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  • 1
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    Interbacterial signaling in Burkholderia [Microbiology] (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-07-21
    Description: In prokaryotes and eukaryotes, cell–cell communication and recognition of self are critical to coordinate multicellular functions. Although kin and kind discrimination are increasingly appreciated to shape naturally occurring microbe populations, the underlying mechanisms that govern these interbacterial interactions are insufficiently understood. Here, we identify a mechanism of interbacterial signal transduction...
    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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  • 2
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    Reverse transcriptase-mediated tropism switching in Bordetella bacteriophage (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-16
    Description: Host-pathogen interactions are often driven by mechanisms that promote genetic variability. We have identified a group of temperate bacteriophages that generate diversity in a gene, designated mtd (major tropism determinant), which specifies tropism for receptor molecules on host Bordetella species. Tropism switching is the result of a template-dependent, reverse transcriptase-mediated process that introduces nucleotide substitutions at defined locations within mtd. This cassette-based mechanism is capable of providing a vast repertoire of potential ligand-receptor interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liu, Minghsun -- Deora, Rajendar -- Doulatov, Sergei R -- Gingery, Mari -- Eiserling, Frederick A -- Preston, Andrew -- Maskell, Duncan J -- Simons, Robert W -- Cotter, Peggy A -- Parkhill, Julian -- Miller, Jeff F -- AI38417/AI/NIAID NIH HHS/ -- AI43986/AI/NIAID NIH HHS/ -- GM-08042/GM/NIGMS NIH HHS/ -- T32A107323/PHS HHS/ -- New York, N.Y. -- Science. 2002 Mar 15;295(5562):2091-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11896279" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages/enzymology/*genetics/*physiology/ultrastructure ; Bordetella bronchiseptica/genetics/metabolism/*virology ; *Genes, Viral ; Genetic Variation ; Genome, Viral ; Mutation ; RNA-Directed DNA Polymerase/genetics/*metabolism ; Receptors, Virus/metabolism ; Repetitive Sequences, Nucleic Acid ; Templates, Genetic
    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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  • 3
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    A widespread family of polymorphic contact-dependent toxin delivery systems in bacteria (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-11-19
    Description: Bacteria have developed mechanisms to communicate and compete with one another in diverse environments. A new form of intercellular communication, contact-dependent growth inhibition (CDI), was discovered recently in Escherichia coli. CDI is mediated by the CdiB/CdiA two-partner secretion (TPS) system. CdiB facilitates secretion of the CdiA 'exoprotein' onto the cell surface. An additional small immunity protein (CdiI) protects CDI(+) cells from autoinhibition. The mechanisms by which CDI blocks cell growth and by which CdiI counteracts this growth arrest are unknown. Moreover, the existence of CDI activity in other bacteria has not been explored. Here we show that the CDI growth inhibitory activity resides within the carboxy-terminal region of CdiA (CdiA-CT), and that CdiI binds and inactivates cognate CdiA-CT, but not heterologous CdiA-CT. Bioinformatic and experimental analyses show that multiple bacterial species encode functional CDI systems with high sequence variability in the CdiA-CT and CdiI coding regions. CdiA-CT heterogeneity implies that a range of toxic activities are used during CDI. Indeed, CdiA-CTs from uropathogenic E. coli and the plant pathogen Dickeya dadantii have different nuclease activities, each providing a distinct mechanism of growth inhibition. Finally, we show that bacteria lacking the CdiA-CT and CdiI coding regions are unable to compete with isogenic wild-type CDI(+) cells both in laboratory media and on a eukaryotic host. Taken together, these results suggest that CDI systems constitute an intricate immunity network with an important function in bacterial competition.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3058911/" 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/PMC3058911/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aoki, Stephanie K -- Diner, Elie J -- de Roodenbeke, Claire T'kint -- Burgess, Brandt R -- Poole, Stephen J -- Braaten, Bruce A -- Jones, Allison M -- Webb, Julia S -- Hayes, Christopher S -- Cotter, Peggy A -- Low, David A -- AI043986/AI/NIAID NIH HHS/ -- GM078634/GM/NIGMS NIH HHS/ -- R01 GM078634/GM/NIGMS NIH HHS/ -- U54 AI065359/AI/NIAID NIH HHS/ -- U54 AI065359-056074/AI/NIAID NIH HHS/ -- U54 AI065359-066074/AI/NIAID NIH HHS/ -- U54 AI065359-07/AI/NIAID NIH HHS/ -- U54AI065359/AI/NIAID NIH HHS/ -- England -- Nature. 2010 Nov 18;468(7322):439-42. doi: 10.1038/nature09490.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of California - Santa Barbara (UCSB), Santa Barbara, California 93106-9625, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21085179" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Toxins/chemistry/genetics/immunology/*metabolism ; Contact Inhibition/immunology/physiology ; Enterobacteriaceae/enzymology/genetics/metabolism ; Escherichia coli Proteins/antagonists & inhibitors/chemistry/genetics/metabolism ; Membrane Proteins/antagonists & inhibitors/chemistry/genetics/metabolism ; Molecular Sequence Data ; Uropathogenic Escherichia coli/enzymology/genetics/growth & ; development/*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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  • 4
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    Caspase-11 protects against bacteria that escape the vacuole (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-01-26
    Description: Caspases are either apoptotic or inflammatory. Among inflammatory caspases, caspase-1 and -11 trigger pyroptosis, a form of programmed cell death. Whereas both can be detrimental in inflammatory disease, only caspase-1 has an established protective role during infection. Here, we report that caspase-11 is required for innate immunity to cytosolic, but not vacuolar, bacteria. Although Salmonella typhimurium and Legionella pneumophila normally reside in the vacuole, specific mutants (sifA and sdhA, respectively) aberrantly enter the cytosol. These mutants triggered caspase-11, which enhanced clearance of S. typhimurium sifA in vivo. This response did not require NLRP3, NLRC4, or ASC inflammasome pathways. Burkholderia species that naturally invade the cytosol also triggered caspase-11, which protected mice from lethal challenge with B. thailandensis and B. pseudomallei. Thus, caspase-11 is critical for surviving exposure to ubiquitous environmental pathogens.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3697099/" 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/PMC3697099/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aachoui, Youssef -- Leaf, Irina A -- Hagar, Jon A -- Fontana, Mary F -- Campos, Cristine G -- Zak, Daniel E -- Tan, Michael H -- Cotter, Peggy A -- Vance, Russell E -- Aderem, Alan -- Miao, Edward A -- AI057141/AI/NIAID NIH HHS/ -- AI063302/AI/NIAID NIH HHS/ -- AI065359/AI/NIAID NIH HHS/ -- AI075039/AI/NIAID NIH HHS/ -- AI080749/AI/NIAID NIH HHS/ -- AI097518/AI/NIAID NIH HHS/ -- P01 AI063302/AI/NIAID NIH HHS/ -- P30 CA016086/CA/NCI NIH HHS/ -- R01 AI075039/AI/NIAID NIH HHS/ -- R01 AI080749/AI/NIAID NIH HHS/ -- R01 AI097518/AI/NIAID NIH HHS/ -- U19 AI100627/AI/NIAID NIH HHS/ -- U54 AI057141/AI/NIAID NIH HHS/ -- U54 AI065359/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2013 Feb 22;339(6122):975-8. doi: 10.1126/science.1230751. Epub 2013 Jan 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23348507" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Burkholderia/pathogenicity/physiology ; Burkholderia Infections/enzymology/immunology/metabolism ; Burkholderia pseudomallei/pathogenicity/physiology ; Caspases/*metabolism ; *Cell Death ; Cytosol/*microbiology ; Gram-Negative Bacterial Infections/enzymology/*immunology/microbiology ; Immunity, Innate ; Inflammasomes/metabolism ; Macrophages/immunology/*microbiology ; Mice ; Mice, Inbred C57BL ; Phagosomes/microbiology ; Salmonella Infections, Animal/enzymology/immunology/microbiology ; Salmonella typhimurium/pathogenicity/physiology ; Vacuoles/*microbiology
    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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    Triggering bacterial virulence (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cotter, P A -- Miller, J F -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1183-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of California at Los Angeles School of Medicine, 90095-1747, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8787124" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Adhesion ; Bacterial Outer Membrane Proteins/*genetics/secretion ; Bacterial Proteins/genetics ; Calcium/metabolism ; Escherichia coli/genetics/*pathogenicity ; *Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; HeLa Cells ; Humans ; Membrane Proteins/genetics ; *Phosphotransferases ; *Virulence/genetics ; Yersinia/genetics/*pathogenicity
    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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  • 6
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    Bordetella filamentous hemagglutinin plays a critical role in immunomodulation, suggesting a mechanism for host specificity (2005)
    National Academy of Sciences
    Details
    Publication Date: 2005-12-09
    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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