Role of Type IV Pili in the Pathogenesis of Enterovirulent Bacteria

atmire.migration.oldid3207
dc.contributor.advisorArmstrong, Glen
dc.contributor.authorMartinez de la Peña, Claudia Fabiola
dc.date.accessioned2015-05-01T18:20:50Z
dc.date.available2015-06-22T07:00:49Z
dc.date.issued2015-05-01
dc.date.submitted2015en
dc.description.abstractType IV pili (T4P) are filamentous structures formed by polymerization of thousands of pilin subunits. They are involved in diverse bacterial functions including twitching motility, DNA uptake, phage attachment, and adherence to biotic and abiotic surfaces. In some bacterial models, T4P are virulence factors involved in host cell adherence. Besides the major structural pilin subunit, T4P possess minor pilin-like proteins. T4P are expressed in many Gram-negative bacteria and were recently found in Gram-positive bacteria. Enteropathogenic Escherichia coli (EPEC) and Clostridium difficile (C. difficile) are two enterovirulent bacteria that cause diarrhoeagenic illness by different mechanisms. EPEC express T4P called Bundle forming pili (BFP) that are involved in the initial adherence of the bacteria to host-cells. C. difficile has the genes required for T4P but their expression or function are unknown. In my study I used a combination of genetic and imaging techniques to investigate T4P expressed by both EPEC and C. difficile. In EPEC, I investigated the role of three pilin-like proteins BfpI, BfpJ, and BfpK in the BFP structure and function. I found that all three proteins are co-assembled in BFP. I also found that BfpI is involved in EPEC adhesion to HEp-2 cells since the phenotype of localized adherence was lost in EPEC expressing BFP without BfpI. I also found that BfpJ is involved in regulating pilus extension since BFP lacking BfpJ forms only short pilus structures. Finally, although BfpK is co-assembled with BfpA within the pilus filament, I could not detect any phenotypic differences between BfpK-deficient and wild-type BFP. In the study involving C. difficile I found growing conditions, which allowed the bacteria to express T4P bundles in the hypervirulent R20291 strain. I then used pilin and pilin-like mutants to discover that only PilA1 and PilU proteins are essential for pilus expression in C. difficile and that PilA1 and PilJ proteins are present within the pilus filament. Furthermore, searching for a role of T4P in colonization, I found that C. difficile T4P is not involved, at least in mice, since there was no difference between wild-type and T4P mutant strains in infecting mice.en_US
dc.identifier.citationMartinez de la Peña, C. F. (2015). Role of Type IV Pili in the Pathogenesis of Enterovirulent Bacteria (Doctoral thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/27688en_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/27688
dc.identifier.urihttp://hdl.handle.net/11023/2224
dc.language.isoeng
dc.publisher.facultyGraduate Studies
dc.publisher.institutionUniversity of Calgaryen
dc.publisher.placeCalgaryen
dc.rightsUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.
dc.subjectMicrobiology
dc.subject.classificationT4Pen_US
dc.subject.classificationEPECen_US
dc.subject.classificationC.difficileen_US
dc.subject.classificationpilin-likeen_US
dc.subject.classificationTEMen_US
dc.subject.classificationType IV pilien_US
dc.titleRole of Type IV Pili in the Pathogenesis of Enterovirulent Bacteria
dc.typedoctoral thesis
thesis.degree.disciplineMicrobiology & Infectious Diseases
thesis.degree.grantorUniversity of Calgary
thesis.degree.nameDoctor of Philosophy (PhD)
ucalgary.item.requestcopytrue
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