The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance
ABSTRACT Enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the last step of the elongation cycle in the synthesis of bacterial fatty acids. The Enterococcus faecalis genome contains two genes annotated as enoyl-ACP reductases, a FabI-type enoyl-ACP reductase and a FabK-type enoyl-ACP reduct...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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American Society for Microbiology
2013-11-01
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| Series: | mBio |
| Online Access: | https://journals.asm.org/doi/10.1128/mBio.00613-13 |
| _version_ | 1818434275809165312 |
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| author | Lei Zhu Hongkai Bi Jincheng Ma Zhe Hu Wenbin Zhang John E. Cronan Haihong Wang |
| author_facet | Lei Zhu Hongkai Bi Jincheng Ma Zhe Hu Wenbin Zhang John E. Cronan Haihong Wang |
| author_sort | Lei Zhu |
| collection | DOAJ |
| description | ABSTRACT Enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the last step of the elongation cycle in the synthesis of bacterial fatty acids. The Enterococcus faecalis genome contains two genes annotated as enoyl-ACP reductases, a FabI-type enoyl-ACP reductase and a FabK-type enoyl-ACP reductase. We report that expression of either of the two proteins restores growth of an Escherichia coli fabI temperature-sensitive mutant strain under nonpermissive conditions. In vitro assays demonstrated that both proteins support fatty acid synthesis and are active with substrates of all fatty acid chain lengths. Although expression of E. faecalis fabK confers to E. coli high levels of resistance to the antimicrobial triclosan, deletion of fabK from the E. faecalis genome showed that FabK does not play a detectable role in the inherent triclosan resistance of E. faecalis. Indeed, FabK seems to play only a minor role in modulating fatty acid composition. Strains carrying a deletion of fabK grow normally without fatty acid supplementation, whereas fabI deletion mutants make only traces of fatty acids and are unsaturated fatty acid auxotrophs. IMPORTANCE The finding that exogenous fatty acids support growth of E. faecalis strains defective in fatty acid synthesis indicates that inhibitors of fatty acid synthesis are ineffective in countering E. faecalis infections because host serum fatty acids support growth of the bacterium. |
| first_indexed | 2024-12-14T16:34:24Z |
| format | Article |
| id | doaj.art-2130a83e9344462b9b0107df7b1a480f |
| institution | Directory Open Access Journal |
| issn | 2150-7511 |
| language | English |
| last_indexed | 2024-12-14T16:34:24Z |
| publishDate | 2013-11-01 |
| publisher | American Society for Microbiology |
| record_format | Article |
| series | mBio |
| spelling | doaj.art-2130a83e9344462b9b0107df7b1a480f2022-12-21T22:54:31ZengAmerican Society for MicrobiologymBio2150-75112013-11-014510.1128/mBio.00613-13The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan ResistanceLei Zhu0Hongkai Bi1Jincheng Ma2Zhe Hu3Wenbin Zhang4John E. Cronan5Haihong Wang6Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong, ChinaDepartment of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USAGuangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong, ChinaGuangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong, ChinaGuangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong, ChinaDepartment of Microbiology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USAGuangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong, ChinaABSTRACT Enoyl-acyl carrier protein (enoyl-ACP) reductase catalyzes the last step of the elongation cycle in the synthesis of bacterial fatty acids. The Enterococcus faecalis genome contains two genes annotated as enoyl-ACP reductases, a FabI-type enoyl-ACP reductase and a FabK-type enoyl-ACP reductase. We report that expression of either of the two proteins restores growth of an Escherichia coli fabI temperature-sensitive mutant strain under nonpermissive conditions. In vitro assays demonstrated that both proteins support fatty acid synthesis and are active with substrates of all fatty acid chain lengths. Although expression of E. faecalis fabK confers to E. coli high levels of resistance to the antimicrobial triclosan, deletion of fabK from the E. faecalis genome showed that FabK does not play a detectable role in the inherent triclosan resistance of E. faecalis. Indeed, FabK seems to play only a minor role in modulating fatty acid composition. Strains carrying a deletion of fabK grow normally without fatty acid supplementation, whereas fabI deletion mutants make only traces of fatty acids and are unsaturated fatty acid auxotrophs. IMPORTANCE The finding that exogenous fatty acids support growth of E. faecalis strains defective in fatty acid synthesis indicates that inhibitors of fatty acid synthesis are ineffective in countering E. faecalis infections because host serum fatty acids support growth of the bacterium.https://journals.asm.org/doi/10.1128/mBio.00613-13 |
| spellingShingle | Lei Zhu Hongkai Bi Jincheng Ma Zhe Hu Wenbin Zhang John E. Cronan Haihong Wang The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance mBio |
| title | The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance |
| title_full | The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance |
| title_fullStr | The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance |
| title_full_unstemmed | The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance |
| title_short | The Two Functional Enoyl-Acyl Carrier Protein Reductases of <named-content content-type="genus-species">Enterococcus faecalis</named-content> Do Not Mediate Triclosan Resistance |
| title_sort | two functional enoyl acyl carrier protein reductases of named content content type genus species enterococcus faecalis named content do not mediate triclosan resistance |
| url | https://journals.asm.org/doi/10.1128/mBio.00613-13 |
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