korreferates danke ich PD Dr. Michael Hoppert sowie Prof. Dr. Heinz Neumann, PD Dr. Boris Görke, PD Dr. Rolf Daniel und Prof. Dr. Botho Bowien für das Mitwirken im Thesis-Komitee. Der Studienstiftung des deutschen Volkes gilt ein besonderer Dank für die finanzielle Unterstützung dieser Arbeit, durch die es mir unter anderem auch möglich war, an Tagungen in fernen Ländern teilzunehmen. Prof. Dr. Michael Hecker und der Gruppe von Dr. Dörte Becher (Universität Greifswald) danke ich für die freundliche Zusammenarbeit bei der Durchführung von zahlreichen Proteomics-Experimenten. Ein ganz besonderer Dank geht dabei an Katrin Gronau, die mich in die Feinheiten der 2D-Gelelektrophorese eingeführt hat. Außerdem möchte ich mich bei Andreas Otto für die zahlreichen Proteinidentifikationen in den letzten Monaten bedanken. Nicht zu vergessen ist auch meine zweite Außenstelle an der Universität in Barcelona. Dr. Maria Lluch-Senar und Dr. -
Mycoplasma Agalactiae MEMBRANE PROTEOME
UNIVERSITÀ DEGLI STUDI DI SASSARI SCUOLA DI DOTTORATO IN SCIENZE BIOMOLECOLARI E BIOTECNOLOGICHE INDIRIZZO MICROBIOLOGIA MOLECOLARE E CLINICA XXIII Ciclo CHARACTERIZATION OF Mycoplasma agalactiae MEMBRANE PROTEOME Direttore: Prof. Bruno Masala Tutor: Dr. Alberto Alberti Tesi di dottorato della Dott.ssa Carla Cacciotto ANNO ACCADEMICO 2009-2010 TABLE OF CONTENTS 1. Abstract 2. Introduction 2.1 Mycoplasmas: taxonomy and main biological features 2.2 Metabolism 2.3 In vitro cultivation 2.4 Mycoplasma lipoproteins 2.5 Invasivity and pathogenicity 2.6 Diagnosis of mycoplasmosis 2.7 Mycoplasma agalactiae and Contagious Agalactia 3. Research objectives 4. Materials and methods 4.1 Media and buffers 4.2 Bacterial strains and culture conditions 4.3 Total DNA extraction and PCR 4.4 Total proteins extraction 4.5 Triton X-114 fractionation 4.6 SDS-PAGE 4.7 Western immunoblotting 4.8 2-D PAGE 4.9 2D DIGE 4.10 Spot picking and in situ tryptic digestion 4.11 GeLC-MS/MS 4.12 MALDI-MS 4.13 LC-MS/MS 4.14 Data analysis Dott.ssa Carla Cacciotto, Characterization of Mycoplasma agalactiae membrane proteome. Tesi di Dottorato in Scienze Biomolecolari e Biotecnologiche, Università degli Studi di Sassari. 5. Results 5.1 Species identification 5.2 Extraction of bacterial proteins and isolation of liposoluble proteins 5.3 2-D PAGE/MS of M. agalactiae PG2T liposoluble proteins 5.4 2D DIGE of liposoluble proteins among the type strain and two field isolates of M. agalactiae 5.5 GeLC-MS/MS of M. agalactiae PG2T liposoluble proteins 5.6 Data analysis and classification 6. Discussion 7. -
MIAMI UNIVERSITY the Graduate School
MIAMI UNIVERSITY The Graduate School Certificate for Approving the Dissertation We hereby approve the Dissertation of Steven Lindau Distelhorst Candidate for the Degree Doctor of Philosophy ______________________________________ Dr. Mitchell F. Balish, Director ______________________________________ Kelly Z. Abshire, Reader ______________________________________ Natosha L. Finley, Reader ______________________________________ Joseph M. Carlin, Reader ______________________________________ Jack C. Vaughn, Graduate School Representative ABSTRACT UNDERSTANDING VIRULENCE FACTORS OF MYCOPLASMA PENETRANS: ATTACHMENT ORGANELLE ORGANIZATION AND GENE EXPRESSION by Steven Lindau Distelhorst The ability to establish and maintain cell polarity plays an important role in cellular organization for both functional and morphological integrity in eukaryotic and prokaryotic organisms. Like eukaryotes, bacteria, including the genomically reduced species of the Mycoplasma genus, use an array of cytoskeletal proteins to generate and maintain cellular polarity. Some mycoplasmas, such as Mycoplasma penetrans, exhibit a distinct polarized structure, known as the attachment organelle (AO), which is used for attachment to host cells and motility. The M. penetrans AO, like AOs of other mycoplasmas, contains a cytoskeletal structure at the core, but lacks any homologs of identified AO core proteins of other investigated mycoplasmas. To characterize the composition of the M. penetrans AO cytoskeleton we purified the detergent-insoluble core material and examined -
Genes Involved in Cell Division in Mycoplasmas
Genetics and Molecular Biology, 30, 1, 174-181 (2007) Copyright by the Brazilian Society of Genetics. Printed in Brazil www.sbg.org.br Research Article Genes involved in cell division in mycoplasmas Frank Alarcón1, Ana Tereza Ribeiro de Vasconcelos1, Lucia Yim2 and Arnaldo Zaha3 1Laboratório Nacional de Computação Científica / Ministério da Ciência e Tecnologia, Petrópolis, RJ, Brazil. 2Instituto de Biologia Molecular do Paraná, Curitiba, PR, Brazil. 3Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil. Abstract Bacterial cell division has been studied mainly in model systems such as Escherichia coli and Bacillus subtilis, where it is described as a complex process with the participation of a group of proteins which assemble into a multiprotein complex called the septal ring. Mycoplasmas are cell wall-less bacteria presenting a reduced genome. Thus, it was important to compare their genomes to analyze putative genes involved in cell division processes. The division and cell wall (dcw) cluster, which in E. coli and B. subtilis is composed of 16 and 17 genes, respectively, is represented by only three to four genes in mycoplasmas. Even the most conserved protein, FtsZ, is not present in all mycoplasma genomes analyzed so far. A model for the FtsZ protein from Mycoplasma hyopneumoniae and Mycoplasma synoviae has been constructed. The conserved residues, essential for GTP/GDP binding, are present in FtsZ from both species. A strong conservation of hydrophobic amino acid patterns is observed, and is probably necessary for the structural stability of the protein when active. M. synoviae FtsZ presents an extended amino acid sequence at the C-terminal portion of the protein, which may participate in interactions with other still unknown proteins crucial for the cell division process. -
Mycoplasma Pneumoniae Terminal Organelle
MYCOPLASMA PNEUMONIAE TERMINAL ORGANELLE DEVELOPMENT AND GLIDING MOTILITY by BENJAMIN MICHAEL HASSELBRING (Under the Direction of Duncan Charles Krause) ABSTRACT With a minimal genome containing less than 700 open reading frames and a cell volume < 10% of that of model prokaryotes, Mycoplasma pneumoniae is considered among the smallest and simplest organisms capable of self-replication. And yet, this unique wall-less bacterium exhibits a remarkable level of cellular complexity with a dynamic cytoskeleton and a morphological asymmetry highlighted by a polar, membrane-bound terminal organelle containing an elaborate macromolecular core. The M. pneumoniae terminal organelle functions in distinct, and seemingly disparate cellular processes that include cytadherence, cell division, and presumably gliding motility, as individual cells translocate over surfaces with the cell pole harboring the structure engaged as the leading end. While recent years have witnessed a dramatic increase in the knowledge of protein interactions required for core stability and adhesin trafficking, the mechanism of M. pneumoniae gliding has not been defined nor have interdependencies between the various terminal organelle functions been assessed. The studies presented in the current volume describe the first genetic and molecular investigations into the location, components, architecture, and regulation of the M. pneumoniae gliding machinery. The data indicate that cytadherence and gliding motility are separable properties, and identify a subset of M. pneumoniae proteins contributing directly to the latter process. Characterizations of novel gliding-deficient mutants confirm that the terminal organelle contains the molecular gliding machinery, revealing that with the loss of a single terminal organelle cytoskeletal element, protein P41, terminal organelles detach from the cell body but retain gliding function. -
Structure of Mycoplasma Mobile
Cytoskeletal ‘‘jellyfish’’ structure of Mycoplasma mobile Daisuke Nakane* and Makoto Miyata*†‡ *Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan; and †PRESTO, Japan Science and Technology Agency, Sumiyoshi-ku, Osaka 558-8585, Japan Edited by David J. DeRosier, Brandeis University, Waltham, MA, and approved October 16, 2007 (received for review May 8, 2007) Mycoplasma mobile, a parasitic bacterium lacking a peptidoglycan This scenario leads to a crucial question: What physical layer, glides on solid surfaces in the direction of a membrane structure could support a gliding force as strong as 27 pN at protrusion at a cell pole by a unique mechanism. Recently, we maximum, while maintaining the flask cell shape? As in the case proposed a working model in which cells are propelled by leg of other mycoplasmas, M. mobile does not have a bacterial cell proteins clustering at the protrusion’s base. The legs repeatedly wall—i.e., a peptidoglycan layer. Moreover, the genome does not catch and release sialic acids on the solid surface, a motion that is have bacterial cytoskeletal proteins, such as MreB or FtsZ (28, driven by the force generated by ATP hydrolysis. Here, to clarify the 29). M. pneumonia, which is positioned at some distance from M. subcellular structure supporting the gliding force and the cell mobile on the phylogenetic tree in mycoplasmas, also can glide shape, we stripped the membrane by Triton X-100 and identified by its membrane protrusion (3, 4, 10, 30, 46). This species has a a unique structure, designated the ‘‘jellyfish’’ structure. In this cytoskeletal structure in the membrane protrusion, and some of structure, an oval solid ‘‘bell’’ Ϸ235 wide and 155 nm long is filled its protein components have been identified (2–5, 31, 32, 46). -
Identification and Characterization of Mycoplasma Promoters Kevin Lee Knudtson Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1993 Identification and characterization of mycoplasma promoters Kevin Lee Knudtson Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Microbiology Commons, and the Molecular Biology Commons Recommended Citation Knudtson, Kevin Lee, "Identification and characterization of mycoplasma promoters " (1993). Retrospective Theses and Dissertations. 10575. https://lib.dr.iastate.edu/rtd/10575 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. U-M-I MICROFILMED 1994 I INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. -
( 12 ) United States Patent
US009956282B2 (12 ) United States Patent ( 10 ) Patent No. : US 9 ,956 , 282 B2 Cook et al. (45 ) Date of Patent: May 1 , 2018 ( 54 ) BACTERIAL COMPOSITIONS AND (58 ) Field of Classification Search METHODS OF USE THEREOF FOR None TREATMENT OF IMMUNE SYSTEM See application file for complete search history . DISORDERS ( 56 ) References Cited (71 ) Applicant : Seres Therapeutics , Inc. , Cambridge , U . S . PATENT DOCUMENTS MA (US ) 3 ,009 , 864 A 11 / 1961 Gordon - Aldterton et al . 3 , 228 , 838 A 1 / 1966 Rinfret (72 ) Inventors : David N . Cook , Brooklyn , NY (US ) ; 3 ,608 ,030 A 11/ 1971 Grant David Arthur Berry , Brookline, MA 4 ,077 , 227 A 3 / 1978 Larson 4 ,205 , 132 A 5 / 1980 Sandine (US ) ; Geoffrey von Maltzahn , Boston , 4 ,655 , 047 A 4 / 1987 Temple MA (US ) ; Matthew R . Henn , 4 ,689 ,226 A 8 / 1987 Nurmi Somerville , MA (US ) ; Han Zhang , 4 ,839 , 281 A 6 / 1989 Gorbach et al. Oakton , VA (US ); Brian Goodman , 5 , 196 , 205 A 3 / 1993 Borody 5 , 425 , 951 A 6 / 1995 Goodrich Boston , MA (US ) 5 ,436 , 002 A 7 / 1995 Payne 5 ,443 , 826 A 8 / 1995 Borody ( 73 ) Assignee : Seres Therapeutics , Inc. , Cambridge , 5 ,599 ,795 A 2 / 1997 McCann 5 . 648 , 206 A 7 / 1997 Goodrich MA (US ) 5 , 951 , 977 A 9 / 1999 Nisbet et al. 5 , 965 , 128 A 10 / 1999 Doyle et al. ( * ) Notice : Subject to any disclaimer , the term of this 6 ,589 , 771 B1 7 /2003 Marshall patent is extended or adjusted under 35 6 , 645 , 530 B1 . 11 /2003 Borody U . -
A Phylogenetic Analysis of the Mycoplasmas: Basis for Their Lc Assification W
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by DigitalCommons@University of Nebraska University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Public Health Resources Public Health Resources 9-1989 A Phylogenetic Analysis of the Mycoplasmas: Basis for Their lC assification W. G. Weisburg University of Illinois J. G. Tully National Institute of Allergy and Infectious Diseases D. L. Rose National Institute of Allergy and Infectious Diseases J. P. Petzel Iowa State University H. Oyaizu University of Illinois See next page for additional authors Follow this and additional works at: https://digitalcommons.unl.edu/publichealthresources Weisburg, W. G.; Tully, J. G.; Rose, D. L.; Petzel, J. P.; Oyaizu, H.; Yang, D.; Mandelco, L.; Sechrest, J.; Lawrence, T. G.; Van Etten, James L.; Maniloff, J.; and Woese, C. R., "A Phylogenetic Analysis of the Mycoplasmas: Basis for Their lC assification" (1989). Public Health Resources. 310. https://digitalcommons.unl.edu/publichealthresources/310 This Article is brought to you for free and open access by the Public Health Resources at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Public Health Resources by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Authors W. G. Weisburg, J. G. Tully, D. L. Rose, J. P. Petzel, H. Oyaizu, D. Yang, L. Mandelco, J. Sechrest, T. G. Lawrence, James L. Van Etten, J. Maniloff, and C. R. Woese This article is available at DigitalCommons@University of Nebraska - Lincoln: https://digitalcommons.unl.edu/ publichealthresources/310 JOURNAL OF BACTERIOLOGY, Dec. 1989, p. 6455-6467 Vol. 171, No.