In Silico Characterization of Glutathione-S-transferase from Genus Trichinella

Authors

  • Somnath Balbhim Waghmare Assistant Professor, Department of Zoology Nowrosjee Wadia College, Pune, Maharashtra 411001, India

DOI:

https://doi.org/10.48165/

Keywords:

Trichinella, Glutathione-S-transferase, Nematode, Physicochemical analysis, Structure prediction, Phylogeny

Abstract

Glutathione-S-transferase is a major  immunomodulator and belongs to the family of  multifunctional enzymes which involves in the  various detoxification processes in the  nematodes. There are various kinds of  membrane-bound glutathione-S-transferases are  present and involved in xenobiotic metabolism  processes. Glutathione-S-transferases have  shown promising properties of a potential target  molecule to control the population of Trichinella  species which is the causative agent of  trichinosis. In silico prediction of gene and  proteins is of great importance for structural and  functional characterization of genomic and  proteomic sequences. In the present  investigations, 07 sequences of Glutathione-S transferase of nematodes from the various  species of genus Trichinella were characterized.  In silco analysis of Glutathione-S-transferase  proteins like their amino acid compositions,  atomic composition, the extinction coefficient of  protein along with estimated half-life, instability  index of protein, aliphatic index and grand  average of hydropathicity were also analyzed.  Physicochemical properties, secondary and  tertiary structural details of proteins with their  relationship with each other will help researchers  to design a synthetic drug against Trichinellosis.  These results may provide theoretical grounds  for future studies of nematode vaccine  development. 

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References

CDC- centre for disease prevention and control. https://www.cdc.gov/ 2. Murrell, K. D., & Pozio, E. (2011). Worldwide Occurrence and Impact of Human Trichinellosis, 1986–2009. Emerging Infectious Diseases, 17(12), 2194-2202.

https://dx.doi.org/10.3201/eid1712.110896.

Wang ZQ, Cui J, Shen LJ. (2007). The epidemiology of animal trichinellosis in China. Vet J. 173, 391–398. doi: 10.1016/j.tvjl.2005.08.002

Cui J, Wang ZQ, Xu BL. (2011). The epidemiology of human trichinellosis in China during 2004–2009. Acta Trop. 118, 1–5. doi: 10.1016/j.actatropica. 2011.02.005

Cui J, Jiang P, Liu LN, Wang ZQ. (2013). Survey of Trichinella infections in domestic pigs from northern and eastern Henan, China. Vet Parasitol. 194, 133–135. doi: 10.1016/j.vetpar.2013.01.038.

Jiang P, Zhang X, Wang LA, Han LH, Yang M, Duan JY, et al. (2016). Survey of Trichinella infection from domestic pigs in the historical endemic areas of Henan province, central China. Parasitol Res. 115, 4707–4709. doi: 10.1007/s00436-016-5240-x

Yang J, Pan W, Sun X, Zhao X, Yuan G, Sun Q, et al. (2015). Immunoproteomic profile of Trichinella spiralis adult worm proteins recognized by early infection sera. Parasit Vectors. 8, 20. doi: 10.1186/s13071-015-0641-8.

Liu CY, Song YY, Ren HN, Sun GG, Liu RD, Jiang P, Long SR, Zhang X, Wang ZQ, Cui J. (2017). Cloning and expression of a Trichinella spiralis putative glutathione S-transferase and its elicited protective immunity against challenge infections. Parasit Vectors. 10(1), 448. doi: 10.1186/s13071-017-2384-1.

Boyer, T.D. (1989), Special article the glutathione Stransferases: An update. Hepatology, 9, 486-496. doi:10.1002/hep.1840090324.

Prashant VT, Uddhav SC, Madura SM, Vishal PD, Renuka RK. (2010). Secondary structure prediction and phylogenetic analysis of salt tolerant proteins. Global Journal of Molecular Sciences 5(1), 30-36.

Gill SC, von Hippel PH. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem, (182), 319-326.

Edelhoch H. (1967). Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, (6), 1948-1954.

Nielsen M, Lundegaard C, Worning P, Lauemoller SL, Lamberth K. (2003). Reliable prediction of T-cell epitopes using neural networks with novel sequence representations. Protein Sci. (12), 1007-1017.

Ciechanover A and Schwartz AL. (1989). How are substrates recognized by the ubiquitin mediated proteolytic system? Trends Biochem Sci, (14), 483-488.

Varshavsky A. (1997). The N-end rule pathway of protein degradation. Genes Cells, (2), 13- 28.

Guruprasad K, Reddy BVB, Pandit MW. (1990). Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng, (4), 155-161.

Ikai AJ. (1980). Thermostability and aliphatic index of globular proteins. J Biochem, (88) 1895- 1898.

Kyte J, Doolittle RF. (1982). A simple method for displaying the hydropathic character of a protein. J Mol Biol, (157), 105-132.

Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., Bairoch A. (2005). Protein Identification and Analysis Tools on the ExPASy Server;(In) John M. Walker (ed): The Proteomics Protocols Handbook, Humana Press 571-607

Bjellqvust B, Hughes GJ, Pasquali C, Paquet N, Ravier F, Sanchez JC, Frutiger S, Hochstrasser D. (1993). The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14(1), 1023-1031.

Umang M, Astha J, Aastha C, Neha A, Vibha R. (2012). Computational structural and functional characterization of protein family: Key for the hidden mystry. Journal of Pharmacy Research 5(7), 3643-3649.

Guruprasad K, Reddy B, Pandit MW. (1990). Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Engineering 4(2), 155-164.

Walker JM. (2005).The Proteomics Protocols Handbook: Humana Press, Chap. 52. 24. Kyte J, Doolittle RF. (1982). A simple method for displaying the hydropathic character of a protein. J Mol Biol, (157), 105-132.

Kumar S, Stecher G, Li M, Knyaz C, and Tamura K (2018) MEGA X: Molecular Evolutionary Genetics Analysis across computing platforms. Molecular Biology and Evolution 35, 1547- 1549.

Pradeep NV, Anupama, Vidyashree KG, Lakshmi P. (2012). In silico characterization of industrial important cellulases using computational tools. Advances in Life Science and Technology 4, 8-14.

Ojeiru FE, Kazuya T, Yuki H, Mohammed SM, Shunsuke M. (2010). Circular dichroism studies on C-terminal zinc finger domain of transcription factor GATA-2. Yonago Acta medica; 53, 25-28.

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Published

2020-07-12

Issue

Vol. 39 No. 2 (2020): Bulletin of Pure and Applied Sciences Zoology (Jul-Dec) 2020

Section

Research Paper

How to Cite

In Silico Characterization of Glutathione-S-transferase from Genus Trichinella . (2020). Bulletin of Pure & Applied Sciences- Zoology , 39(2), 261–271. https://doi.org/10.48165/