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Mol. Cells 2013; 35(2): 106-114

Published online February 21, 2013

https://doi.org/10.1007/s10059-013-2132-0

© The Korean Society for Molecular and Cellular Biology

Broad Activity against Porcine Bacterial Pathogens Displayed by Two Insect Antimicrobial Peptides Moricin and Cecropin B

Han Hu, Chunmei Wang, Xiaozhen Guo, Wentao Li, Yang Wang, and Qigai He

State Key Laboratory of Agricultural Microbiology, Division of Animal Infectious Disease, Huazhong Agricultural University, Wuhan, Hubei, China

Received: May 4, 2012; Revised: November 18, 2012; Accepted: November 20, 2012

Abstract

In response to infection, insects produce a variety of antimicrobial peptides (AMPs) to kill the invading patho-gens. 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 ?g/ml, while cecropin B mainly showed antimicrobial activity against the Gram-negative strains with MICs ranging from 0.5 to 16 ?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.

Keywords antimicrobial peptide, cecropin B, Haemophilus parasuis SH 0165, moricin, transmission electron microscopy

Article

Research Article

Mol. Cells 2013; 35(2): 106-114

Published online February 28, 2013 https://doi.org/10.1007/s10059-013-2132-0

Copyright © The Korean Society for Molecular and Cellular Biology.

Broad Activity against Porcine Bacterial Pathogens Displayed by Two Insect Antimicrobial Peptides Moricin and Cecropin B

Han Hu, Chunmei Wang, Xiaozhen Guo, Wentao Li, Yang Wang, and Qigai He

State Key Laboratory of Agricultural Microbiology, Division of Animal Infectious Disease, Huazhong Agricultural University, Wuhan, Hubei, China

Received: May 4, 2012; Revised: November 18, 2012; Accepted: November 20, 2012

Abstract

In response to infection, insects produce a variety of antimicrobial peptides (AMPs) to kill the invading patho-gens. 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 ?g/ml, while cecropin B mainly showed antimicrobial activity against the Gram-negative strains with MICs ranging from 0.5 to 16 ?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.

Keywords: antimicrobial peptide, cecropin B, Haemophilus parasuis SH 0165, moricin, transmission electron microscopy

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

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