A CRITICAL INSIGHT INTO SHIKIMATE KINASE PATHWAY
Objective: Tuberculosis is the most infectious disease that appears to be dreadful even in the presence of anti tubercular drugs. The problem of MDR-TB is growing at an alarming rate and the prevalence of the disease cause devastation to the molecular level. We hereby carry out a review of shikimate pathway used for tuberculosis management. Based on the available evidence on its vital roles, we highlight ways in which their therapeutic potential can be properly harnessed for possible integration into the country's healthcare system.
Methods: Information was obtained from a literature search of electronic databases such as Google Scholar, Pubmed and Scopus up to 20115 for publications on shikimate pathways and their therapeutic targets for Multi Drug Resistance Tuberculosis (MDR-TB).
Results: Numerous factors have been reported to be the causative agent in the progression of the disease. Apart from this, a number of transcription factors is also been involved in the down regulation of the modulatory pathology. The emergence of MDR-TB washes out the treatment and control of Tuberculosis at an extremely difficult stage. Epidemilogical data revels that Tuberculosis kill approx. 3 million people in a year. Shikimate Kinase and other agents can be involved therapeutic target and evaluation of new pathways. Emphasis need to be urgently given for the diagnosis and treatment of the TB in the society effectively.
Conclusion: This review, therefore, provides a useful resource to enable a thorough assessment of the profile of Shikimate Kinase Pathway used in MDR-TB management so as to ensure a more rational use. Shikimate Kinase is one of the main enzymes involved in Shikimate pathway that has emerged as a vital target in many of the morbidity.Keywords: Tuberculosis, MDR-TB, Shikimate Kinase, Shikimate pathway.
2. Diana M, Joao P, Jorge R, Isabel C, Isabel P, Claudia R, et al. High-level resistance to isoniazid and ethionamide in multidrug-resistant mycobacterium tuberculosis of the Lisboa family is associated with inhA double mutations. J Antimicrobial Chemother 2013;68:1728-32.
3. Marais BJ, Mlambo CK, Nalin R, Thierry Z, Adriano GD, Thomas CV, et al. Epidemic spread of multidrug-resistant tuberculosis in Johannesburg, South Afr J Clin Microbiol 2013;51:1818-25.
4. Lukas F, Matthias E, Thomas B, Ekkehardt A, Marcel Z, Katia J, et al. Effect of mutation and genetic background on drug resistance in Mycobacterium tuberculosis. Antimicrob Agents Chemother 2012;56:3047-53.
5. Yu P, Yang Z, Bing Z, Guan L, Guanglu J, Hui X, et al. Spoligotyping and drug resistance analysis of Mycobacterium tuberculosis strains from national survey in China. Plos One 2012;7:329-76.
6. Juan W, Yan L, Chun-Lei Z, Bin-Ying J, Liu-Zhuo Z, Yong-Zhen S, et al. Genotypes and characteristics of clustering and drug-susceptibility of Mycobacterium tuberculosisisolates in heilongjiang province, China. J Clin Microbiol 2011;10:2274-10.
7. Halima MS, Marleen MK, Nazir AI, Matsie M, Kamaldeen B, Shaheed VO, et al. Molecular characterization and second-line antituberculosis drug resistance patterns of multidrug-resistant Mycobacterium tuberculosis isolates from the northern region of South Africa. J Clin Microbiol 2012;50:2857-62.
8. Weiwei J, Zhiguang L, Rui H, Xiuqin Z, Fang D, Haiyan D, et al. A country-wide study of spoligotype and drug resistance characteristics of Mycobacterium tuberculosis isolates from children in China. Plos One 2013;10:e84315. doi: 10.1371/journal.pone.0084315. [Article in Press]
9. Van SD, Kremer K. Findings and ongoing research in the molecular epidemiology of tuberculosis. Kekkaku 2009;84:83-9.
10. Claudio UK, Silke F, David KS, John AC, Archer, Stefan N. Importance of the genetic diversity within the Mycobacterium tuberculosis complex for the development of novel antibiotics and diagnostic tests of drug resistance. Antimicrob Agents Chemother 2012;56:6080-7.
11. Rafia M, Shais J, Singh TP. The shikimate pathway: review of amino acid sequence, function and three-dimensional structures of the enzymes. Crit Rev Microbiol 2013;41:172-89.
12. Vered T, Gad G. New insights into the shikimate and aromatic amino acids biosynthesis pathways in plants. Molecular Plant 2010;3:956-72.
13. Hermann KM, Weaver LM. The shikimate pathway. Annu Rev Plant Physiol Plant Mol Biol 1999;50:473-503.
14. Ruben V, Igor C, Katarzyna R, Yuguo X, Lisa S, Geert G, et al. Caffeoyl shikimate esterase (CSE) is an enzyme in the lignin biosynthetic pathway in arabidopsis. Science 2013;341:1103-6.
15. Angkanang S, Therdsak P, Angkana C, Saranya P. Molecular characterization of amikacin, kanamycin and capreomycin resistance in M/XDR-TB strains isolated in Thailand. BMC Microbiol 2014;14:165.
16. Mehri H, Davood DS, Abbas AIF, Sedigheh J, Abdorrazagh H, Farideh S, et al. Spoligotyping and drug resistance patterns of Mycobacterium tuberculosis isolates from five provinces of Iran. Microbiol Open 2013;2:988-96.
17. Zhang Z, Liu M, Wang Y, Pang Y, Kam KM, Zhao Y. Molecular and phenotypic characterization of multidrug-resistant Mycobacterium tuberculosis isolates resistant to kanamycin, amikacin and capreomycin. Eur J Microbiol Infect Dis 2014;33:1959-66.
18. Saidemberg M, Passarelli AW, Rodrigues AV, Basso LA, Santos DS, Palma MS. Shikimate kinase (EC 126.96.36.199) from Mycobacterium tuberculosis: kinetics and structural dynamics of a potential molecular target for drug development. Curr Med Chem 2011;18:1299-310.
19. Carolina PV, Walter FAJ. Identification of new potential Mycobacterium tuberculosis shikimate kinase inhibitors through molecular docking simulations. J Mol Model 2012;18:755-64.
20. Manoj K, Shikha V, Sujata S, Alagiri S, Tej PS, Punit K. Structure-based in silico design of a high-affinity dipeptide inhibitor for novel protein drug target shikimate kinase of Mycobacterium tuberculosis. Chem Biol Drug Design 2010;76:277-84.
21. Yijun G, Ludmila R, Yue L, Yan W, Honggao Y, Shivendra S, et al. Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis. J Mol Biol 2002;319:779-89.
22. Tomioka H, Namba K. Development of antituberculous drugs: current status and future prospects. Kekkaku Tuberculosis 2006;81:753-74.
23. Denis VB. Shikimic acid: review of its analytical, isolation, and purification techniques from plant and microbial sources. J Chem Biol 2012;5:5-17.
24. Pereira JH, Oliveira JS, Canduri F, Dias MVB, Palma MS, Basso LA, et al. Structure of shikimate kinase from Mycobacterium tuberculosis reveals the binding of shikimic acid. Acta Crystallographica 2004;60:2310-9.
25. Pereira JH, Jose H, Vasconcelos IB, Oliveira JS, Caceres RA, Azevedo WF, et al. Shikimate kinase: a potential target for development of novel antitubercular agents. Current Drug Targets 2007;8:459-68.
26. Coracini JD, Azevedo WF. Shikimate kinase, a protein target for drug design. Curr Med Chem 2014;21:592-604.
27. Jose HP, Jaim SO, Fernanda C, Marcio VBD, Mario SP, Luiz AB, et al. Iinteraction of shikimic acid with shikimate kinase. Biochem Biophys Res Commun 2004;325:10-7.
28. Ducati RG, Basso LA, Santos DS. Mycobacterial shikimate pathway enzymes as targets for drug design. Curr Drug Targets 2007;8:423-35.