Deletion of the phosphoinositide-3-kinase RhoGAP domain to assess inhibition of Staphylococcus aureus infection

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dc.contributor.advisor McDowell, Susan A. en_US
dc.contributor.author Haaning, Kelsey L. en_US
dc.date.accessioned 2011-06-03T19:41:44Z
dc.date.available 2011-06-03T19:41:44Z
dc.date.created 2008 en_US
dc.date.issued 2008
dc.identifier LD2489.Z78 2008 .H33 en_US
dc.identifier.uri http://cardinalscholar.bsu.edu/handle/handle/188457
dc.description.abstract It is important to understand the mechanism of endocytic invasion into the host cell by Staphylococcus aureus. Activation of phosphoinositide-3-kinase (PI3K) is essential to S. aureus invasion. In a normal cell, the p85 subunit of PI3K is bound at the Rho GTPase activating protein (RhoGAP) domain to small guanosine triphosphate binding proteins (GTPases), which are attached to the cell membrane by a prenyl group. This association anchors PI3K near the cellular membrane. PI3K must be anchored near the membrane in order to phosphorylate its substrate. The hypothesis for this project is that deletion of the binding domain between PI3K and small GTPases will block endocytic bacterial invasion by sequestering PI3K in the cytosol. To investigate this hypothesis, the RhoGAP binding domain of PI3K p85 was mutated using site-directed mutagenesis and S. aureus invasion was reduced by up to 86% (p<0.05), which shows that this domain is important to bacterial invasion.
dc.description.sponsorship Department of Biology
dc.format.extent viii, 80 leaves : ill. (some col.) ; 28 cm. en_US
dc.source Virtual Press en_US
dc.subject.lcsh Phosphotransferases. en_US
dc.subject.lcsh Rho GTPases -- Inhibitors. en_US
dc.subject.lcsh Staphylococcus aureus infections -- Treatment. en_US
dc.title Deletion of the phosphoinositide-3-kinase RhoGAP domain to assess inhibition of Staphylococcus aureus infection en_US
dc.title.alternative RhoGAP deletion en_US
dc.description.degree Thesis (M.S.)
dc.identifier.cardcat-url http://liblink.bsu.edu/catkey/1398713 en_US


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  • Master's Theses [5454]
    Master's theses submitted to the Graduate School by Ball State University master's degree candidates in partial fulfillment of degree requirements.

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