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1. Full Text Outer membrane vesicles mediate transport of biologically active Vibrio cholerae cytolysin (VCC) from V. cholerae strains
by Elluri, Sridhar and Enow, Constance and Vdovikova, Svitlana and Rompikuntal, Pramod K and Dongre, Mitesh and Carlsson, Sven and Pal, Amit and Uhlin, Bernt Eric and Wai, Sun Nyunt and Medicinska fakulteten and Institutionen för medicinsk kemi och biofysik and Institutionen för molekylärbiologi (Medicinska fakulteten) and Molekylär Infektionsmedicin, Sverige (MIMS) and Umeå universitet
PLoS ONE, ISSN 1932-6203, 09/2014, Volume 9, Issue 9, pp. e106731 - e106731
Background: Outer membrane vesicles (OMVs) released from Gram-negative bacteria can serve as vehicles for the translocation of virulence factors. Vibrio... 
ACTINOBACILLUS-ACTINOMYCETEMCOMITANS | BIOTYPE EL-TOR | VIRULENCE FACTORS | CYTOLETHAL DISTENDING TOXIN | PORE-FORMING TOXIN | MULTIDISCIPLINARY SCIENCES | STRUCTURAL GENE HLYA | ENTEROTOXIGENIC ESCHERICHIA-COLI | CELL VACUOLATION | NUCLEOTIDE-SEQUENCE | MOLECULAR ANALYSIS | Extracellular Vesicles - chemistry | Pore Forming Cytotoxic Proteins - biosynthesis | Humans | Vibrio cholerae - pathogenicity | Recombinant Proteins - biosynthesis | Vibrio cholerae - chemistry | Cytotoxins - toxicity | Pore Forming Cytotoxic Proteins - toxicity | Recombinant Proteins - isolation & purification | Bacterial Proteins - toxicity | Cytotoxins - biosynthesis | Escherichia coli - metabolism | HEK293 Cells | Erythrocytes - cytology | Virulence Factors - toxicity | Rabbits | Gene Expression | Virulence Factors - isolation & purification | Cytotoxins - isolation & purification | Vibrio cholerae - metabolism | Erythrocytes - drug effects | Animals | Pore Forming Cytotoxic Proteins - isolation & purification | Escherichia coli - genetics | Recombinant Proteins - toxicity | Bacterial Proteins - biosynthesis | HeLa Cells | Bacterial Proteins - isolation & purification | Virulence Factors - biosynthesis | Bacteria | Hostages | Cholera toxin | Virulence (Microbiology) | Analysis | Cells | Water-borne diseases | Epidemics | Laboratories | Toxicity | Pathogenesis | Epithelial cells | Virulence | Centrifugation | Erythrocytes | Cytotoxicity | Confocal microscopy | Infections | Biochemistry | Confocal | Autophagy | Mammalian cells | Proteins | Vesicles | Red blood cells | E coli | Virulence factors | Ultrastructure | Toxicity testing | Gram-negative bacteria | Ultrasonic testing | Strains (organisms) | Translocation | Pathogens | Secretion | Blood cells | Cloning | Membrane vesicles | Forming | Biological activity | Bacteriology | Medicine | Studies | Signaling | Microscopy | Plasmids | Cholera | Toxins | Mutation | Molecular biology | Phagocytosis | Pore formation | Vibrio | Index Medicus | Medical Biotechnology | Medical and Health Sciences | Medicin och hälsovetenskap | Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) | Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi), molekylärbiologi, mikrobiologi, biokemi eller biofarmaci) | Medicinsk bioteknologi
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2. Full Text Crystal structure of a concentrative nucleoside transporter from Vibrio cholerae at 2.4 Å
by Johnson, Zachary Lee and Cheong, Cheom-Gil and Lee, Seok-Yong
Nature, ISSN 0028-0836, 03/2012, Volume 483, Issue 7390, pp. 489 - 493
Nucleosides are required for DNA and RNA synthesis, and the nucleoside adenosine has a function in a variety of signalling processes. Transport of nucleosides... 
Humans | Models, Molecular | Crystallography, X-Ray | Nucleoside Transport Proteins - metabolism | Sodium - metabolism | Vibrio cholerae - chemistry | Protein Folding | Biological Transport | Nucleoside Transport Proteins - chemistry | Nucleosides - metabolism | Protein Conformation | Uridine - metabolism | Binding Sites | Uridine - chemistry | Index Medicus
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3. Full Text Sulfonamide inhibition studies of the β-carbonic anhydrase from the pathogenic bacterium Vibrio cholerae
by Del Prete, Sonia and Vullo, Daniela and De Luca, Viviana and Carginale, Vincenzo and Ferraroni, Marta and Osman, Sameh M and AlOthman, Zeid and Supuran, Claudiu T and Capasso, Clemente
Bioorganic & Medicinal Chemistry, ISSN 0968-0896, 03/2016, Volume 24, Issue 5, pp. 1115 - 1120
The genome of the pathogenic bacterium encodes for three carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β- and γ-classes. VchCA, the α-CA from this... 
Inhibitors | Sulfonamide | Carbonic anhydrase | Metalloenzymes | Pathogenic bacteria | Hydratase activity | CHEMISTRY, MEDICINAL | CRYSTAL-STRUCTURE | PORPHYROMONAS-GINGIVALIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CHEMISTRY, ORGANIC | DRUG TARGETS | THERAPEUTIC APPLICATIONS | PH-DEPENDENT ACTIVITY | PLASMODIUM-FALCIPARUM | SELECTIVE INHIBITORS | ISOZYME-II | BIOCHEMICAL-PROPERTIES | Amino Acid Sequence | Sulfonamides - chemistry | Carbonic Anhydrase Inhibitors - chemistry | Humans | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Carbonic Anhydrase Inhibitors - pharmacology | Vibrio cholerae - chemistry | Carbonic Anhydrases - chemistry | Sulfonamides - pharmacology | Carbonic Anhydrases - metabolism | Vibrio cholerae - enzymology | Cholera - drug therapy | Base Sequence | Vibrio cholerae - drug effects | Cholera - microbiology | Index Medicus
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4. Full Text Type VI secretion requires a dynamic contractile phage tail-like structure
by Basler, M and Pilhofer, M and Henderson, G.P and Jensen, G.J and Mekalanos, J.J
Nature, ISSN 0028-0836, 03/2012, Volume 483, Issue 7388, pp. 182 - 186
Type VI secretion systems are bacterial virulence-associated nanomachines composed of proteins that are evolutionarily related to components of bacteriophage... 
SYSTEM | TOMOGRAPHY | BACTERIA | ALIGNMENT | ACTIN | PSEUDOMONAS-AERUGINOSA | TARGET-CELLS | MULTIDISCIPLINARY SCIENCES | PROTEIN SECRETION | APPARATUS | ENTEROAGGREGATIVE ESCHERICHIA-COLI | Bacteriophages - chemistry | Electron Microscope Tomography | Bacterial Proteins - chemistry | Vibrio cholerae - chemistry | Vibrio cholerae - cytology | Bacterial Secretion Systems - physiology | Vibrio cholerae - metabolism | Cryoelectron Microscopy | Vibrio cholerae - ultrastructure | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Cell Membrane - metabolism | Bacteriophages - physiology | Microscopy, Fluorescence | Bacteriophages | Contractility (Biology) | Research | Secretion | Proteins | Bacteria | Index Medicus
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5. Full Text Subunit-subunit interactions play a key role in the heme-degradation reaction of HutZ from: Vibrio cholerae
by Uchida, Takeshi and Ota, Kazuki and Sekine, Yukari and Dojun, Nobuhiko and Ishimori, Koichiro
Dalton Transactions, ISSN 1477-9226, 2019, Volume 48, Issue 12, pp. 3973 - 3983
HutZ, a dimeric protein, from Vibrio cholerae is a protein that catalyzes the oxygen-dependent degradation of heme. Interestingly, the ascorbic acid-supported... 
CORYNEBACTERIUM-DIPHTHERIAE | DEGRADING ENZYMES | GRAM-NEGATIVE BACTERIA | PROXIMAL LIGAND | OXYGENASE COMPLEX | HMU O | CRYSTAL-STRUCTURE | CYTOCHROME-C PEROXIDASE | STAPHYLOCOCCUS-AUREUS ISDG | RESONANCE RAMAN | CHEMISTRY, INORGANIC & NUCLEAR | Heme - metabolism | Heme - chemistry | Oxidation-Reduction | Bacterial Proteins - chemistry | Models, Molecular | Spectrometry, Fluorescence | Bacterial Proteins - metabolism | Molecular Structure | Vibrio cholerae - chemistry | Bacterial Proteins - isolation & purification | Vibrio cholerae - metabolism | Hydrogen-Ion Concentration
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6. Full Text Structure of the Type VI Secretion System Contractile Sheath
by Kudryashev, Mikhail and Wang, Ray Yu-Ruei and Brackmann, Maximilian and Scherer, Sebastian and Maier, Timm and Baker, David and DiMaio, Frank and Stahlberg, Henning and Egelman, Edward H and Basler, Marek
Cell, ISSN 0092-8674, 02/2015, Volume 160, Issue 5, pp. 952 - 962
Bacteria use rapid contraction of a long sheath of the type VI secretion system (T6SS) to deliver effectors into a target cell. Here, we present an... 
HELICAL FILAMENTS | COMPLEX | MECHANISM | NEAR-ATOMIC-RESOLUTION | PSEUDOMONAS-AERUGINOSA | BACTERIOPHAGE-T4 | RECONSTRUCTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTEIN SECRETION | ELECTRON-MICROSCOPY | CRYO-EM | CELL BIOLOGY | Cryoelectron Microscopy | Amino Acid Sequence | Sequence Alignment | Bacterial Secretion Systems | Vibrio cholerae - ultrastructure | Bacterial Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Vibrio cholerae - chemistry | Vibrio cholerae - cytology | Vibrio cholerae - metabolism | Proteins | Bacteria | Cholera toxin | Electron microscopy | Adenosine triphosphatase | Resveratrol | Index Medicus
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7. Full Text Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a beta-strand sliding mechanism
by Hadzi, S and Garcia-Pino, A and Haesaerts, S and Jurenas, D and Gerdes, K and Lah, J and Loris, R
NUCLEIC ACIDS RESEARCH, ISSN 0305-1048, 05/2017, Volume 45, Issue 8, pp. 4972 - 4983
Toxin-antitoxin (TA) modules are small operons involved in bacterial stress response and persistence. higBA operons form a family of TA modules with an... 
TOXIN-ANTITOXIN COMPLEX | PROTEIN | STRUCTURAL BASIS | MESSENGER-RNA RECOGNITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | X-RAY-SCATTERING | LOCI | RELE | DINJ-YAFQ | CLEAVAGE | Catalytic Domain | Ribonucleases - genetics | Ribonucleases - chemistry | Escherichia coli | Protein Multimerization | RNA, Messenger - genetics | Bacterial Proteins - genetics | Ribosomes - chemistry | Crystallography, X-Ray | Multiprotein Complexes - genetics | Vibrio cholerae - chemistry | Antitoxins - chemistry | Bacterial Toxins - chemistry | Multiprotein Complexes - chemistry | Vibrio cholerae - enzymology | Protein Conformation, beta-Strand | Ribosomes - genetics | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Toxins - genetics | RNA, Messenger - chemistry | DNA Topoisomerase IV - genetics | Antitoxins - genetics | Index Medicus | Structural Biology
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8. Full Text Spermine inhibits Vibrio cholerae biofilm formation through the NspS–MbaA polyamine signaling system
by Sobe, Richard C and Bond, Whitney G and Wotanis, Caitlin K and Zayner, Josiah P and Burriss, Marybeth A and Fernandez, Nicolas and Bruger, Eric L and Waters, Christopher M and Neufeld, Howard S and Karatan, Ece
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 41, pp. 17025 - 17036
The aquatic bacterium and human intestinal pathogen, Vibrio cholerae, senses and responds to a variety of environment-specific cues to regulate biofilm... 
cyclic di-GMP (c-di-GMP) | MANNOSE-SENSITIVE HEMAGGLUTININ | SOLUTE-BINDING-PROTEINS | Vibrio cholerae | BIOCHEMISTRY & MOLECULAR BIOLOGY | RUGOSE COLONY MORPHOLOGY | COLONIZATION | IDENTIFICATION | polyamine | EL-TOR | biofilm | bacterial signal transduction | NORSPERMIDINE | CHITIN | CYCLIC DI-GMP | MOTILITY | Biofilms - drug effects | Periplasmic Proteins - chemistry | Phosphoric Diester Hydrolases - metabolism | Humans | Intestines - metabolism | Vibrio cholerae - chemistry | Phosphoric Diester Hydrolases - chemistry | Intestines - microbiology | Cyclic GMP - analogs & derivatives | Cyclic GMP - metabolism | Signal Transduction - drug effects | Spermine - pharmacology | Models, Biological | Vibrio cholerae - physiology | Periplasmic Proteins - metabolism | Index Medicus | Microbiology
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9. Full Text Crystal structure and kinetic studies of a tetrameric type II β‐carbonic anhydrase from the pathogenic bacterium Vibrio cholerae
by Ferraroni, Marta and Del Prete, Sonia and Vullo, Daniela and Capasso, Clemente and Supuran, Claudiu T
Acta Crystallographica Section D, ISSN 1399-0047, 12/2015, Volume 71, Issue 12, pp. 2449 - 2456
Carbonic anhydrase (CA) is a zinc enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate (hydrogen carbonate) and a proton. CAs have... 
carbonic anhydrase | crystal structure | type II CA | β‐carbonic anhydrase | Vibrio cholerae | β-carbonic anhydrase | Carbonic anhydrase | Type II CA | Crystal structure | MYCOBACTERIUM-TUBERCULOSIS | beta-carbonic anhydrase | ACTIVE-SITE | PORPHYROMONAS-GINGIVALIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | BIOCHEMICAL-CHARACTERIZATION | ALPHA | CRYSTALLOGRAPHY | HYDRATION | REFINEMENT | EVOLUTION | BIOPHYSICS | PH-DEPENDENT ACTIVITY | INHIBITORS | Protons | Carbon Dioxide - chemistry | Zinc - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Acetazolamide | Carbonic Anhydrase II - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Vibrio cholerae - chemistry | Zinc - chemistry | Protein Subunits - metabolism | Carbonic Anhydrase Inhibitors | Vibrio cholerae - enzymology | Escherichia coli - metabolism | Bicarbonates - chemistry | Carbonic Anhydrase II - genetics | Protein Subunits - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Gene Expression | Carbon Dioxide - metabolism | Protein Structure, Secondary | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Sequence Alignment | Escherichia coli - genetics | Bicarbonates - metabolism | Protein Binding | Bacterial Proteins - metabolism | Protein Subunits - chemistry | Kinetics | Carbonic Anhydrase II - chemistry | Index Medicus | Enzymes | Inhibitors | Carbon dioxide | Bicarbonates | Bacteria | Zinc | Vibrio
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10. Full Text Functional mapping of the lectin activity site on theβ-Prism Domain of Vibrio cholerae Cytolysin: Implications for the membrane pore-formation mechanism of the toxin
by Rai, Anand Kumar and Paul, Karan and Chattopadhyay, Kausik
Journal of Biological Chemistry, ISSN 0021-9258, 01/2013, Volume 288, Issue 3, pp. 1665 - 1673
Vibrio cholerae cytolysin (VCC) is a prominent member in the family of beta-barrel pore-forming toxins. It induces lysis of target eukaryotic cells by forming... 
BIOTYPE EL-TOR | COMPLEX | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEPTAMERIC TRANSMEMBRANE PORE | FORMING TOXINS | MODE | PURIFICATION | HEMOLYSIN | BINDING | Perforin - genetics | Glycoconjugates - chemistry | Escherichia coli | Humans | Bacterial Proteins - chemistry | Structure-Activity Relationship | Erythrocytes - chemistry | Vibrio cholerae - chemistry | Lectins - metabolism | Cytotoxins - metabolism | Lectins - chemistry | Circular Dichroism | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Perforin - chemistry | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Erythrocytes - microbiology | Cytotoxins - chemistry | Vibrio cholerae - physiology | Bacterial Proteins - metabolism | Calorimetry | Lectins - genetics | Perforin - metabolism | Kinetics | Mutation | Cytotoxins - genetics | Index Medicus | Protein Structure and Folding | Carbohydrate-binding Protein | Lectin | Protein Self-assembly | Pore-forming Protein Toxin | Bacterial Toxins | Protein Domains | Protein Structure | Vibrio cholerae Cytolysin
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11. Full Text Amino acid addition to Vibrio cholerae LPS establishes a link between surface remodeling in Gram-positive and Gram-negative bacteria
by Jessica V. Hankins and James A. Madsen and David K. Giles and Jennifer S. Brodbelt and M. Stephen Trent
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2012, Volume 109, Issue 22, pp. 8722 - 8727
Historically, the O1 El Tor and classical biotypes of Vibrio cholerae have been differentiated by their resistance to the antimicrobial peptide polymyxin B.... 
Cell wall components | Carrier proteins | Antimicrobials | Gram positive bacteria | Cell walls | Vibrio cholerae | Lipids | Amino acids | Teichoic acids | Polymyxins | Ultraviolet photodissociation | Endotoxin | Cell envelope | Outer membrane | outer membrane | 4-AMINO-4-DEOXY-L-ARABINOSE | LIPOTEICHOIC ACID | cell envelope | MULTIDISCIPLINARY SCIENCES | ALANYL CARRIER PROTEIN | ANTIMICROBIAL PEPTIDES | PHOSPHOETHANOLAMINE | PHOTODISSOCIATION | EL-TOR | SALMONELLA-TYPHIMURIUM | RESISTANCE | ultraviolet photodissociation | DIFFERENTIATION | endotoxin | Polymyxin B - pharmacology | Glycine - metabolism | Gram-Positive Bacteria - chemistry | Drug Resistance, Bacterial | Lipopolysaccharides - metabolism | Molecular Sequence Data | Gram-Negative Bacteria - metabolism | Vibrio cholerae - chemistry | Carbon-Nitrogen Ligases - genetics | Gram-Positive Bacteria - genetics | Glycine - chemistry | Base Sequence | Molecular Structure | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Gram-Negative Bacteria - genetics | Lipid A - chemistry | Amino Acid Sequence | Carbon-Nitrogen Ligases - metabolism | Lipid A - metabolism | Vibrio cholerae - genetics | Bacterial Proteins - genetics | Cell Wall - chemistry | Sequence Homology, Nucleic Acid | Vibrio cholerae - metabolism | Gram-Positive Bacteria - metabolism | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Carrier Proteins - metabolism | Gram-Negative Bacteria - chemistry | Cell Wall - metabolism | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Lipopolysaccharides - chemistry | Mutation | Genetic aspects | Cell membranes | Properties | Health aspects | Genotype & phenotype | Bacteria | Peptides | Index Medicus | Biological Sciences
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12. Full Text Crystal structure of the Vibrio cholerae ferric uptake regulator (Fur) reveals insights into metal co-ordination
by Sheikh, Md. Arif and Taylor, Garry L
Molecular Microbiology, ISSN 0950-382X, 06/2009, Volume 72, Issue 5, pp. 1208 - 1220
The ferric uptake regulator (Fur) is a metal-dependent DNA-binding protein that acts as both a repressor and an activator of numerous genes involved in... 
BACILLUS-SUBTILIS | PSEUDOMONAS-AERUGINOSA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | FUNCTIONAL DOMAINS | IRON ACQUISITION | MICROBIOLOGY | REPRESSOR | SITE-DIRECTED MUTAGENESIS | BINDING | UPTAKE REGULATION PROTEIN | MASS-SPECTROMETRY | Protein Structure, Tertiary | Metals - metabolism | Repressor Proteins - chemistry | Metalloproteins - chemistry | Vibrio cholerae - genetics | Bacterial Proteins - chemistry | Cloning, Molecular | Vibrio cholerae - chemistry | Binding Sites | Iron compounds | Analysis | Water quality | Crystals | Cholera toxin | Binding proteins | Structure | Monomers | Protein binding | Proteins | E coli | Metals | Cholera | Deoxyribonucleic acid--DNA | Binding sites | Crystal structure | Index Medicus
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13. Full Text Small Molecule-Induced Allosteric Activation of the Vibrio cholerae RTX Cysteine Protease Domain
by Patrick J. Lupardus and Aimee Shen and Matthew Bogyo and K. Christopher Garcia
Science, ISSN 0036-8075, 10/2008, Volume 322, Issue 5899, pp. 265 - 268
Vibrio cholerae RTX (repeats in toxin) is an actin-disrupting toxin that is autoprocessed by an internal cysteine protease domain (CPD). The RTX CPD is... 
Molecules | Enzymes | Active sites | Vibrio cholerae | Cephalopelvic disproportion | Actins | Amino acids | Reports | Toxins | Catalysis | Eukaryotic cells | DEPENDS | MICE | BACTERIAL | CLEAVAGE | CLOSTRIDIUM-DIFFICILE TOXIN | MULTIDISCIPLINARY SCIENCES | Cysteine Endopeptidases - chemistry | Surface Plasmon Resonance | Allosteric Regulation | Bacterial Proteins - chemistry | Crystallography, X-Ray | Vibrio cholerae - chemistry | Acyltransferases - metabolism | Acyltransferases - genetics | Cysteine Endopeptidases - metabolism | Phytic Acid - metabolism | Bacterial Toxins - genetics | Binding Sites | Catalytic Domain | Protein Structure, Secondary | Bacterial Proteins - genetics | Models, Molecular | Bacterial Toxins - chemistry | Point Mutation | Bacterial Toxins - metabolism | Guanosine 5'-O-(3-Thiotriphosphate) - metabolism | Hydrogen Bonding | Cysteine Endopeptidases - genetics | Bacterial Proteins - metabolism | Acyltransferases - chemistry | Enzyme Activation | Physiological aspects | Cysteine proteinases | Properties | Toxicology | Biochemistry | Mutation | Molecular biology | Proteases | Index Medicus
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