Broad activity against porcine bacterial pathogens displayed by two insect antimicrobial peptides moricin and cecropin B

被引:49
作者
Hu, Han [1 ]
Wang, Chunmei [1 ]
Guo, Xiaozhen [1 ]
Li, Wentao [1 ]
Wang, Yang [1 ]
He, Qigai [1 ]
机构
[1] Huazhong Agr Univ, Div Anim Infect Dis, State Key Lab Agr Microbiol, Wuhan, Hubei, Peoples R China
基金
中国博士后科学基金;
关键词
antimicrobial peptide; cecropin B; Haemophilus parasuis SH 0165; moricin; transmission electron microscopy; ANTIBACTERIAL PEPTIDE; SILKWORM; IMMUNITY; TRANSMISSION; PROTEGRIN-1; PREVALENCE; EXPRESSION; RESISTANCE; CLONING; P1;
D O I
10.1007/s10059-013-2132-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In response to infection, insects produce a variety of antimicrobial peptides (AMPs) to kill the invading pathogens. To study their physicochemical properties and bioactivities for clinical and commercial use in the porcine industry, we chemically synthesized the mature peptides Bombyx mori moricin and Hyalophora cecropia cecropin B. In this paper, we described the antimicrobial activity of the two AMPs. Moricin exhibited antimicrobial activity on eight strains tested with minimal inhibitory concentration values (MICs) ranging between 8 and 128 mu g/ml, while cecropin B mainly showed antimicrobial activity against the Gramnegative strains with MICs ranging from 0.5 to 16 mu g/ml. Compared to the potent antimicrobial activity these two AMPs displayed against most of the bacterial pathogens tested, they exhibited limited hemolytic activity against porcine red blood cells. The activities of moricin and cecropin B against Haemophilus parasuis SH 0165 were studied in further detail. Transmission electron microscopy (TEM) of moricin and cecropin B treated H. parasuis SH 0165 indicated extensive damage to the membranes of the bacteria. Insights into the probable mechanism utilized by moricin and cecropin B to eliminate pathogens are also presented. The observations from this study are important for the future application of AMPs in the porcine industry.
引用
收藏
页码:106 / 114
页数:9
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