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    Role of the S. typhimurium actin-binding protein SipA in bacterial internalization (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-03-26
    Description: Entry of the bacterium Salmonella typhimurium into host cells requires membrane ruffling and rearrangement of the actin cytoskeleton. Here, it is shown that the bacterial protein SipA plays a critical role in this process. SipA binds directly to actin, decreases its critical concentration, and inhibits depolymerization of actin filaments. These activities result in the spatial localization and more pronounced outward extension of the Salmonella-induced membrane ruffles, thereby facilitating bacterial uptake.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, D -- Mooseker, M S -- Galan, J E -- AI30492/AI/NIAID NIH HHS/ -- DK25387/DK/NIDDK NIH HHS/ -- GM52543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Mar 26;283(5410):2092-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Boyer Center for Molecular Medicine, Yale School of Medicine, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10092234" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry/genetics/*metabolism ; Antigens, Bacterial/metabolism ; Bacterial Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Biopolymers ; Cell Membrane/ultrastructure ; HeLa Cells ; Humans ; *Microfilament Proteins ; Microscopy, Fluorescence ; Mutation ; Recombinant Fusion Proteins/metabolism ; Salmonella typhimurium/genetics/metabolism/*pathogenicity ; Signal Transduction ; Vinculin/metabolism
    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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    Salmonella modulates vesicular traffic by altering phosphoinositide metabolism (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-19
    Description: Salmonella enterica, the cause of food poisoning and typhoid fever, induces actin cytoskeleton rearrangements and membrane ruffling to gain access into nonphagocytic cells, where it can replicate and avoid innate immune defenses. Here, we found that SopB, a phosphoinositide phosphatase that is delivered into host cells by a type III secretion system, was essential for the establishment of Salmonella's intracellular replicative niche. SopB mediated the formation of spacious phagosomes following bacterial entry and was responsible for maintaining high levels of phosphatidylinositol-three-phosphate [PtdIns(3)P] in the membrane of the bacteria-containing vacuoles. Absence of SopB caused a significant defect in the maturation of the Salmonella-containing vacuole and impaired bacterial intracellular growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hernandez, Lorraine D -- Hueffer, Karsten -- Wenk, Markus R -- Galan, Jorge E -- AI055472/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1805-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15205533" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/metabolism ; Bacterial Proteins/genetics/*metabolism ; Cell Line ; Cell Membrane/metabolism/ultrastructure ; Cytoplasmic Vesicles/metabolism/*microbiology/ultrastructure ; Epithelial Cells/microbiology ; Gene Deletion ; Genomic Islands ; Humans ; Intestinal Mucosa/cytology/*microbiology ; Lysosome-Associated Membrane Glycoproteins ; Microscopy, Video ; Mutation ; Phagosomes/metabolism/*microbiology ; Phosphatidylinositol Phosphates/metabolism ; Phosphatidylinositols/*metabolism ; Recombinant Fusion Proteins/metabolism ; Salmonella typhimurium/genetics/growth & development/*metabolism/pathogenicity ; Vacuoles/metabolism/microbiology/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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
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