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Michael S. Donnenberg

Researcher at University of Maryland, Baltimore

Publications -  131
Citations -  15224

Michael S. Donnenberg is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Enteropathogenic Escherichia coli & Pilus. The author has an hindex of 55, co-authored 126 publications receiving 14656 citations. Previous affiliations of Michael S. Donnenberg include University of British Columbia & United States Department of Veterans Affairs.

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A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens.

TL;DR: It is reported that in EPEC a 35-kbp locus containing several regions implicated in formation of these lesions is found, which hybridize to E. coli O157:H7 and other pathogens of three genera that cause similar lesions but do not hybridized to avirulent members of the same species.
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Construction of an eae deletion mutant of enteropathogenic Escherichia coli by using a positive-selection suicide vector.

TL;DR: The use of a novel suicide vector containing the pir-dependent R6K replicon and the sacB gene of Bacillus subtilis to construct an eae deletion mutant of EPEC is reported, establishing the utility of a new system for the construction of deletion mutations.
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The complete sequence of the locus of enterocyte effacement (LEE) from enteropathogenic Escherichia coli E2348/69.

TL;DR: The entire LEE of EPEC strain E2348/69 is sequenced and the final LEE sequence entry contains corrections to some of these previously reported genes and predicted proteins and changes the name of several previously described genes comprising the type III secretion system ofEPEC.
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Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation

TL;DR: The identified EPEC chromosomal genes whose predicted protein sequences are similar to components of a recently described secretory pathway (type III) responsible for exporting proteins lacking a typical signal sequence suggest that the EPEC Sep proteins are component of a type III secretory apparatus necessary for the export of virulence determinants.