Cargando…
Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea‐derived AMP–Leg2, termed “functionalized chickpea‐derived Leg2 antimicrobial p...
Autores principales: | , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951321/ https://www.ncbi.nlm.nih.gov/pubmed/36563134 http://dx.doi.org/10.1002/advs.202205301 |
_version_ | 1784893363173982208 |
---|---|
author | He, Qiao Yang, Zhehao Zou, Zhipeng Qian, Mengyan Wang, Xiaolei Zhang, Xinhui Yin, Zhongping Wang, Jinhai Ye, Xingqian Liu, Donghong Guo, Mingming |
author_facet | He, Qiao Yang, Zhehao Zou, Zhipeng Qian, Mengyan Wang, Xiaolei Zhang, Xinhui Yin, Zhongping Wang, Jinhai Ye, Xingqian Liu, Donghong Guo, Mingming |
author_sort | He, Qiao |
collection | PubMed |
description | The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea‐derived AMP–Leg2, termed “functionalized chickpea‐derived Leg2 antimicrobial peptides” (FCLAPs). Among the FCLAPs, KTA and KTR show superior antibacterial efficacy against the foodborne pathogen Escherichia coli (E. coli) O157:H7 (with MICs in the range of 2.5–4.7 µmol L(−1)) and demonstrate satisfactory feasibility in alleviating E. coli O157:H7‐induced intestinal infection. Additionally, the low cytotoxicity along with insusceptibility to antimicrobial resistance increases the potential of FCLAPs as appealing antimicrobials. Combining the multi‐omics profiling andpeptide‐membrane interaction assays, a unique dual‐targeting mode of action is characterized. To specify the antibacterial mechanism, microscopical observations, membrane‐related physicochemical properties studies, and mass spectrometry assays are further performed. Data indicate that KTA and KTR induce membrane damage by initially targeting the lipopolysaccharide (LPS), thus promoting the peptides to traverse the outer membrane. Subsequently, the peptides intercalate into the peptidoglycan (PGN) layer, blocking its synthesis, and causing a collapse of membrane structure. These findings altogether imply the great potential of KTA and KTR as promising antibacterial candidates in combating the growing threat of E. coli O157:H7. |
format | Online Article Text |
id | pubmed-9951321 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-99513212023-02-25 Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides He, Qiao Yang, Zhehao Zou, Zhipeng Qian, Mengyan Wang, Xiaolei Zhang, Xinhui Yin, Zhongping Wang, Jinhai Ye, Xingqian Liu, Donghong Guo, Mingming Adv Sci (Weinh) Research Articles The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea‐derived AMP–Leg2, termed “functionalized chickpea‐derived Leg2 antimicrobial peptides” (FCLAPs). Among the FCLAPs, KTA and KTR show superior antibacterial efficacy against the foodborne pathogen Escherichia coli (E. coli) O157:H7 (with MICs in the range of 2.5–4.7 µmol L(−1)) and demonstrate satisfactory feasibility in alleviating E. coli O157:H7‐induced intestinal infection. Additionally, the low cytotoxicity along with insusceptibility to antimicrobial resistance increases the potential of FCLAPs as appealing antimicrobials. Combining the multi‐omics profiling andpeptide‐membrane interaction assays, a unique dual‐targeting mode of action is characterized. To specify the antibacterial mechanism, microscopical observations, membrane‐related physicochemical properties studies, and mass spectrometry assays are further performed. Data indicate that KTA and KTR induce membrane damage by initially targeting the lipopolysaccharide (LPS), thus promoting the peptides to traverse the outer membrane. Subsequently, the peptides intercalate into the peptidoglycan (PGN) layer, blocking its synthesis, and causing a collapse of membrane structure. These findings altogether imply the great potential of KTA and KTR as promising antibacterial candidates in combating the growing threat of E. coli O157:H7. John Wiley and Sons Inc. 2022-12-23 /pmc/articles/PMC9951321/ /pubmed/36563134 http://dx.doi.org/10.1002/advs.202205301 Text en © 2022 The Authors. Advanced Science published by Wiley‐VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles He, Qiao Yang, Zhehao Zou, Zhipeng Qian, Mengyan Wang, Xiaolei Zhang, Xinhui Yin, Zhongping Wang, Jinhai Ye, Xingqian Liu, Donghong Guo, Mingming Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides |
title | Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides |
title_full | Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides |
title_fullStr | Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides |
title_full_unstemmed | Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides |
title_short | Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides |
title_sort | combating escherichia coli o157:h7 with functionalized chickpea‐derived antimicrobial peptides |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951321/ https://www.ncbi.nlm.nih.gov/pubmed/36563134 http://dx.doi.org/10.1002/advs.202205301 |
work_keys_str_mv | AT heqiao combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT yangzhehao combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT zouzhipeng combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT qianmengyan combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT wangxiaolei combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT zhangxinhui combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT yinzhongping combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT wangjinhai combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT yexingqian combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT liudonghong combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides AT guomingming combatingescherichiacolio157h7withfunctionalizedchickpeaderivedantimicrobialpeptides |