Antibacterial Mechanism of Gloverin2 from Silkworm, Bombyx mori

International Journal of Molecular Sciences

Yunshi Zhang¹  Zhan Wang¹  Pengchao Guo¹  Qingyou Xia¹  Ping Zhao¹  Shan Jiang¹  Huawei Liu¹  Qian Wang¹  Wenzhe Han¹ 

[1] State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400715, China;

关键词: silkworm;    antibacterial peptide;    Gloverin;    gram-negative bacteria;    antibacterial mechanism;   

DOI  :  10.3390/ijms19082275

来源: DOAJ

【 摘 要 】

Gloverin is one of the glycine-rich antimicrobial peptide exclusively found in Lepidoptera insects. It is generally activated through the innate immune system in insects. In this study, recombinant Gloverin2 from Bombyx mori (BmGlv2) was synthesized using a prokaryotic expression system. Circular dichroism spectroscopy showed that the recombinant BmGlv2 has random coil structure, which is relatively stable at the temperatures ranging from 15 to 82.5 °C. Antimicrobial activity analysis revealed that BmGlv2 significantly inhibited the growth of gram-negative bacteria, Escherichia coli JM109 and Pseudomonas putida, by disrupting cell integrity. Western blotting and immunofluorescence analyses suggested that BmGlv2 absorbed on the cell surface after incubation, which might be the first step in the antibacterial process. Our results also proved that the cell wall component lipopolysaccharides (LPS) induce a conformational change in BmGlv2 from a random coil to α-helix. Subsequently, α-helical BmGlv2 would recruit more BmGlv2 and form higher aggregation state. Collectively, these findings expand our understanding of antibacterial mechanism of BmGlv2.

【 授权许可】

Unknown