In-Silico Analysis and Structural Prediction of Catalase Protein in Emu (Dromaius novaehollandiae) Through Homology Modeling

International Journal of Veterinary Science
© 2016 by SSRG - IJVS Journal
Volume 2 Issue 3
Year of Publication : 2016
Authors : Thashi Bharadwaj, Rexon G, Tony Grace
How to Cite?

Thashi Bharadwaj, Rexon G, Tony Grace, "In-Silico Analysis and Structural Prediction of Catalase Protein in Emu (Dromaius novaehollandiae) Through Homology Modeling," SSRG International Journal of Veterinary Science, vol. 2,  no. 3, pp. 1-5, 2016. Crossref,


Applicability of immune defense proteins from non-mammalian species can be beneficial in devising novel disease management strategies to overcome the concerns of resistance to current antibiotic therapeutics. Understanding the proteins involved in antimicrobial defense against infections can also aid in developing new generation of antibiotics. Evolution of new emerging diseases and atypical host diseases, it is imperative that we have in depth understanding of the presence and evolution of different proteins involved in defense mechanisms. Here we report the identification and structural dynamics of Catalase enzyme in Emu, a member of the oldest class of order of living birds.


Structure prediction, Homology modeling, Catalase, Computational analysis, Immune defense.


[1] DaSilva, E. and Iaccarino, M., Emerging diseases: a global threat. Biotechnology Advances, 17(4), pp.363-384, 1999.
[2] Bloom, David E., and David Canning. Epidemics and, 2006.
[3] Akira, S., Uematsu, S. and Takeuchi, O., Pathogen recognition and innate immunity.Cell, 124(4), pp.783-801, 2006.
[4] Mogensen, T.H., Pathogen recognition and inflammatory signaling in innate immune defenses. Clinical microbiology reviews, 22(2), pp.240-273, 2009.
[5] Thompson, M.R., Kaminski, J.J., Kurt-Jones, E.A. and Fitzgerald, K.A., Pattern recognition receptors and the innate immune response to viral infection.Viruses, 3(6), pp.920-940, 2011
[6] Aderem, A. and Ulevitch, R.J., Toll-like receptors in the induction of the innate immune response. Nature, 406(6797), pp.782-787 2000.
[7] Bonizzi, G. and Karin, M., The two NF-κB activation pathways and their role in innate and adaptive immunity. Trends in immunology, 25(6), pp.280-288, 2004.
[8] de Geus, E.D., Tefsen, B., van Haarlem, D.A., van Eden, W., van Die, I. and Vervelde, L., Glycans from avian influenza virus are recognized by chicken dendritic cells and are targets for the humoral immune response in chicken. Molecular immunology, 56(4), pp.452-462, 2013.
[9] . Staines, K., Young, J.R. and Butter, C., Expression of chicken DEC205 reflects the unique structure and function of the avian immune system. PloS one, 8(1), p.e51799, 2013.
[10] Gong, Q., Qu, N., Niu, M., Qin, C., Cheng, M., Sun, X. and Zhang, A., Immune responses and protective efficacy of a novel DNA vaccine encoding outer membrane protein of avian Pasteurellamultocida. Veterinary immunology and immunopathology, 152(3), pp.317-324, 2013.
[11] Min, W., Kim, W.H., Lillehoj, E.P. and Lillehoj, H.S., Recent progress in host immunity to avian coccidiosis: IL-17 family cytokines as sentinels of the intestinal mucosa. Developmental & Comparative Immunology, 41(3), pp.418-428, 2013.
[12] Tim Downing, Paul Cormican, Cliona O'Farrelly, Daniel G Bradley and Andrew T Lloyd, Evidence of the adaptive evolution of immune genes in chicken BMC Research Notes, 2:254 doi:10.1186/1756-0500-2-254, 2009.
[13] Hammond, E.L., Lymbery, A.J., Martin, G.B., Groth, D. and Wetherall, J.D., Microsatellite analysis of genetic diversity in wild and farmed emus (Dromaius novaehollandiae). Journal of Heredity, 93(5), pp.376-380, 2002.
[14] Roff, D.A., The evolution of flightlessness: is history important?.Evolutionary Ecology, 8(6), pp.639-657, 1994.
[15] Maina, J.N. and King, A.S., The lung of the emu, Dromaiusnovaehollandiae: a microscopic and morphometric study. Journal of anatomy, 163, p.67, 1989.
[16] Herd, R.M. and Dawson, T.J., Fiber digestion in the emu, Dromaiusnovaehollandiae, a large bird with a simple gut and high rates of passage. Physiological Zoology, pp.70-84, 1984.
[17] Baker, A.J., Daugherty, C.H., Colbourne, R. and McLennan, J.L., Flightless brown kiwis of New Zealand possess extremely subdivided population structure and cryptic species like small mammals. Proceedings of the National Academy of Sciences, 92(18), pp.8254-8258, 1995.
[18] Jeengar, M.K., Kumar, P.S., Thummuri, D., Shrivastava, S., Guntuku, L., Sistla, R. and Naidu, V.G.M., Review on emu products for use as complementary and alternative medicine. Nutrition, 31(1), pp.21-27, 2015.
[19] Warale, R.H., Chauhan, H.D., Parmar, D., Kulkarni, R.C., Srivastava, A.K., Makwana, R.B., Pawar, M.M. and Bhagwat, S.R., Emu Farming: An Alternative to Indian Poultry, 2014.
[20] Bennett, D.C., Code, W.E., Godin, D.V. and Cheng, K.M., Comparison of the antioxidant properties of emu oil with other avian oils. Animal Production Science, 48(10), pp.1345-1350, 2008.
[21] Guan, L.M., Zhao, J. and Scandalios, J.G., Cis‐elements and trans‐factors that regulate expression of the maize Cat1 antioxidant gene in response to ABA and osmotic stress: H2O2 is the likely intermediary signaling molecule for the response. The Plant Journal, 22(2), pp.87-95, 2000.
[22] Su, Y., Guo, J., Ling, H., Chen, S., Wang, S., Xu, L., Allan, A.C. and Que, Y., Isolation of a novel peroxisomal catalase gene from sugarcane, which is responsive to biotic and abiotic stresses. PloS one, 9(1), p.e84426, 2014.
[23] Untergasser, A., Cutcutache, I., Koressaar, T., Ye, J., Faircloth, B.C., Remm, M. and Rozen, S.G.,. Primer3—new capabilities and interfaces. Nucleic acids research, 40(15), pp.e115-e115, 2012.
[24] Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I., Appel, R.D. and Bairoch, A., ExPASy: the proteomics server for in-
depth protein knowledge and analysis. Nucleic acids research, 31(13), pp.3784-3788, 2003.
[25] Krogh, A., Larsson, B., Von Heijne, G. and Sonnhammer, E.L., Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. Journal of molecular biology, 305(3), pp.567-580, 2001.
[26] Geourjon, C. and Deleage, G., SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Computer applications in the biosciences: CABIOS, 11(6), pp.681-684, 1995.
[27] Kelley, L.A. and Sternberg, M.J., Protein structure prediction on the Web: a case study using the Phyre server. Nature protocols, 4(3), pp.363-371, 2009.
[28] Sayle, R. and Bissell, A., RasMol: A program for fast, realistic rendering of molecular structures with shadows. In Proceedings of the 10th Eurographics UK (Vol. 92, pp. 7-9), 1992.
[29] Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M., PROCHECK: a program to check the stereochemical quality of protein structures. Journal of applied crystallography, 26(2), pp.283-291, 1993.