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  • 1
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    Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-02-04
    Description: The success of Mycobacterium species as pathogens depends on their ability to maintain an infection inside the phagocytic vacuole of the macrophage. Although the bacteria are reported to modulate maturation of their intracellular vacuoles, the nature of such modifications is unknown. In this study, vacuoles formed around Mycobacterium avium failed to acidify below pH 6.3 to 6.5. Immunoelectron microscopy of infected macrophages and immunoblotting of isolated phagosomes showed that Mycobacterium vacuoles acquire the lysosomal membrane protein LAMP-1, but not the vesicular proton-adenosine triphosphatase (ATPase) responsible for phagosomal acidification. This suggests either a selective inhibition of fusion with proton-ATPase-containing vesicles or a rapid removal of the complex from Mycobacterium phagosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sturgill-Koszycki, S -- Schlesinger, P H -- Chakraborty, P -- Haddix, P L -- Collins, H L -- Fok, A K -- Allen, R D -- Gluck, S L -- Heuser, J -- Russell, D G -- AI26889/AI/NIAID NIH HHS/ -- AI34207/AI/NIAID NIH HHS/ -- AR42370/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Feb 4;263(5147):678-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University Medical Center, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8303277" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Hydrogen-Ion Concentration ; Leishmania mexicana/physiology ; Lysosome-Associated Membrane Glycoproteins ; Macrophages/metabolism/*microbiology/parasitology/ultrastructure ; Membrane Fusion ; Membrane Glycoproteins/metabolism ; Mice ; Microscopy, Immunoelectron ; Mycobacterium avium/*physiology ; Mycobacterium tuberculosis/physiology ; Phagosomes/metabolism/*microbiology/parasitology/ultrastructure ; Proton-Translocating ATPases/*metabolism ; Vacuoles/metabolism/microbiology/parasitology/ultrastructure
    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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    Infection by tubercular mycobacteria is spread by nonlytic ejection from their amoeba hosts (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-28
    Description: To generate efficient vaccines and cures for Mycobacterium tuberculosis, we need a far better understanding of its modes of infection, persistence, and spreading. Host cell entry and the establishment of a replication niche are well understood, but little is known about how tubercular mycobacteria exit host cells and disseminate the infection. Using the social amoeba Dictyostelium as a genetically tractable host for pathogenic mycobacteria, we discovered that M. tuberculosis and M. marinum, but not M. avium, are ejected from the cell through an actin-based structure, the ejectosome. This conserved nonlytic spreading mechanism requires a cytoskeleton regulator from the host and an intact mycobacterial ESX-1 secretion system. This insight offers new directions for research into the spreading of tubercular mycobacteria infections in mammalian cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2770343/" 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/PMC2770343/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagedorn, Monica -- Rohde, Kyle H -- Russell, David G -- Soldati, Thierry -- AI 067027/AI/NIAID NIH HHS/ -- HL 055936/HL/NHLBI NIH HHS/ -- R01 AI067027/AI/NIAID NIH HHS/ -- R01 AI067027-04/AI/NIAID NIH HHS/ -- R01 HL055936/HL/NHLBI NIH HHS/ -- R01 HL055936-09/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2009 Mar 27;323(5922):1729-33. doi: 10.1126/science.1169381.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departement de Biochimie, Faculte des Sciences, Universite de Geneve, Sciences II, 30 quai Ernest Ansermet, CH-1211 Geneve-4, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19325115" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*physiology ; Animals ; Bacterial Proteins/metabolism ; Cell Membrane/microbiology ; Cytoskeleton/*microbiology/physiology/ultrastructure ; Cytosol/microbiology ; Dictyostelium/*microbiology/ultrastructure ; GTP Phosphohydrolases/metabolism ; Mycobacterium avium/genetics/pathogenicity/*physiology ; Mycobacterium marinum/genetics/pathogenicity/*physiology ; Mycobacterium tuberculosis/genetics/pathogenicity/*physiology ; Phagocytosis ; Pressure ; 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)
    Location Call Number Expected Availability
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