Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.639854
Title: Studies on the structure, lipid modification and interactions of the virulence-associated proteins of Rhodococcus equi
Author: Okoko, Tebekeme
ISNI:       0000 0004 5365 5676
Awarding Body: Northumbria University
Current Institution: Northumbria University
Date of Award: 2014
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Abstract:
Rhodococcus equi is a Gram-positive soil organism that causes an aggressive bronchopneumonia in foals and opportunistic infections in immuno-compromised humans. Virulent strains possess an 80 – 90 kb plasmid that encodes an immunogenic surface-located virulence-associated protein VapA. The virulence of the organism has been largely attributed to this protein since mutants lacking vapA are attenuated for virulence in mice. VapA is an unusual lipoprotein and existing evidence suggests its biogenesis may not involve normal lipoprotein processing. In order to understand the structure of VapA and other virulence associated proteins, their genes were cloned, expressed, purified and crystallised. VapG produce high quality crystals that diffracted to 1.8 Å. The structure was resolved to be a closed β-barrel with a long unstructured N-terminus which is similar to both VapB and VapD which have also recently been characterised.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.639854  DOI: Not available
Keywords: C500 Microbiology
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