A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish
New antimicrobial agents are urgently needed to address the increasing emergence and dissemination of multidrug-resistant bacteria. In the study, a chemically synthesized truncated peptide containing 22-amino acids derived from a C-type lectin homolog SpCTL6 of <i>Scylla paramamosain</i>...
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MDPI AG
2022-12-01
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author | Yan-Chao Chen Wanlei Qiu Weibin Zhang Jingrong Zhang Roushi Chen Fangyi Chen Ke-Jian Wang |
author_facet | Yan-Chao Chen Wanlei Qiu Weibin Zhang Jingrong Zhang Roushi Chen Fangyi Chen Ke-Jian Wang |
author_sort | Yan-Chao Chen |
collection | DOAJ |
description | New antimicrobial agents are urgently needed to address the increasing emergence and dissemination of multidrug-resistant bacteria. In the study, a chemically synthesized truncated peptide containing 22-amino acids derived from a C-type lectin homolog SpCTL6 of <i>Scylla paramamosain</i> was screened and found to exhibit broad-spectrum antimicrobial activity, indicating that it is an antimicrobial peptide (AMP), named Sp-LECin. Sp-LECin possessed the basic characteristics of most cationic AMPs, such as positive charge (+4) and a relatively high hydrophobicity (45%). After treatment with Sp-LECin, the disruption of microbial membrane integrity and even leakage of cellular contents was observed by scanning electron microscopy (SEM). In addition, Sp-LECin could bind lipopolysaccharide (LPS), increase the outer and inner membrane permeability and induce reactive oxygen species (ROS) production, ultimately leading to the death of <i>Pseudomonas aeruginosa</i>. Furthermore, Sp-LECin exhibited potent anti-biofilm activity against <i>P. aeruginosa</i> during both biofilm formation and maturation. Notably, Sp-LECin had no obvious cytotoxicity and could greatly improve the survival of <i>P. aeruginosa</i>-infected zebrafish, by approximately 40% over the control group after 72 h of treatment. This study indicated that Sp-LECin is a promising antibacterial agent with the potential to be used against devastating global pathogen infections such as <i>P. aeruginosa.</i> |
first_indexed | 2024-03-11T09:59:34Z |
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issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-11T09:59:34Z |
publishDate | 2022-12-01 |
publisher | MDPI AG |
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series | International Journal of Molecular Sciences |
spelling | doaj.art-1d3302609dc04924a2fe1e7584701b902023-11-16T15:31:04ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-12-0124126710.3390/ijms24010267A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in ZebrafishYan-Chao Chen0Wanlei Qiu1Weibin Zhang2Jingrong Zhang3Roushi Chen4Fangyi Chen5Ke-Jian Wang6State Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaState Key Laboratory of Marine Environmental Science, College of Ocean & Earth Sciences, Xiamen University, Xiamen 361102, ChinaNew antimicrobial agents are urgently needed to address the increasing emergence and dissemination of multidrug-resistant bacteria. In the study, a chemically synthesized truncated peptide containing 22-amino acids derived from a C-type lectin homolog SpCTL6 of <i>Scylla paramamosain</i> was screened and found to exhibit broad-spectrum antimicrobial activity, indicating that it is an antimicrobial peptide (AMP), named Sp-LECin. Sp-LECin possessed the basic characteristics of most cationic AMPs, such as positive charge (+4) and a relatively high hydrophobicity (45%). After treatment with Sp-LECin, the disruption of microbial membrane integrity and even leakage of cellular contents was observed by scanning electron microscopy (SEM). In addition, Sp-LECin could bind lipopolysaccharide (LPS), increase the outer and inner membrane permeability and induce reactive oxygen species (ROS) production, ultimately leading to the death of <i>Pseudomonas aeruginosa</i>. Furthermore, Sp-LECin exhibited potent anti-biofilm activity against <i>P. aeruginosa</i> during both biofilm formation and maturation. Notably, Sp-LECin had no obvious cytotoxicity and could greatly improve the survival of <i>P. aeruginosa</i>-infected zebrafish, by approximately 40% over the control group after 72 h of treatment. This study indicated that Sp-LECin is a promising antibacterial agent with the potential to be used against devastating global pathogen infections such as <i>P. aeruginosa.</i>https://www.mdpi.com/1422-0067/24/1/267antimicrobial peptideSp-LECinmembrane permeability<i>Pseudomonas aeruginosa</i>antibacterial agent |
spellingShingle | Yan-Chao Chen Wanlei Qiu Weibin Zhang Jingrong Zhang Roushi Chen Fangyi Chen Ke-Jian Wang A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish International Journal of Molecular Sciences antimicrobial peptide Sp-LECin membrane permeability <i>Pseudomonas aeruginosa</i> antibacterial agent |
title | A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish |
title_full | A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish |
title_fullStr | A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish |
title_full_unstemmed | A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish |
title_short | A Novel Antimicrobial Peptide Sp-LECin with Broad-Spectrum Antimicrobial Activity and Anti-<i>Pseudomonas aeruginosa</i> Infection in Zebrafish |
title_sort | novel antimicrobial peptide sp lecin with broad spectrum antimicrobial activity and anti i pseudomonas aeruginosa i infection in zebrafish |
topic | antimicrobial peptide Sp-LECin membrane permeability <i>Pseudomonas aeruginosa</i> antibacterial agent |
url | https://www.mdpi.com/1422-0067/24/1/267 |
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