Characterising the role of human mTOR in Listeria monocytogenes infection
|dc.contributor.author||Law, Daria Rose|
|dc.identifier.citation||Law, D. R. (2013). Characterising the role of human mTOR in Listeria monocytogenes infection (Thesis, Bachelor of Biomedical Sciences with Honours). University of Otago. Retrieved from http://hdl.handle.net/10523/4481||en|
|dc.description.abstract||The pathogenic food bourne bacterium Listeria monocytogenes has the potential to cause gastroenteritis, meningitis and abortion in an infected individual. L. monocytogenes is a facultative intracellular bacterium that facilitates its internalisation into some host cells by binding of the bacterial surface protein InlB with its cognate human receptor, the receptor tyrosine kinase Met. This binding stimulates a number of cellular signaling events, which ultimately lead to host cell membrane rearrangement and engulfment of the bacterium. One human signaling protein the Mammalian target of Rapamycin (mTOR) was recently shown to be important in the InlB mediated internalisation of L. monocytogenes. However the molecular mechanism underlying mTOR’s role in internalisation is not understood. Using an RNA interference based method, this project set out to elucidate which components of mTOR are important in L. monocytogenes internalisation into the human epithelial cell line HeLa. Here we find that the mammalian target of rapamycin complex 2 (mTORC2) and its downstream substrate PKC-α are involved in the InlB mediated internalisation of L. monocytogenes into the epithelial cell line HeLa.|
|dc.publisher||University of Otago|
|dc.rights||All items in OUR Archive are provided for private study and research purposes and are protected by copyright with all rights reserved unless otherwise indicated.|
|dc.title||Characterising the role of human mTOR in Listeria monocytogenes infection|
|thesis.degree.discipline||Microbiology and Immunology|
|thesis.degree.name||Bachelor of Biomedical Sciences with Honours|
|thesis.degree.grantor||University of Otago|
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