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  • 1
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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
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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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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  • 3
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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
    Published by Nature Publishing Group (NPG)
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  • 4
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    Type 6 secretion dynamics within and between bacterial cells (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-07-07
    Description: The bacterial type 6 secretion system (T6SS) functions as a virulence factor capable of attacking both eukaryotic and prokaryotic target cells by a process that involves protein transport through a contractile bacteriophage tail-like structure. The T6SS apparatus is composed, in part, of an exterior sheath wrapped around an interior tube. Here, we report that in living cells the cytoplasmic adenosine triphosphatase called ClpV specifically recognizes the contracted T6SS sheath structure, causing its disassembly within seconds. ClpV imaging allowed spatial and temporal documentation of cell-cell interactions (termed T6SS dueling) that likely mark the location of repeated T6SS-mediated protein translocation events between bacterial cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3557511/" 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/PMC3557511/" 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 -- Mekalanos, J 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. 2012 Aug 17;337(6096):815. doi: 10.1126/science.1222901. Epub 2012 Jul 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunobiology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22767897" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/genetics/metabolism ; Amino Acid Substitution ; Bacterial Proteins/genetics/*metabolism ; *Bacterial Secretion Systems ; Green Fluorescent Proteins/genetics/metabolism ; Microscopy, Fluorescence/methods ; Molecular Imaging/methods ; Mutation ; Protein Transport ; Pseudomonas aeruginosa/metabolism/*physiology ; Recombinant Fusion Proteins/genetics/metabolism ; Tyrosine/genetics/metabolism ; Vibrio cholerae/metabolism/*physiology
    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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  • 5
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    Synthesis of Substituted [8]Cycloparaphenylenes by [2 + 2 + 2] Cycloaddition (2014)
    American Chemical Society (ACS)
    Details
    Publication Date: 2014-03-06
    Description: Organic Letters DOI: 10.1021/ol500194s
    Print ISSN: 1523-7060
    Electronic ISSN: 1523-7052
    Topics: Chemistry and Pharmacology
    Published by American Chemical Society (ACS)
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  • 6
    Electronic Resource
    Electronic Resource
    Antiphase locking in a two-dimensional Josephson junction array (1996)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 80 (1996), S. 3598-3600 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We consider theoretically phase locking in a simple two-dimensional Josephson junction array consisting of two loops coupled via a joint line transverse to the bias current. Ring inductances are supposed to be small, and special emphasis is taken on the influence of external flux. It is shown that in the stable oscillation regime both cells oscillate with a phase shift equal to π (i.e., antiphase). This result may explain the low radiation output obtained so far in two-dimensional Josephson junction arrays experimentally. © 1996 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.363234
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  • 7
    Electronic Resource
    Electronic Resource
    How to achieve in-phase locking in small-inductance Josephson junction ladder arrays (1998)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 72 (1998), S. 252-254 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We present the results of an analytical study of phase locking in externally loaded two-dimensional Josephson junction ladder arrays with small, but non-vanishing ring inductances. A Lyapunov stability based condition is found controlling realization of the radiating in-phase oscillation regime. © 1998 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.120701
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  • 8
    Electronic Resource
    Electronic Resource
    On non-abelain SU(2) plane waves
    Amsterdam : Elsevier
    Physics Letters B 144 (1984), S. 83-86 
    Details
    ISSN: 0370-2693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0370-2693(84)90180-1
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  • 9
    Electronic Resource
    Electronic Resource
    Phase-locking in strongly coupled SQUID cells
    Amsterdam : Elsevier
    Physics Letters A 190 (1994), S. 489-494 
    Details
    ISSN: 0375-9601
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0375-9601(94)90739-0
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  • 10
    Electronic Resource
    Electronic Resource
    Canonical quantization and cosmological particle production in non-abelian gauge theories
    Amsterdam : Elsevier
    Physics Letters B 212 (1988), S. 418-422 
    Details
    ISSN: 0370-2693
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0370-2693(88)91791-1
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