The ability of Shigella flexineri to spread within and between epithelial cells is essential for Shigella infection causing bacillary dysentery. This is a particular problem in the developing world. The movement of Shigella within the host cell requires the accumulation of actin at one pole of the bacterium and the protein VirG is responsible for this function. While the C-terminal domain (β-domain) of VirG is integrated into the outer membrane of Shigella, the N-Terminal domain (α-domain) is exposed on the surface of the bacterium. The β-domain acts as autotransporter of the α-domain. The exposed α-domain has multiple binding partners including N-WASP, Vinculin and IcsB that are required for infection in man and cell to cell spread. To understand the molecular basis of VirG’s activity, it is first necessary to produce the protein in quantity; this study investigates the expression of VirG α-domain in E.coli. The optimum construct corresponded to residues 58-506 of VirG expressed in Rossetta-gami cells.
| Identifer | oai:union.ndltd.org:bl.uk/oai:ethos.bl.uk:667463 |
| Date | January 2015 |
| Creators | Tashiro, Yumiko |
| Publisher | Queen Mary, University of London |
| Source Sets | Ethos UK |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Source | http://qmro.qmul.ac.uk/xmlui/handle/123456789/9097 |
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