ACTA AGRICULTURAE BOREALI-SINICA ›› 2017, Vol. 32 ›› Issue (6): 134-138. doi: 10.7668/hbnxb.2017.06.020

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Domain Reconstruction and Lysis Activity of Phage Lysin

ZHANG Hui1, ZHOU Yan1, BAO Hongduo1, YANG Zhenquan3, ZHU Ruyi3, ZHOU Chenlu3, ZHANG Lili1, WANG Ran1,2   

  1. 1. Jiangsu Key Laboratory of Food Quality and Safety-State Key Laboratory Cultivation Base of MOST, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China;
    2. Jiangsu Collaborative Innovation Center of Meat Production and Processing, Quality and Safety Control, Nanjing 210095, China;
    3. College of Food Science and Engineering, Yangzhou University, Yangzhou 225009, China
  • Received:2017-08-09 Published:2017-12-28

Abstract: In order to get wide host-range phage lysin,the cell-binding domains of Staphylococcus aureus Ply187 CHAP and SH3b (lysin K) were synthesized based on the sequence,according to the specificity and structure of the phage lysin.The cell-binding domain was amplified from Listeria monocytogenes phage lysin LysZ5.All the domain were reconstructed and the lysis function were analyzed.From the SDS-PAGE,reconstruction lysin Ply187KS-Z5,containing two cell-binding domains,showed the specific protein band at 58 kDa.Clear zone observed after Lysin Ply187KS-Z5 added on the plate of both S.aureus and L.monocytogenes. Lysin Ply187-KS could reduce number of S. aureus to 2.16 log in 1 hour,but the reconstruction lysin Ply187KS-Z5 was able to inhibit the growth of both S.aureus and L.monocytogenes.Therefore,domain reconstruction should be a new approach to develop wide-host-range lysin.

Key words: Lysin, Staphylococcus aureus, Listeria monocytogenes

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Cite this article

ZHANG Hui, ZHOU Yan, BAO Hongduo, YANG Zhenquan, ZHU Ruyi, ZHOU Chenlu, ZHANG Lili, WANG Ran. Domain Reconstruction and Lysis Activity of Phage Lysin[J]. ACTA AGRICULTURAE BOREALI-SINICA, 2017, 32(6): 134-138. doi: 10.7668/hbnxb.2017.06.020.

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