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dc.contributor.advisorJohn M. Leong
dc.contributor.authorCampellone, Kenneth Geno
dc.date2022-08-11T08:08:46.000
dc.date.accessioned2022-08-23T16:07:52Z
dc.date.available2022-08-23T16:07:52Z
dc.date.issued2003-05-22
dc.date.submitted2006-08-11
dc.identifier.doi10.13028/bgmm-dh06
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32334
dc.description<p>Some images did not scan well. Please consult original document.</p>
dc.description.abstractEnteropathogenic Escherichia coli (EPEC) and enterohemorrhagic E. coli O157:H7 (EHEC) form characteristic lesions on infected mammalian cells called actin pedestals. Each of these two pathogens injects its own translocated intimin receptor (Tir) molecule into the plasma membranes of host cells. Interaction of translocated Tir with the bacterial outer membrane protein intimin is required to trigger the assembly of actin into focused pedestals beneath bound bacteria. Despite similarities between the Tir molecules and the host components that associate with pedestals, recent work indicates that EPEC and EHEC Tir are not functionally interchangeable. For EPEC, Tir-mediated binding of Nck, a host adaptor protein implicated in actin signaling, is both necessary and sufficient to initiate actin assembly. In contrast, for EHEC, pedestals are formed independently of Nck, and require translocation of bacterial factors in addition to Tir to trigger actin signaling.
dc.language.isoen_US
dc.rightsCopyright is held by the author, with all rights reserved.
dc.subjectActins
dc.subjectAdhesins
dc.subjectEscherichia coli
dc.subjectEscherichia coli Proteins
dc.subjectReceptors
dc.subjectCell Surface
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBacteria
dc.subjectMacromolecular Substances
dc.titleActin Pedestal Formation on Mammalian Cells by Enteropathogenic <em>Escherichia coli</em>: A Dissertation
dc.typeDoctoral Dissertation
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1095&amp;context=gsbs_diss&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_diss/95
dc.legacy.embargo2017-04-24T00:00:00-07:00
dc.identifier.contextkey191370
refterms.dateFOA2022-08-24T04:22:06Z
html.description.abstract<p>Enteropathogenic <em>Escherichia coli</em> (EPEC) and enterohemorrhagic <em>E. coli</em> O157:H7 (EHEC) form characteristic lesions on infected mammalian cells called actin pedestals. Each of these two pathogens injects its own translocated intimin receptor (Tir) molecule into the plasma membranes of host cells. Interaction of translocated Tir with the bacterial outer membrane protein intimin is required to trigger the assembly of actin into focused pedestals beneath bound bacteria. Despite similarities between the Tir molecules and the host components that associate with pedestals, recent work indicates that EPEC and EHEC Tir are not functionally interchangeable. For EPEC, Tir-mediated binding of Nck, a host adaptor protein implicated in actin signaling, is both necessary and sufficient to initiate actin assembly. In contrast, for EHEC, pedestals are formed independently of Nck, and require translocation of bacterial factors in addition to Tir to trigger actin signaling.</p>
dc.identifier.submissionpathgsbs_diss/95
dc.contributor.departmentMolecular Genetics & Microbiology
dc.description.thesisprogramMolecular Genetics and Microbiology


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