›› 2013, Vol. 40 ›› Issue (6): 19-26.

Previous Articles     Next Articles

Fusion Expression of Recombinant Cathelicidins Genes in Escherichia coli and Study on its Antibacterial Activity against Staphylococcus aureus in vivo

WU Jing1,2, LIANG Yong-li3, LI Yu-feng1, MA Xiu-li1, JIANG Yi-fei1   

  1. 1. Poultry Institute of Shandong Academy of Agricultural Sciences, Jinan 250023, China;
    2. School of Life Sciences, Shandong University, Jinan 250100, China;
    3. Shandong Experimental Animal Center, Jinan 250002, China
  • Received:2012-11-30 Online:2013-06-20 Published:2013-06-20

Abstract: Cathelicidins comprised a family of antimicrobial peptides sharing a highly conserved cathelin domain, they played a critical role in the innate immune system of chicken. In this study, the constructed positive clones of Rosetta(DE3)/pET30-CathL1S, pET30-CathL2S and pET30-CathL3S were cultured and induced to express target protein by addition of 1.0 mmol/L IPTG in LB. SDS-PAGE and Western blotting analysis demonstrated that Cathelicidins genes were expressed in the form of fusion protein, except for CathL-1 mature peptide, and the apparent molecular weight of expression products were 7, 8, 7.5 ku, respectively. The recombinant Cathelicidins were able to kill both gram negative bacteria and gram positive bacteria by the means of agar well diffusion assay (AWDA), especially for the antibiotic-resistant strains. Young chickens as animal model were used to test antibacterial activity and the result indicated that 5 mg/kg recombinant CathL-1 could completely protect the chicken from infection of Staphylococcus aureus(ATCC 6538). Low dose of CathL-1 could apparently increase weight of chickens.

Key words: antimicrobial peptide; Cathelicidins; fusion expression; purification; antibacterial activity; Staphylococcus aureus

CLC Number: