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Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential
BACKGROUND: Certain legume plants produce a plethora of AMP-like peptides in their symbiotic cells. The cationic subgroup of the nodule-specific cysteine-rich (NCR) peptides has potent antimicrobial activity against gram-negative and gram-positive bacteria as well as unicellular and filamentous fung...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4964015/ https://www.ncbi.nlm.nih.gov/pubmed/27465344 http://dx.doi.org/10.1186/s12941-016-0159-8 |
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author | Mikuláss, Kata R. Nagy, Krisztina Bogos, Balázs Szegletes, Zsolt Kovács, Etelka Farkas, Attila Váró, György Kondorosi, Éva Kereszt, Attila |
author_facet | Mikuláss, Kata R. Nagy, Krisztina Bogos, Balázs Szegletes, Zsolt Kovács, Etelka Farkas, Attila Váró, György Kondorosi, Éva Kereszt, Attila |
author_sort | Mikuláss, Kata R. |
collection | PubMed |
description | BACKGROUND: Certain legume plants produce a plethora of AMP-like peptides in their symbiotic cells. The cationic subgroup of the nodule-specific cysteine-rich (NCR) peptides has potent antimicrobial activity against gram-negative and gram-positive bacteria as well as unicellular and filamentous fungi. FINDINGS: It was shown by scanning and atomic force microscopies that the cationic peptides NCR335, NCR247 and Polymyxin B (PMB) affect differentially on the surfaces of Sinorhizobium meliloti bacteria. Similarly to PMB, both NCR peptides caused damages of the outer and inner membranes but at different extent and resulted in the loss of membrane potential that could be the primary reason of their antimicrobial activity. CONCLUSIONS: The primary reason for bacterial cell death upon treatment with cationic NCR peptides is the loss of membrane potential. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12941-016-0159-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4964015 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-49640152016-07-29 Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential Mikuláss, Kata R. Nagy, Krisztina Bogos, Balázs Szegletes, Zsolt Kovács, Etelka Farkas, Attila Váró, György Kondorosi, Éva Kereszt, Attila Ann Clin Microbiol Antimicrob Short Report BACKGROUND: Certain legume plants produce a plethora of AMP-like peptides in their symbiotic cells. The cationic subgroup of the nodule-specific cysteine-rich (NCR) peptides has potent antimicrobial activity against gram-negative and gram-positive bacteria as well as unicellular and filamentous fungi. FINDINGS: It was shown by scanning and atomic force microscopies that the cationic peptides NCR335, NCR247 and Polymyxin B (PMB) affect differentially on the surfaces of Sinorhizobium meliloti bacteria. Similarly to PMB, both NCR peptides caused damages of the outer and inner membranes but at different extent and resulted in the loss of membrane potential that could be the primary reason of their antimicrobial activity. CONCLUSIONS: The primary reason for bacterial cell death upon treatment with cationic NCR peptides is the loss of membrane potential. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12941-016-0159-8) contains supplementary material, which is available to authorized users. BioMed Central 2016-07-28 /pmc/articles/PMC4964015/ /pubmed/27465344 http://dx.doi.org/10.1186/s12941-016-0159-8 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Short Report Mikuláss, Kata R. Nagy, Krisztina Bogos, Balázs Szegletes, Zsolt Kovács, Etelka Farkas, Attila Váró, György Kondorosi, Éva Kereszt, Attila Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
title | Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
title_full | Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
title_fullStr | Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
title_full_unstemmed | Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
title_short | Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
title_sort | antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential |
topic | Short Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4964015/ https://www.ncbi.nlm.nih.gov/pubmed/27465344 http://dx.doi.org/10.1186/s12941-016-0159-8 |
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