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  • Virulence  (2)
  • *Calcium-Binding Proteins  (1)
  • Calcium-Calmodulin-Dependent Protein Kinases/*antagonists & inhibitors  (1)
  • 1
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    Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-18
    Description: The bacterial pathogen Yersinia uses a type III secretion system to inject several virulence factors into target cells. One of the Yersinia virulence factors, YopJ, was shown to bind directly to the superfamily of MAPK (mitogen-activated protein kinase) kinases (MKKs) blocking both phosphorylation and subsequent activation of the MKKs. These results explain the diverse activities of YopJ in inhibiting the extracellular signal-regulated kinase, c-Jun amino-terminal kinase, p38, and nuclear factor kappa B signaling pathways, preventing cytokine synthesis and promoting apoptosis. YopJ-related proteins that are found in a number of bacterial pathogens of animals and plants may function to block MKKs so that host signaling responses can be modulated upon infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orth, K -- Palmer, L E -- Bao, Z Q -- Stewart, S -- Rudolph, A E -- Bliska, J B -- Dixon, J E -- 18024/PHS HHS/ -- AI35175/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 17;285(5435):1920-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10489373" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*physiology ; Calcium-Calmodulin-Dependent Protein Kinases/*antagonists & inhibitors ; Cell Line ; Enzyme Activation ; Enzyme Inhibitors/*pharmacology ; HeLa Cells ; Humans ; *MAP Kinase Kinase Kinase 1 ; NF-kappa B/metabolism ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Transfection ; Virulence ; Yersinia pseudotuberculosis/genetics/metabolism/pathogenicity/*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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    Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-25
    Description: Homologs of the Yersinia virulence effector YopJ are found in both plant and animal bacterial pathogens, as well as plant symbionts. These YopJ family members were shown to act as cysteine proteases. The catalytic triad of the protease was required for inhibition of the mitogen-activated protein kinase (MAPK) and nuclear factor kappaB (NF-kappaB) signaling in animal cells and for induction of localized cell death in plants. The substrates for YopJ were shown to be highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ family members exert their pathogenic effect on cells by disrupting this posttranslational modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orth, K -- Xu, Z -- Mudgett, M B -- Bao, Z Q -- Palmer, L E -- Bliska, J B -- Mangel, W F -- Staskawicz, B -- Dixon, J E -- 18024/PHS HHS/ -- AI41599/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090361" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Catalysis ; Catalytic Domain ; Cell Line ; Cysteine Endopeptidases/chemistry/genetics/*metabolism ; Humans ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Plant Leaves/cytology/virology ; SUMO-1 Protein ; Sequence Alignment ; Signal Transduction ; Transfection ; Ubiquitins/metabolism ; Virulence ; Xanthomonas campestris/enzymology/pathogenicity ; Yersinia pseudotuberculosis/enzymology/metabolism/*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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  • 3
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    A process for controlling intracellular bacterial infections induced by membrane injury (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-05
    Description: Strategies for inhibiting phagolysosome fusion are essential for the intracellular survival and replication of many pathogens. We found that the lysosomal synaptotagmin Syt VII is required for a mechanism that promotes phagolysosomal fusion and limits the intracellular growth of pathogenic bacteria. Syt VII was required for a form of Ca2+-dependent phagolysosome fusion that is analogous to Ca2+-regulated exocytosis of lysosomes, which can be triggered by membrane injury. Bacterial type III secretion systems, which permeabilize membranes and cause Ca2+ influx in mammalian cells, promote lysosomal exocytosis and inhibit intracellular survival in Syt VII +/+ but not -/- cells. Thus, the lysosomal repair response can also protect cells against pathogens that trigger membrane permeabilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roy, Deepannita -- Liston, David R -- Idone, Vincent J -- Di, Anke -- Nelson, Deborah J -- Pujol, Celine -- Bliska, James B -- Chakrabarti, Sabyasachi -- Andrews, Norma W -- AI34867/AI/NIAID NIH HHS/ -- AI43389/AI/NIAID NIH HHS/ -- AI48507/AI/NIAID NIH HHS/ -- GM64625/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 4;304(5676):1515-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis and Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15178804" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacteria/*growth & development/metabolism ; Bacterial Proteins/genetics/metabolism ; CHO Cells ; Calcium/metabolism ; *Calcium-Binding Proteins ; Cell Membrane/*physiology ; Cells, Cultured ; Cricetinae ; Endocytosis ; Exocytosis ; Listeria monocytogenes/growth & development ; Lysosomes/microbiology/physiology ; Macrophages/microbiology ; Membrane Glycoproteins/genetics/*physiology ; Mice ; Mutation ; Nerve Tissue Proteins/genetics/*physiology ; Permeability ; Phagosomes/microbiology/physiology ; Salmonella typhimurium/*growth & development/metabolism ; Synaptotagmins ; Vacuoles/microbiology ; Yersinia pseudotuberculosis/genetics/growth & development
    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)
    Location Call Number Expected Availability
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