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Investigation of glycosylation in flagellin biosynthesis and LPS O-antigen biosynthesis in Aeromonas caviae

Rui, Shengtao (2018) Investigation of glycosylation in flagellin biosynthesis and LPS O-antigen biosynthesis in Aeromonas caviae. MPhil thesis, University of Sheffield.

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Abstract

Aeromonas species are Gram-negative facultative anaerobic bacteria which are widespread in fresh water and salt water. Aeromonas caviae and Aeromonas hydrophila are two kinds of mesophilic aeromonads which belong to genus Aeromonas and are emerging as major pathogens in humans. Flagella are important pathogenic factors of bacteria and there are two kinds of flagella discovered in A. caviae and A. hydrophila which are polar flagella and lateral flagella (Rabaan et al. 2001; Tabei et al. 2009; Canals et al. 2006a). The flagella of Aeromonas are glycosylated and investigation of glycosylation in flagellin biosynthesis is valuable for the understanding of pathogenicity of Aeromonas species. The aim of this project is to investigate the glycosylation during flagellin biosynthesis in A. caviae. It has been discovered that the flagella of A. caviae are glycosylated 6 to 8 times by Pse5Ac7Ac which is under the control of Maf1 which is known as flagellin glycosyl-transferase (Parker et al. 2012). Theoretically, Maf1 of A. caviae Sch3N has the ability to transfer activated pseudaminic acid (CMP- Pse5Ac7Ac) to the hydroxyl group of serine and threonine residues in the central immunogenic D2/D3 domain of flagellin of A. caviae Sch3N (Parker et al. 2012; Tabei et al. 2009). The details of how Maf1 interacts with flagellin will be explored in this project. CMP-Pse5Ac7Ac which is the substrate for glycosylation is generated from UDP-GlcNAc. The biosynthesis of CMP-Pse5Ac7Ac is under the control of flm locus including flmA, flmB, neuA, neuB, flmD. The pseudaminic acid biosynthetic pathway has been confirmed in Campylobacter jejuni and related enzymes are homologous proteins of A. caviae (Schoenhofen et al. 2006). The proteins encoded by the flm genes will be applied in this project to investigate the biosynthesis of CMP- Pse5Ac7Ac. In addition, there is evidence that the LPS O-antigen incorporates with Pse5Ac7Ac. The substrate of O-antigen glycosylation is also CMP-Pse5Ac7Ac (Tomás 2012). The connections between glycosylation in LPS O-antigen biosynthesis and flagellin biosynthesis will be investigated in this project.

Item Type: Thesis (MPhil)
Academic Units: The University of Sheffield > Faculty of Medicine, Dentistry and Health (Sheffield)
The University of Sheffield > Faculty of Medicine, Dentistry and Health (Sheffield) > Medicine (Sheffield)
Depositing User: Mr Shengtao Rui
Date Deposited: 16 Apr 2018 09:38
Last Modified: 16 Apr 2018 09:38
URI: http://etheses.whiterose.ac.uk/id/eprint/19565

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