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dc.contributor.authorTashiro, Yumiko
dc.identifier.citationTashiro. Y. 2015. Overproduction of recombinant VirG from Shigella flexneri. Queen Mary University of London.en_US
dc.description.abstractThe 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 (domain) of VirG is integrated into the outer membrane of Shigella, the N-Terminal domain (domain) is exposed on the surface of the bacterium. The -domain acts as autotransporter of the domain. The exposed 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 domain in E.coli. The optimum construct corresponded to residues 58-506 of VirG expressed in Rossetta-gami cells.en_US
dc.publisherQueen Mary University of London
dc.subjectElectronic Waste recycling Malaysiaen_US
dc.subjectElectronic Waste recycling Singaporeen_US
dc.subjectElectrical waste recycling Malaysiaen_US
dc.subjectElectrical waste recycling Singaporeen_US
dc.titleOverproduction of recombinant VirG from Shigella flexneri.en_US
dc.rights.holderThe copyright of this thesis rests with the author and no quotation from it or information derived from it may be published without the prior written consent of the author

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