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Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity
Toxin–antitoxin (TA) systems are diverse genetic modules with demonstrated roles in plasmid stability, stress management, biofilm formation and antibiotic persistence. However, relatively little is known about their functional significance in plant pathogens. In this study we characterize type II an...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6521040/ https://www.ncbi.nlm.nih.gov/pubmed/30959879 http://dx.doi.org/10.3390/toxins11040206 |
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author | Shidore, Teja Zeng, Quan Triplett, Lindsay R. |
author_facet | Shidore, Teja Zeng, Quan Triplett, Lindsay R. |
author_sort | Shidore, Teja |
collection | PubMed |
description | Toxin–antitoxin (TA) systems are diverse genetic modules with demonstrated roles in plasmid stability, stress management, biofilm formation and antibiotic persistence. However, relatively little is known about their functional significance in plant pathogens. In this study we characterize type II and IV TA systems in the economically important plant pathogen Erwinia amylovora. Hidden Markov Model (HMM) and BLAST-based programs were used to predict the identity and distribution of putative TA systems among sequenced genomes of E. amylovora and other plant-associated Erwinia spp. Of six conserved TA systems tested for function from E. amylovora, three (CbtA/CbeA, ParE/RHH and Doc/PhD) were validated as functional. CbtA was toxic to E. amylovora, but not to Escherichia coli. While the E. coli homolog of CbtA elicits the formation of lemon-shaped cells upon overexpression and targets cytoskeletal proteins FtsZ and MreB, E. amylovora CbtA led to cell elongation and did not interact with these cytoskeletal proteins. Phylogenetic analysis revealed that E. amylovora CbtA belongs to a distinct clade from the CbtA of pathogenic E. coli. This study expands the repertoire of experimentally validated TA systems in plant pathogenic bacteria, and suggests that the E. amylovora homolog of CbtA is functionally distinct from that of E. coli. |
format | Online Article Text |
id | pubmed-6521040 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-65210402019-05-31 Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity Shidore, Teja Zeng, Quan Triplett, Lindsay R. Toxins (Basel) Article Toxin–antitoxin (TA) systems are diverse genetic modules with demonstrated roles in plasmid stability, stress management, biofilm formation and antibiotic persistence. However, relatively little is known about their functional significance in plant pathogens. In this study we characterize type II and IV TA systems in the economically important plant pathogen Erwinia amylovora. Hidden Markov Model (HMM) and BLAST-based programs were used to predict the identity and distribution of putative TA systems among sequenced genomes of E. amylovora and other plant-associated Erwinia spp. Of six conserved TA systems tested for function from E. amylovora, three (CbtA/CbeA, ParE/RHH and Doc/PhD) were validated as functional. CbtA was toxic to E. amylovora, but not to Escherichia coli. While the E. coli homolog of CbtA elicits the formation of lemon-shaped cells upon overexpression and targets cytoskeletal proteins FtsZ and MreB, E. amylovora CbtA led to cell elongation and did not interact with these cytoskeletal proteins. Phylogenetic analysis revealed that E. amylovora CbtA belongs to a distinct clade from the CbtA of pathogenic E. coli. This study expands the repertoire of experimentally validated TA systems in plant pathogenic bacteria, and suggests that the E. amylovora homolog of CbtA is functionally distinct from that of E. coli. MDPI 2019-04-06 /pmc/articles/PMC6521040/ /pubmed/30959879 http://dx.doi.org/10.3390/toxins11040206 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Shidore, Teja Zeng, Quan Triplett, Lindsay R. Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity |
title | Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity |
title_full | Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity |
title_fullStr | Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity |
title_full_unstemmed | Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity |
title_short | Survey of Toxin–Antitoxin Systems in Erwinia amylovora Reveals Insights into Diversity and Functional Specificity |
title_sort | survey of toxin–antitoxin systems in erwinia amylovora reveals insights into diversity and functional specificity |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6521040/ https://www.ncbi.nlm.nih.gov/pubmed/30959879 http://dx.doi.org/10.3390/toxins11040206 |
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