Use this URL to cite or link to this record in EThOS:
Title: Molecular and biochemical characterisation of glycosyltransferases involved in cell wall assembly of Corynebacterineae
Author: Jankute, Monika
ISNI:       0000 0004 5351 2210
Awarding Body: University of Birmingham
Current Institution: University of Birmingham
Date of Award: 2015
Availability of Full Text:
Access from EThOS:
Full text unavailable from EThOS. Thesis embargoed until 01 Jun 2018
Access from Institution:
Mycobacterium tuberculosis, the etiological agent of tuberculosis, remains the leading cause of mortality from a single infectious organism. The persistence of this human pathogen is associated with its distinctive lipid rich cell wall structure that is highly impermeable to hydrophilic drugs. This highly complex and unique structure is crucial for the growth, viability and virulence of M. tuberculosis, thus representing an attractive target for vaccine and drug development. In this study, we have demonstrated that enzymes involved in Corynebacterium glutamicum cell wall assembly and precursor formation build complicated multi-protein complexes. Specifically, we have identified 24 putative interactions in vivo between 12 proteins responsible for AG biosynthesis. Additionally, we have investigated enzymes involved in the assembly of both AG and LAM biosynthesis in M. smegmatis and C. glutamicum. Finally, we examined biophysical characterisation of membrane cell wall proteins solubilised in a stryrene maleic acid polymer, demonstrating that detergent free extraction of highly hydrophobic proteins from corynebacteria is possible. These findings provide a useful recourse for understanding the biosynthesis and function of the vital cell wall (lipo)polysaccharides of Corynebacterineae, as well as providing new therapeutic targets for drug design against the pathogenic species of M. tuberculosis, Mycobacterium marinum and Corynebacterium diphtheriae.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: QH301 Biology