INFORMATION CHANGE THE WORLD

International Journal of Information Engineering and Electronic Business(IJIEEB)

ISSN: 2074-9023 (Print), ISSN: 2074-9031 (Online)

Published By: MECS Press

IJIEEB Vol.3, No.1, Feb. 2011

Bioinformatics Analysis and Characteristics of the giant panda Interferon-alpha

Full Text (PDF, 1570KB), PP.45-54


Views:54   Downloads:1

Author(s)

YueYi,Zhiwen Xu

Index Terms

Ailuropoda melanoleuca,interferon alpha,clone,sequence analysis,Structure analysis

Abstract

In this report, the amino acid sequence of giant panda interferon-α (gpIFN-α) was determined and compared with 15 corresponding IFN-α sequences. Phylogenetic analysis showed that the 15 interferons fell into two large groups. The giant panda and ferret branched and were most closely related to fox and dog and evolved into a distinct phylogenetic lineage from that of eukaryotic mammalians which evolved into another lineage. After analyzing the encoded amino acid sequence of the gpIFN-α using bioinformatics, the results revealed that in the full amino acid sequence, there were no transmembrane domain, one N-glycosylation sites, eight O-glycosylation sites and nine antigenic determinants. Secondary structure analyzed showed that the Alpha helix, Extended strand, Beta turn and Random coil each occupied 60.37%(99aa), 4.88%(8aa), 9.76%, 25%(41aa) respectively. In conclusion, our results will give the opportunity to investigate more in detail function study in giant panda and add to studies on the evolution of the IFN system in vertebrates and avian more generally.

Cite This Paper

YueYi,Zhiwen Xu,"Bioinformatics Analysis and Characteristics of the giant panda Interferon-alpha", IJIEEB, vol.3, no.1, pp.45-54, 2011.

Reference

[1]C. Samuel, “Antiviral actions of interferons,” Clinical Microbiology Reviews, vol. 14, no. 4, pp. 778, 2001.

[2]H. Nguyen, J. Hiscott, and P. Pitha, “The growing family of interferon regulatory factors,” Cytokine & growth factor reviews, vol. 8, no. 4, pp. 293-312, 1997.

[3]M. Colonna, A. Krug, and M. Cella, “Interferon-producing cells: on the front line in immune responses against pathogens,” Current opinion in immunology, vol. 14, no. 3, pp. 373-379, 2002.

[4]W. Stewart, and J. Vil ek, The interferon system: Springer-Verlag New York, 1979.

[5]P. Familletti, R. McCandliss, and S. Pestka, “Production of high levels of human leukocyte interferon from a continuous human myeloblast cell culture,” Antimicrobial agents and chemotherapy, vol. 20, no. 1, pp. 5, 1981.

[6]W. Feng, and G. Li, “The saving of giant panda,” Published by Sichuan Science and Technology Publishing Company, pp. 113-129, 2000.

[7]X. Tan, Y. Tang, Y. Yang et al., “Gene cloning, sequencing, expression and biological activity of giant panda (Ailuropoda melanoleuca) interferon-[alpha],” Molecular immunology, vol. 44, no. 11, pp. 3061-3069, 2007.

[8]L. Xu, B. Zeng, R. Peng et al., “Molecular cloning and sequence analysis of the gene encoding interleukin-6 of the giant panda (Ailuropoda melanoleuca),” Journal of Natural History, vol. 42, no. 39, pp. 2585-2591, 2008.

[9]W. Feng, R. Wang, S. Zhong et al., “Analysis on the dead cause of the anatomical carcass of giant panda (Ailuropoda melanoleuca),” A study on breeding and diseases of the giant panda, pp. 244-248.

[10]H. Tjalsma, A. Bolhuis, J. Jongbloed et al., “Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome,” Microbiology and Molecular Biology Reviews, vol. 64, no. 3, pp. 515, 2000.

[11]G. von Heijne, “The signal peptide,” Journal of Membrane Biology, vol. 115, no. 3, pp. 195-201, 1990.

[12]R. Wonderling, T. Powell, S. Baldwin et al., “Cloning, expression, purification, and biological activity of five feline type I interferons,” Veterinary immunology and immunopathology, vol. 89, no. 1-2, pp. 13-27, 2002.

[13]R. Devos, H. Cheroutre, Y. Taya et al., “Molecular cloning of human immune interferon cDNA and its expression in eukaryotic cells,” Nucleic acids research, vol. 10, no. 8, pp. 2487, 1982.

[14]E. Weerapana, and B. Imperiali, “Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems,” Glycobiology, vol. 16, no. 6, pp. 91R, 2006.

[15]R. Huby, R. Dearman, and I. Kimber, “Why are some proteins allergens?,” Toxicological Sciences, vol. 55, no. 2, pp. 235, 2000.

[16]S. Zhang, A. Cheng, M. Wang et al., "Molecular Cloning and Nucleotide Sequence Analysis of the Newly Identified UL53 Gene of Duck Enteritis Virus." pp. 1-6.

[17]S. Kumar, K. Tamura, and M. Nei, “MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment,” Briefings in bioinformatics, vol. 5, no. 2, pp. 150, 2004.