Proteomic profile of Mycobacterium tuberculosis after eupomatenoid-5 induction reveals potential drug targets. (August 2017)

• Record Type: Journal Article
• Authors: Ghiraldi-Lopes, Luciana D; Campanerut-Sá, Paula AZ; Meneguello, Jean E; Seixas, Flávio AV; Lopes-Ortiz, Mariana A; Scodro, Regiane BL; Pires, Claudia TA; da Silva, Rosi Z; Siqueira, Vera LD; Nakamura, Celso V; Cardoso, Rosilene F
• Is Part Of: Future microbiology. Volume 12:Number 10(2017)
• Page Start: 867
• Page End: 879
• Publication Date: 2017-08
• Subjects: 2D gel electrophoresis -- drug targets -- eupomatenoid-5 -- LC/MS-MS -- Mycobacterium tuberculosis -- protein changes -- proteome -- scanning electron microscopy -- STRING database -- tuberculosis; Microbiology -- Research -- Periodicals; 616.9041
• DOI: 10.2217/fmb-2017-0023
• Languages: English
• ISSNs: 1746-0913

Abstract

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).