Enzymatic Study of Lipid A Phosphoethanolamine Transferase from Pathogenic Neisseria
A wide variety of antibiotics are targeted to the bacterial membrane due to its unique arrangement and composition relative to the host mammalian membranes. Two pathogenic Neisseria species, N. meningitidis and N. gonorrhoeae, modify the lipid A (endotoxin) component found in the outer membrane through the addition of phosphoethanolamine (pEtN). This modification, catalysed by enzyme lipid A phosphoethanolamine transferase (EptA), confers resistance to polymyxin and the host immune system. Through enzymatic studies and protein crystallography, the catalytic mechanism of the enzyme will be studied and used as guidance for the development of potential inhibitor compounds against EptA.
Importance of Research
The main goal of this study is to understand the molecular mechanism of interaction between EptA, its substrates and potential inhibitors. This knowledge will lead to the development of novel therapeutic agents as anti-virulence factors that will improve the clearance of N. gonorrhoeae and N. meningitidis by the human innate immune response or in combination with current antibiotics.
The University of Western Australia
4 Oct 2016 → 23 Jan 2019
Award Date: 27 Jul 2019
Pelita Harapan University
10 Aug 2009 → 6 Sep 2013
Award Date: 6 Sep 2013
Research expertise keywords
- Structural biology