›› 2011, Vol. 38 ›› Issue (5): 101-104.

• 生物技术 • Previous Articles     Next Articles

Recombination and Fusion Expression of Porcine Defensin Gene pBD-2 in E.coli

XU Hai-tao1, MA Li-bao2, HE Qi-gai1, LIAO Bing-lin2, REN Fen-fen3   

  1. 1. National Key Laboratory of Agricultural Microbiology,Huazhong Agricultural University,Wuhan 430070,China;2. College of Animal Science and Technology,Huazhong Agricultural University,Wuhan 430070,China;3. College of Animal Science and Technology,Hunan Agricultural University,Chansha 410128,China
  • Received:2010-10-27 Revised:1900-01-01 Online:2011-05-20 Published:2011-05-20

Abstract: Defensin is an important antimicrobial peptide produced in the course of animals’ defense against pathogens,which has a broad antibacterial spectrum and plays an important role in innate immunity. Based on cDNA sequence of porcine defensin β-defensin-2 gene reported in this study,three gene fragment (1,2,3) were synthesized in this experiment. Fragment 1,2 and fragment 2,3 had respectively 15 bases for complementary pair. pBD-2 gene was produced by PCR amplifing,and pBD-2 was inserted into expression vector (pGEX-KG) and recombinant vector transformed into E.coli,where recombinant vector produced fusion protein successfully.The expression of pBD-2 gene lays a foundation in research on antimicrobial activities of defensin.

Key words: porcine defensin β-defensin-2; prokaryotic expression; fusion protein

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