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BioMed Research International
Volume 2017 (2017), Article ID 9390803, 10 pages
https://doi.org/10.1155/2017/9390803
Research Article

Molecular Cloning, Bioinformatic Analysis, and Expression of Bombyx mori Lebocin 5 Gene Related to Beauveria bassiana Infection

1School of Biotechnology and Sericultural Research Institute, Jiangsu University of Science and Technology, Zhenjiang 212018, China
2Nursing School, Zhenjiang College, Zhenjiang 212003, China

Correspondence should be addressed to Xijie Guo; moc.621@eijixoug

Received 4 October 2016; Revised 21 November 2016; Accepted 19 December 2016; Published 17 January 2017

Academic Editor: Qiang Gao

Copyright © 2017 Dingding Lü et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. C.-X. Hou, G.-X. Qin, T. Liu et al., “Differentially expressed genes in the cuticle and hemolymph of the silkworm, Bombyx mori, injected with the fungus Beauveria bassiana,” Journal of Insect Science, vol. 13, article 138, 14 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  2. X. Chen, C. Huang, L. He, S. Zhang, and Z. Li, “Molecular tracing of white muscardine in the silkworm, Bombyx mori (Linn.) II. Silkworm white muscardine is not caused by artificial release or natural epizootic of Beauveria bassiana in China,” Journal of Invertebrate Pathology, vol. 125, pp. 16–22, 2015. View at Publisher · View at Google Scholar · View at Scopus
  3. E. A. Steinhaus, “Microbial diseases of insects,” Annual review of microbiology, vol. 11, pp. 165–182, 1957. View at Publisher · View at Google Scholar · View at Scopus
  4. D. Lu, M. Pava-Ripoll, Z. Li, and C. Wang, “Insecticidal evaluation of Beauveria bassiana engineered to express a scorpion neurotoxin and a cuticle degrading protease,” Applied Microbiology and Biotechnology, vol. 81, no. 3, pp. 515–522, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. M. D. Lavine and M. R. Strand, “Insect hemocytes and their role in immunity,” Insect Biochemistry and Molecular Biology, vol. 32, no. 10, pp. 1295–1309, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. N. A. Ratcliffe, “Invertebrate immunity—a primer for the non-specialist,” Immunology Letters, vol. 10, no. 5, pp. 253–270, 1985. View at Publisher · View at Google Scholar · View at Scopus
  7. P. Bulet, R. Stöcklin, and L. Menin, “Anti-microbial peptides: from invertebrates to vertebrates,” Immunological Reviews, vol. 198, no. 1, pp. 169–184, 2004. View at Publisher · View at Google Scholar · View at Scopus
  8. C. Luna, X. Wang, Y. Huang, J. Zhang, and L. Zheng, “Characterization of four Toll related genes during development and immune responses in Anopheles gambiae,” Insect Biochemistry and Molecular Biology, vol. 32, no. 9, pp. 1171–1179, 2002. View at Publisher · View at Google Scholar · View at Scopus
  9. P. Bulet, C. Hetru, J.-L. Dimarcq, and D. Hoffmann, “Antimicrobial peptides in insects; structure and function,” Developmental and Comparative Immunology, vol. 23, no. 4-5, pp. 329–344, 1999. View at Publisher · View at Google Scholar · View at Scopus
  10. B. Lemaitre and J. Hoffmann, “The host defense of Drosophila melanogaster,” Annual Review of Immunology, vol. 25, no. 1, pp. 697–743, 2007. View at Publisher · View at Google Scholar · View at Scopus
  11. C. Hetru and J. A. Hoffmann, “NF-kappaB in the immune response of Drosophila,” Cold Spring Harbor perspectives in biology, vol. 1, no. 6, p. a000232, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. T. Cheng, P. Zhao, C. Liu et al., “Structures, regulatory regions, and inductive expression patterns of antimicrobial peptide genes in the silkworm Bombyx mori,” Genomics, vol. 87, no. 3, pp. 356–365, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. Y. Yamano, M. Matsumoto, K. Sasahara, E. Sakamoto, and I. Morishima, “Structure of genes for cecropin A and an inducible nuclear protein that binds to the promoter region of the genes from the silkworm, Bombyx mori,” Bioscience, Biotechnology and Biochemistry, vol. 62, no. 2, pp. 237–241, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. K. Taniai, K. Kadono-Okuda, Y. Kato et al., “Structure of two cecropin B-encoding genes and bacteria-inducible DNA-binding proteins which bind to the 5′-upstream regulatory region in the silkworm, Bombyx mori,” Gene, vol. 163, no. 2, pp. 215–219, 1995. View at Publisher · View at Google Scholar · View at Scopus
  15. J. Yang, S. Furukawa, A. Sagisaka et al., “cDNA cloning and gene expression of cecropin D, an antibacterial protein in the silkworm, Bombyx mori,” Comparative Biochemistry and Physiology—B Biochemistry and Molecular Biology, vol. 122, no. 4, pp. 409–414, 1999. View at Publisher · View at Google Scholar · View at Scopus
  16. S. Hara and M. Yamakawa, “Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori,” Journal of Biological Chemistry, vol. 270, no. 50, pp. 29923–29927, 1995. View at Publisher · View at Google Scholar · View at Scopus
  17. S. Kawaoka, S. Katsuma, T. Daimon et al., “Functional analysis of four gloverin-like genes in the silkworm, Bombyx mori,” Archives of Insect Biochemistry and Physiology, vol. 67, no. 2, pp. 87–96, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. M. Sugiyama, H. Kuniyoshi, E. Kotani et al., “Characterization of a Bombyx mori cDNA encoding a novel member of the attacin family of insect antibacterial proteins,” Insect Biochemistry and Molecular Biology, vol. 25, no. 3, pp. 385–392, 1995. View at Publisher · View at Google Scholar · View at Scopus
  19. S. H. Kim, B. S. Park, E. Y. Yun et al., “Cloning and expression of a novel gene encoding a new antibacterial peptide from silkworm, Bombyx mori,” Biochemical and Biophysical Research Communications, vol. 246, no. 2, pp. 388–392, 1998. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Chowdhury, K. Taniai, S. Hara et al., “cDNA cloning and gene expression of lebocin, a novel member of antibacterial peptides from the silkworm, Bombyx mori,” Biochemical and Biophysical Research Communications, vol. 214, no. 1, pp. 271–278, 1995. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Furukawa, K. Taniai, J. Ishibashi, S. Hara, T. Shono, and M. Yamakawa, “A novel member of lebocin gene family from the silkworm, Bombyx mori,” Biochemical and Biophysical Research Communications, vol. 238, no. 3, pp. 769–774, 1997. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Hara and M. Yamakawa, “A novel antibacterial peptide family isolated from the silkworm, Bombyx mori,” Biochemical Journal, vol. 310, no. 2, pp. 651–656, 1995. View at Publisher · View at Google Scholar · View at Scopus
  23. G. Liu, D. Kang, and H. Steiner, “Trichoplusia ni lebocin, an inducible immune gene with a downstream insertion element,” Biochemical and Biophysical Research Communications, vol. 269, no. 3, pp. 803–807, 2000. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. Bao, Y. Yamano, and I. Morishima, “A novel lebocin-like gene from eri-silkworm, Samia cynthia ricini, that does not encode the antibacterial peptide lebocin,” Comparative Biochemistry and Physiology—B Biochemistry and Molecular Biology, vol. 140, no. 1, pp. 127–131, 2005. View at Publisher · View at Google Scholar · View at Scopus
  25. M. D. Lavine, G. Chen, and M. R. Strand, “Immune challenge differentially affects transcript abundance of three antimicrobial peptides in hemocytes from the moth Pseudoplusia includens,” Insect Biochemistry and Molecular Biology, vol. 35, no. 12, pp. 1335–1346, 2005. View at Publisher · View at Google Scholar · View at Scopus
  26. S. Rayaprolu, Y. Wang, M. R. Kanost, S. Hartson, and H. Jiang, “Functional analysis of four processing products from multiple precursors encoded by a lebocin-related gene from Manduca sexta,” Developmental and Comparative Immunology, vol. 34, no. 6, pp. 638–647, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. X.-J. Rao, X.-X. Xu, and X.-Q. Yu, “Functional analysis of two lebocin-related proteins from Manduca sexta,” Insect Biochemistry and Molecular Biology, vol. 42, no. 4, pp. 231–239, 2012. View at Publisher · View at Google Scholar · View at Scopus
  28. K. Casteels-Josson, W. Zhang, T. Capaci, P. Casteels, and P. Tempst, “Acute transcriptional response of the honeybee peptide-antibiotics gene repertoire and required post-translational conversion of the precursor structures,” Journal of Biological Chemistry, vol. 269, no. 46, pp. 28569–28575, 1994. View at Google Scholar · View at Scopus
  29. S. Y. Hara and M. Yamakawa, “Cooperative antibacterial relationship between lebocin and cecropin D, antibacterial peptides isolated from the silkworm, Bombyx mori (Lepidoptera: Bombycidae),” Applied Entomology and Zoology, vol. 30, no. 4, pp. 606–608, 1995. View at Google Scholar
  30. C. Hou, G. Qin, T. Liu et al., “Transcriptome analysis of silkworm, Bombyx mori, during early response to Beauveria bassiana challenges,” PLoS ONE, vol. 9, no. 3, Article ID e91189, 2014. View at Publisher · View at Google Scholar · View at Scopus
  31. D. Lu, T. Geng, C. Hou, Y. Huang, G. Qin, and X. Guo, “Bombyx mori cecropin A has a high antifungal activity to entomopathogenic fungus Beauveria bassiana,” Gene, vol. 583, no. 1, pp. 29–35, 2016. View at Publisher · View at Google Scholar · View at Scopus
  32. S. Kumar, G. Stecher, and K. Tamura, “MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets,” Molecular Biology and Evolution, vol. 33, no. 7, pp. 1870–1874, 2016. View at Publisher · View at Google Scholar
  33. N. Saitou and M. Nei, “The neighbor-joining method: a new method for reconstructing phylogenetic trees,” Molecular Biology and Evolution, vol. 4, no. 4, pp. 406–425, 1987. View at Google Scholar · View at Scopus
  34. K. J. Livak and T. D. Schmittgen, “Analysis of relative gene expression data using real-time quantitative PCR and the 2-ΔΔCT method,” Methods, vol. 25, no. 4, pp. 402–408, 2001. View at Publisher · View at Google Scholar · View at Scopus
  35. I. B. H. Wilson, Y. Gavel, and G. Von Heijne, “Amino acid distributions around O-linked glycosylation sites,” Biochemical Journal, vol. 275, no. 2, pp. 529–534, 1991. View at Publisher · View at Google Scholar · View at Scopus
  36. L. Devi, “Consensus sequence for processing of peptide precursors at monobasic sites,” FEBS Letters, vol. 280, no. 2, pp. 189–194, 1991. View at Publisher · View at Google Scholar · View at Scopus
  37. J. A. Veenstra, “Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors,” Archives of Insect Biochemistry and Physiology, vol. 43, no. 2, pp. 49–63, 2000. View at Publisher · View at Google Scholar · View at Scopus
  38. Y. Yamano, M. Matsumoto, K. Inoue, T. Kawabata, and I. Morishima, “Cloning of cdnas for cecropins a and b, and expression of the genes in the silkworm, bombyx mori,” Bioscience, Biotechnology and Biochemistry, vol. 58, no. 8, pp. 1476–1478, 1994. View at Publisher · View at Google Scholar · View at Scopus