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    Mechanism and Function of Actin Pedestal Formation by Enterohemorrhagic <em>Escherichia coli</em> O157:H7: A Dissertation

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    Authors
    Brady, Michael John
    Faculty Advisor
    Peter Pryciak, Ph.D.
    Academic Program
    Molecular Genetics and Microbiology
    UMass Chan Affiliations
    Biochemistry and Molecular Pharmacology
    Document Type
    Doctoral Dissertation
    Publication Date
    2007-06-14
    Keywords
    Escherichia coli O157
    Escherichia coli Proteins
    Actins
    Microfilaments
    Receptors
    Cell Surface
    Adhesins
    Escherichia coli
    Amino Acids, Peptides, and Proteins
    Bacteria
    Cells
    Macromolecular Substances
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    Abstract
    Enterohemorrhagic Escherichia coli O157:H7 (EHEC) and enteropathogenic E. coli O127:H7 (EPEC) induce characteristic F-actin rich pedestals on infected mammalian cells. Each pathogen delivers its own translocated intimin receptor (Tir) to the host cell to act as a receptor for the bacterial outer membrane adhesin, intimin. Interaction of translocated Tir with intimin is essential for mammalian cell binding and host colonization, as well as to induce actin pedestal formation in vitro. In spite of these parallels, EHEC and EPEC Tir appear to generate actin pedestals by distinct mechanisms. Further, while the ability to form actin pedestals is a striking phenotype, the function of pedestals during infection remains unclear. To address these issues, a systematic and quantitative analysis of Tir-mediated actin assembly was conducted. We identified a three-residue Tir sequence involved in actin pedestal formation for both EHEC and EPEC, and developed evidence that the two pathogens trigger a common pathway for actin assembly. Further, the ability of these bacteria to promote actin assembly appears to promote both intimin-mediated bacterial binding in vitro and optimal colonization during experimental animal infection.
    DOI
    10.13028/zjb9-1j13
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/31660
    Rights
    Copyright is held by the author, with all rights reserved.
    ae974a485f413a2113503eed53cd6c53
    10.13028/zjb9-1j13
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    Morningside GSBS Dissertations and Theses

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