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System for Efficacy and Cytotoxicity Screening of Inhibitors Targeting Intracellular Mycobacterium tuberculosis
Published on: April 5, 2017
Proteomic profile of Mycobacterium tuberculosis after eupomatenoid-5 induction reveals potential drug targets
Luciana D Ghiraldi-Lopes1,2, Paula Az Campanerut-Sá2, Jean E Meneguello3
1Postgraduate Program in Health Sciences, Department of Clinical Analyses & Biomedicine, State University of Maringá, Avenida Colombo, 5790, 87020-900, Maringá, Paraná, Brazil.
Aim:
We investigated a proteome profile, protein-protein interaction and morphological changes of Mycobacterium tuberculosis after different times of eupomatenoid-5 (EUP-5) induction to evaluate the cellular response to the drug-induced damages.
Methods:
The bacillus was induced to sub-minimal inhibitory concentration of EUP-5 at 12 h, 24 h and 48 h. The proteins were separated by 2D gel electrophoresis, identified by LC/MS-MS. Scanning electron microscopy and Search Tool for the Retrieval of Interacting Genes/Proteins analyses were performed.
Results:
EUP-5 impacts mainly in M. tuberculosis proteins of intermediary metabolism and interactome suggests a multisite disturbance that contributes to bacilli death. Scanning electron microscopy revealed the loss of bacillary form.
Conclusion:
Some of the differentially expressed proteins have the potential to be drug targets such as citrate synthase (Rv0896), phosphoglycerate kinase (Rv1437), ketol-acid reductoisomerase (Rv3001c) and ATP synthase alpha chain (Rv1308).
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