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  • 1
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    Coordinate regulation and sensory transduction in the control of bacterial virulence (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-17
    Description: Genes and operons that encode bacterial virulence factors are often subject to coordinate regulation. These regulatory systems are capable of responding to various environmental signals that may be encountered during the infectious cycle. For some pathogens, proteins that mediate sensory transduction and virulence control are similar to components of other bacterial information processing systems. Understanding the molecular mechanisms governing global regulation of pathogenicity is essential for understanding bacterial infectious diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, J F -- Mekalanos, J J -- Falkow, S -- AI23945/AI/NIAID NIH HHS/ -- AI26195/AI/NIAID NIH HHS/ -- AI26289/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):916-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2537530" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*pathogenicity ; Bacterial Infections/microbiology ; Bordetella pertussis/pathogenicity ; Humans ; Rhizobium/pathogenicity ; Vibrio cholerae/pathogenicity ; Virulence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    A virulence locus of Pseudomonas aeruginosa encodes a protein secretion apparatus (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-10
    Description: Bacterial pathogens frequently use protein secretion to mediate interactions with their hosts. Here we found that a virulence locus (HSI-I) of Pseudomonas aeruginosa encodes a protein secretion apparatus. The apparatus assembled in discrete subcellular locations and exported Hcp1, a hexameric protein that forms rings with a 40 angstrom internal diameter. Regulatory patterns of HSI-I suggested that the apparatus functions during chronic infections. We detected Hcp1 in pulmonary secretions of cystic fibrosis (CF) patients and Hcp1-specific antibodies in their sera. Thus, HSI-I likely contributes to the pathogenesis of P. aeruginosa in CF patients. HSI-I-related loci are widely distributed among bacterial pathogens and may play a general role in mediating host interactions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2800167/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2800167/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mougous, Joseph D -- Cuff, Marianne E -- Raunser, Stefan -- Shen, Aimee -- Zhou, Min -- Gifford, Casey A -- Goodman, Andrew L -- Joachimiak, Grazyna -- Ordonez, Claudia L -- Lory, Stephen -- Walz, Thomas -- Joachimiak, Andrzej -- Mekalanos, John J -- AI21451/AI/NIAID NIH HHS/ -- AI26289/AI/NIAID NIH HHS/ -- GM074942/GM/NIGMS NIH HHS/ -- GM62414/GM/NIGMS NIH HHS/ -- P50 GM062414/GM/NIGMS NIH HHS/ -- P50 GM062414-02/GM/NIGMS NIH HHS/ -- U54 GM074942/GM/NIGMS NIH HHS/ -- U54 GM074942-04S2/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 9;312(5779):1526-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763151" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*genetics/physiology/secretion ; Crystallography, X-Ray ; Cystic Fibrosis/complications/microbiology ; Humans ; Models, Molecular ; Protein Conformation ; Pseudomonas Infections/complications/microbiology ; Pseudomonas aeruginosa/*genetics/pathogenicity ; Rats ; Recombinant Fusion Proteins ; Sequence Alignment ; Virulence/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Type 6 secretion system-mediated immunity to type 4 secretion system-mediated gene transfer (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-10-12
    Description: Gram-negative bacteria use the type VI secretion system (T6SS) to translocate toxic effector proteins into adjacent cells. The Pseudomonas aeruginosa H1-locus T6SS assembles in response to exogenous T6SS attack by other bacteria. We found that this lethal T6SS counterattack also occurs in response to the mating pair formation (Mpf) system encoded by broad-host-range IncPalpha conjugative plasmid RP4 present in adjacent donor cells. This T6SS response was eliminated by disruption of Mpf structural genes but not components required only for DNA transfer. Because T6SS activity was also strongly induced by membrane-disrupting natural product polymyxin B, we conclude that RP4 induces "donor-directed T6SS attacks" at sites corresponding to Mpf-mediated membrane perturbations in recipient P. aeruginosa cells to potentially block acquisition of parasitic foreign DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034461/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034461/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ho, Brian T -- Basler, Marek -- Mekalanos, John J -- AI-018045/AI/NIAID NIH HHS/ -- AI-26289/AI/NIAID NIH HHS/ -- R01 AI018045/AI/NIAID NIH HHS/ -- R01 AI026289/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2013 Oct 11;342(6155):250-3. doi: 10.1126/science.1243745.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24115441" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibiosis ; Bacterial Secretion Systems/drug effects/*physiology ; *Conjugation, Genetic ; DNA, Bacterial/genetics ; Gene Transfer, Horizontal/drug effects/*physiology ; Plasmids/genetics ; Polymyxin B/pharmacology ; Pseudomonas aeruginosa/drug effects/*genetics/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    An open letter to Elias Zerhouni (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-03-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altman, Sidney -- Bassler, Bonnie L -- Beckwith, Jon -- Belfort, Marlene -- Berg, Howard C -- Bloom, Barry -- Brenchley, Jean E -- Campbell, Allan -- Collier, R John -- Connell, Nancy -- Cozzarelli, Nicholas R -- Craig, Nancy L -- Darst, Seth -- Ebright, Richard H -- Elledge, Stephen J -- Falkow, Stanley -- Galan, Jorge E -- Gottesman, Max -- Gourse, Richard -- Grindley, Nigel D F -- Gross, Carol A -- Grossman, Alan -- Hochschild, Ann -- Howe, Martha -- Hurwitz, Jerard -- Isberg, Ralph R -- Kaplan, Samuel -- Kornberg, Arthur -- Kustu, Sydney G -- Landick, Robert C -- Landy, Arthur -- Levy, Stuart B -- Losick, Richard -- Long, Sharon R -- Maloy, Stanley R -- Mekalanos, John J -- Neidhardt, Frederick C -- Pace, Norman R -- Ptashne, Mark -- Roberts, Jeffrey W -- Roth, John R -- Rothman-Denes, Lucia B -- Salyers, Abigail -- Schaechter, Moselio -- Shapiro, Lucy -- Silhavy, Thomas J -- Simon, Melvin I -- Walker, Graham -- Yanofsky, Charles -- Zinder, Norton -- New York, N.Y. -- Science. 2005 Mar 4;307(5714):1409-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15746409" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Warfare ; *Biomedical Research/economics ; *Bioterrorism ; Financing, Government ; *Microbiology ; *National Institutes of Health (U.S.) ; Peer Review, Research ; Public Health ; *Research Support as Topic ; United States
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Small-molecule inhibitor of Vibrio cholerae virulence and intestinal colonization (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-15
    Description: Increasing antibiotic resistance requires the development of new approaches to combating infection. Virulence gene expression in vivo represents a target for antibiotic discovery that has not yet been explored. A high-throughput, phenotypic screen was used to identify a small molecule 4-[N-(1,8-naphthalimide)]-n-butyric acid, virstatin, that inhibits virulence regulation in Vibrio cholerae. By inhibiting the transcriptional regulator ToxT, virstatin prevents expression of two critical V. cholerae virulence factors, cholera toxin and the toxin coregulated pilus. Orogastric administration of virstatin protects infant mice from intestinal colonization by V. cholerae.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hung, Deborah T -- Shakhnovich, Elizabeth A -- Pierson, Emily -- Mekalanos, John J -- AI26289/AI/NIAID NIH HHS/ -- K08 AI060708-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 28;310(5748):670-4. Epub 2005 Oct 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA. dhung@partners.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16223984" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Bacterial Agents/*pharmacology ; Bacterial Proteins/biosynthesis/drug effects ; Butyrates/*pharmacology ; Cell Line ; Cholera/microbiology ; Cholera Toxin/biosynthesis ; Fimbriae, Bacterial/drug effects ; Gene Expression Regulation, Bacterial/drug effects ; Intestine, Small/*microbiology ; Mice ; Microbial Sensitivity Tests ; Naphthalenes/*pharmacology ; Naphthalimides ; Transcription Factors/biosynthesis/drug effects ; Vibrio cholerae/*drug effects/pathogenicity ; Virulence/drug effects ; Virulence Factors/biosynthesis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    T6SS sheaths for antigen display [Microbiology] (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-03-16
    Description: The bacterial type 6 secretion system (T6SS) is a dynamic apparatus that translocates proteins between cells by a mechanism analogous to phage tail contraction. T6SS sheaths are cytoplasmic tubular structures composed of stable VipA-VipB (named for ClpV-interacting protein A and B) heterodimers. Here, the structure of the VipA/B sheath was...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
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    Satellite phage TLCphi enables toxigenic conversion by CTX phage through dif site alteration (2010)
    Nature Publishing Group (NPG)
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    Publication Date: 2010-10-15
    Description: Bacterial chromosomes often carry integrated genetic elements (for example plasmids, transposons, prophages and islands) whose precise function and contribution to the evolutionary fitness of the host bacterium are unknown. The CTXphi prophage, which encodes cholera toxin in Vibrio cholerae, is known to be adjacent to a chromosomally integrated element of unknown function termed the toxin-linked cryptic (TLC). Here we report the characterization of a TLC-related element that corresponds to the genome of a satellite filamentous phage (TLC-Knphi1), which uses the morphogenesis genes of another filamentous phage (fs2phi) to form infectious TLC-Knphi1 phage particles. The TLC-Knphi1 phage genome carries a sequence similar to the dif recombination sequence, which functions in chromosome dimer resolution using XerC and XerD recombinases. The dif sequence is also exploited by lysogenic filamentous phages (for example CTXphi) for chromosomal integration of their genomes. Bacterial cells defective in the dimer resolution often show an aberrant filamentous cell morphology. We found that acquisition and chromosomal integration of the TLC-Knphi1 genome restored a perfect dif site and normal morphology to V. cholerae wild-type and mutant strains with dif(-) filamentation phenotypes. Furthermore, lysogeny of a dif(-) non-toxigenic V. cholerae with TLC-Knphi1 promoted its subsequent toxigenic conversion through integration of CTXphi into the restored dif site. These results reveal a remarkable level of cooperative interactions between multiple filamentous phages in the emergence of the bacterial pathogen that causes cholera.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2967718/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2967718/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hassan, Faizule -- Kamruzzaman, M -- Mekalanos, John J -- Faruque, Shah M -- R01 AI070963/AI/NIAID NIH HHS/ -- R01 AI070963-02/AI/NIAID NIH HHS/ -- R01 AI070963-03/AI/NIAID NIH HHS/ -- R01 GM068851/GM/NIGMS NIH HHS/ -- R01 GM068851-06/GM/NIGMS NIH HHS/ -- R01 GM068851-07/GM/NIGMS NIH HHS/ -- R01-AI070963/AI/NIAID NIH HHS/ -- R01-GM068851/GM/NIGMS NIH HHS/ -- England -- Nature. 2010 Oct 21;467(7318):982-5. doi: 10.1038/nature09469. Epub 2010 Oct 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Genetics Laboratory, International Centre for Diarrhoeal Disease Research, Bangladesh, Dhaka-1212, Bangladesh.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20944629" target="_blank"〉PubMed〈/a〉
    Keywords: Attachment Sites, Microbiological/genetics ; Base Sequence ; Cholera/epidemiology/microbiology ; Cholera Toxin/genetics ; Evolution, Molecular ; Genes, Bacterial/genetics ; Genes, Viral/*genetics ; Genome, Bacterial/genetics ; Genome, Viral/genetics ; Helper Viruses/genetics/physiology ; Humans ; Inovirus/*genetics/pathogenicity/*physiology ; Lysogeny/genetics/physiology ; Molecular Sequence Data ; Phenotype ; Plasmids/genetics ; Prophages/genetics/physiology ; Recombination, Genetic/genetics ; Transduction, Genetic ; Vibrio cholerae/classification/*genetics/pathogenicity/*virology ; Virus Integration/*genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 8
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    PAAR-repeat proteins sharpen and diversify the type VI secretion system spike (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-08-09
    Description: The bacterial type VI secretion system (T6SS) is a large multicomponent, dynamic macromolecular machine that has an important role in the ecology of many Gram-negative bacteria. T6SS is responsible for translocation of a wide range of toxic effector molecules, allowing predatory cells to kill both prokaryotic as well as eukaryotic prey cells. The T6SS organelle is functionally analogous to contractile tails of bacteriophages and is thought to attack cells by initially penetrating them with a trimeric protein complex called the VgrG spike. Neither the exact protein composition of the T6SS organelle nor the mechanisms of effector selection and delivery are known. Here we report that proteins from the PAAR (proline-alanine-alanine-arginine) repeat superfamily form a sharp conical extension on the VgrG spike, which is further involved in attaching effector domains to the spike. The crystal structures of two PAAR-repeat proteins bound to VgrG-like partners show that these proteins sharpen the tip of the T6SS spike complex. We demonstrate that PAAR proteins are essential for T6SS-mediated secretion and target cell killing by Vibrio cholerae and Acinetobacter baylyi. Our results indicate a new model of the T6SS organelle in which the VgrG-PAAR spike complex is decorated with multiple effectors that are delivered simultaneously into target cells in a single contraction-driven translocation event.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3792578/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3792578/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shneider, Mikhail M -- Buth, Sergey A -- Ho, Brian T -- Basler, Marek -- Mekalanos, John J -- Leiman, Petr G -- AI-01845/AI/NIAID NIH HHS/ -- AI-026289/AI/NIAID NIH HHS/ -- R01 AI018045/AI/NIAID NIH HHS/ -- R01 AI026289/AI/NIAID NIH HHS/ -- England -- Nature. 2013 Aug 15;500(7462):350-3. doi: 10.1038/nature12453. Epub 2013 Aug 7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ecole Polytechnique Federale de Lausanne (EPFL), BSP-415, 1015 Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23925114" target="_blank"〉PubMed〈/a〉
    Keywords: Acinetobacter/genetics/metabolism ; Bacterial Proteins/*chemistry/*secretion ; Bacterial Secretion Systems/*genetics ; Microsatellite Repeats/*physiology ; Protein Binding ; Vibrio cholerae/genetics/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 9
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    Type VI secretion requires a dynamic contractile phage tail-like structure (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-03-01
    Description: Type VI secretion systems are bacterial virulence-associated nanomachines composed of proteins that are evolutionarily related to components of bacteriophage tails. Here we show that protein secretion by the type VI secretion system of Vibrio cholerae requires the action of a dynamic intracellular tubular structure that is structurally and functionally homologous to contractile phage tail sheath. Time-lapse fluorescence light microscopy reveals that sheaths of the type VI secretion system cycle between assembly, quick contraction, disassembly and re-assembly. Whole-cell electron cryotomography further shows that the sheaths appear as long tubular structures in either extended or contracted conformations that are connected to the inner membrane by a distinct basal structure. These data support a model in which the contraction of the type VI secretion system sheath provides the energy needed to translocate proteins out of effector cells and into adjacent target cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3527127/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3527127/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Basler, M -- Pilhofer, M -- Henderson, G P -- Jensen, G J -- Mekalanos, J J -- AI-018045/AI/NIAID NIH HHS/ -- AI-26289/AI/NIAID NIH HHS/ -- GM094800B/GM/NIGMS NIH HHS/ -- R01 AI018045/AI/NIAID NIH HHS/ -- R01 AI026289/AI/NIAID NIH HHS/ -- R37 AI018045/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Feb 26;483(7388):182-6. doi: 10.1038/nature10846.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunobiology, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22367545" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/metabolism/*ultrastructure ; Bacterial Secretion Systems/*physiology ; Bacteriophages/*chemistry/physiology ; Cell Membrane/metabolism ; Cryoelectron Microscopy ; Electron Microscope Tomography ; Microscopy, Fluorescence ; Vibrio cholerae/*chemistry/cytology/*metabolism/ultrastructure
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 10
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    Lysogenic conversion by a filamentous phage encoding cholera toxin (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-28
    Description: Vibrio cholerae, the causative agent of cholera, requires two coordinately regulated factors for full virulence: cholera toxin (CT), a potent enterotoxin, and toxin-coregulated pili (TCP), surface organelles required for intestinal colonization. The structural genes for CT are shown here to be encoded by a filamentous bacteriophage (designated CTXphi), which is related to coliphage M13. The CTXphi genome chromosomally integrated or replicated as a plasmid. CTXphi used TCP as its receptor and infected V. cholerae cells within the gastrointestinal tracts of mice more efficiently than under laboratory conditions. Thus, the emergence of toxigenic V. cholerae involves horizontal gene transfer that may depend on in vivo gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldor, M K -- Mekalanos, J J -- AI01321/AI/NIAID NIH HHS/ -- AI18045/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1910-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Shipley Institute of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658163" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages/*genetics/physiology ; Base Sequence ; Cholera/*microbiology ; Cholera Toxin/*genetics ; DNA Primers ; Digestive System/microbiology ; Fimbriae, Bacterial/physiology/virology ; Gene Expression ; Genes, Bacterial ; *Lysogeny ; Mice ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Transduction, Genetic ; Vibrio cholerae/genetics/*pathogenicity/*virology ; Virulence/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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