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. / Department of Biology
| Identifer | oai:union.ndltd.org:BSU/oai:cardinalscholar.bsu.edu:handle/188457 |
| Date | January 2008 |
| Creators | Haaning, Kelsey L. |
| Contributors | McDowell, Susan A. |
| Source Sets | Ball State University |
| Detected Language | English |
| Format | viii, 80 leaves : ill. (some col.) ; 28 cm. |
| Source | Virtual Press |
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