Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> 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...
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| Format: | Article |
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MDPI AG
2019-04-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/11/4/206 |
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| author | Teja Shidore Quan Zeng Lindsay R. Triplett |
| author_facet | Teja Shidore Quan Zeng Lindsay R. Triplett |
| author_sort | Teja Shidore |
| collection | DOAJ |
| 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 <i>Erwinia amylovora</i>. Hidden Markov Model (HMM) and BLAST-based programs were used to predict the identity and distribution of putative TA systems among sequenced genomes of <i>E. amylovora</i> and other plant-associated <i>Erwinia</i> spp. Of six conserved TA systems tested for function from <i>E. amylovora</i>, three (CbtA/CbeA, ParE/RHH and Doc/PhD) were validated as functional. CbtA was toxic to <i>E. amylovora</i>, but not to <i>Escherichia coli</i>. While the <i>E. coli</i> homolog of CbtA elicits the formation of lemon-shaped cells upon overexpression and targets cytoskeletal proteins FtsZ and MreB, <i>E. amylovora</i> CbtA led to cell elongation and did not interact with these cytoskeletal proteins. Phylogenetic analysis revealed that <i>E. amylovora</i> CbtA belongs to a distinct clade from the CbtA of pathogenic <i>E. coli</i>. This study expands the repertoire of experimentally validated TA systems in plant pathogenic bacteria, and suggests that the <i>E. amylovora</i> homolog of CbtA is functionally distinct from that of <i>E. coli</i>. |
| first_indexed | 2024-04-14T00:57:47Z |
| format | Article |
| id | doaj.art-ca7d568e64ae4c82b57b3c5d5050f83e |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-04-14T00:57:47Z |
| publishDate | 2019-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-ca7d568e64ae4c82b57b3c5d5050f83e2022-12-22T02:21:33ZengMDPI AGToxins2072-66512019-04-0111420610.3390/toxins11040206toxins11040206Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional SpecificityTeja Shidore0Quan Zeng1Lindsay R. Triplett2Department of Plant Pathology and Ecology, the Connecticut Agricultural Experiment Station, New Haven, CT 06511, USADepartment of Plant Pathology and Ecology, the Connecticut Agricultural Experiment Station, New Haven, CT 06511, USADepartment of Plant Pathology and Ecology, the Connecticut Agricultural Experiment Station, New Haven, CT 06511, USAToxin–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 <i>Erwinia amylovora</i>. Hidden Markov Model (HMM) and BLAST-based programs were used to predict the identity and distribution of putative TA systems among sequenced genomes of <i>E. amylovora</i> and other plant-associated <i>Erwinia</i> spp. Of six conserved TA systems tested for function from <i>E. amylovora</i>, three (CbtA/CbeA, ParE/RHH and Doc/PhD) were validated as functional. CbtA was toxic to <i>E. amylovora</i>, but not to <i>Escherichia coli</i>. While the <i>E. coli</i> homolog of CbtA elicits the formation of lemon-shaped cells upon overexpression and targets cytoskeletal proteins FtsZ and MreB, <i>E. amylovora</i> CbtA led to cell elongation and did not interact with these cytoskeletal proteins. Phylogenetic analysis revealed that <i>E. amylovora</i> CbtA belongs to a distinct clade from the CbtA of pathogenic <i>E. coli</i>. This study expands the repertoire of experimentally validated TA systems in plant pathogenic bacteria, and suggests that the <i>E. amylovora</i> homolog of CbtA is functionally distinct from that of <i>E. coli</i>.https://www.mdpi.com/2072-6651/11/4/206toxin–antitoxin system<i>Erwinia amylovora</i>YeeVCbtAParEDoccell elongation |
| spellingShingle | Teja Shidore Quan Zeng Lindsay R. Triplett Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional Specificity Toxins toxin–antitoxin system <i>Erwinia amylovora</i> YeeV CbtA ParE Doc cell elongation |
| title | Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional Specificity |
| title_full | Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional Specificity |
| title_fullStr | Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional Specificity |
| title_full_unstemmed | Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional Specificity |
| title_short | Survey of Toxin–Antitoxin Systems in <i>Erwinia amylovora</i> Reveals Insights into Diversity and Functional Specificity |
| title_sort | survey of toxin antitoxin systems in i erwinia amylovora i reveals insights into diversity and functional specificity |
| topic | toxin–antitoxin system <i>Erwinia amylovora</i> YeeV CbtA ParE Doc cell elongation |
| url | https://www.mdpi.com/2072-6651/11/4/206 |
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