Site‐directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B from Botrytis cinerea highlights different roles in enzyme activity and inhibitor binding
Carboxamide fungicides target succinate dehydrogenase (SDH). Recent field monitoring studies have identified Botrytis cinerea isolates resistant to one or several SDH inhibitors (SDHIs) with amino acid substitutions in the SDH B subunit. We confirmed, by site‐directed mutagenesis of the sdhB gene, t...
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| Veröffentlicht in: | Environmental microbiology 2014-07, Vol.16 (7), p.2253-2266 |
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| creator | Lalève, Anaïs Gamet, Stéphanie Walker, Anne‐Sophie Debieu, Danièle Toquin, Valérie Fillinger, Sabine |
| description | Carboxamide fungicides target succinate dehydrogenase (SDH). Recent field monitoring studies have identified Botrytis cinerea isolates resistant to one or several SDH inhibitors (SDHIs) with amino acid substitutions in the SDH B subunit. We confirmed, by site‐directed mutagenesis of the sdhB gene, that each of the mutations identified in field strains conferred resistance to boscalid in B. cinerea, and in some cases cross‐resistance to other SDHIs (fluopyram, carboxin). Enzyme inhibition studies showed that the studied modifications (SdhB_P225T/L/F, N230I, H272Y/R/L) affected the inhibition of SDH activity by SDHIs, directly contributing to resistance. Our results confirm the importance of H272, P225 and N230 for carboxamide binding. Modifications of P225 and N230 conferred resistance to the four carboxamides tested (boscalid, fluopyram, carboxin, bixafen). Modifications of H272 had differential effects on the susceptibility of SDH to SDHIs. SdhBᴴ²⁷²ᴸ, affected susceptibility to all SDHIs, SdhBᴴ²⁷²ᴿ conferred resistance to all SDHIs tested except fluopyram, and SdhBᴴ²⁷²Y conferred fluopyram hypersensitivity. Affinity‐binding studies with radiolabelled fluopyram revealed strong correlations among the affinity of SDHIs for SDH, SDH inhibition and in vivo growth inhibition in the wild type. The sdhBᴴ²⁷²Y mutation did not affect SDH and respiration activities, whereas all the other mutations affected respiration by decreasing SDH activity. |
| doi_str_mv | 10.1111/1462-2920.12282 |
| format | Article |
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Recent field monitoring studies have identified Botrytis cinerea isolates resistant to one or several SDH inhibitors (SDHIs) with amino acid substitutions in the SDH B subunit. We confirmed, by site‐directed mutagenesis of the sdhB gene, that each of the mutations identified in field strains conferred resistance to boscalid in B. cinerea, and in some cases cross‐resistance to other SDHIs (fluopyram, carboxin). Enzyme inhibition studies showed that the studied modifications (SdhB_P225T/L/F, N230I, H272Y/R/L) affected the inhibition of SDH activity by SDHIs, directly contributing to resistance. Our results confirm the importance of H272, P225 and N230 for carboxamide binding. Modifications of P225 and N230 conferred resistance to the four carboxamides tested (boscalid, fluopyram, carboxin, bixafen). Modifications of H272 had differential effects on the susceptibility of SDH to SDHIs. SdhBᴴ²⁷²ᴸ, affected susceptibility to all SDHIs, SdhBᴴ²⁷²ᴿ conferred resistance to all SDHIs tested except fluopyram, and SdhBᴴ²⁷²Y conferred fluopyram hypersensitivity. Affinity‐binding studies with radiolabelled fluopyram revealed strong correlations among the affinity of SDHIs for SDH, SDH inhibition and in vivo growth inhibition in the wild type. The sdhBᴴ²⁷²Y mutation did not affect SDH and respiration activities, whereas all the other mutations affected respiration by decreasing SDH activity.</description><identifier>ISSN: 1462-2912</identifier><identifier>EISSN: 1462-2920</identifier><identifier>DOI: 10.1111/1462-2920.12282</identifier><identifier>PMID: 24119086</identifier><language>eng</language><publisher>Oxford: Blackwell Science</publisher><subject>Amino Acid Substitution ; Animal, plant and microbial ecology ; Benzamides ; Biological and medical sciences ; Biphenyl Compounds ; boscalid ; Botrytis - drug effects ; Botrytis - enzymology ; Botrytis - genetics ; Botrytis cinerea ; Carboxin ; Dehydrogenases ; Drug Resistance, Fungal - genetics ; enzyme activity ; enzyme inhibition ; Enzyme Inhibitors ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Fungicides, Industrial ; General aspects ; genes ; growth retardation ; hypersensitivity ; Life Sciences ; Microbial ecology ; Microbiology ; Miscellaneous ; monitoring ; Mutagenesis ; Mutagenesis, Site-Directed ; Mutation ; Mycology ; Niacinamide - analogs & derivatives ; Protein Binding ; Protein Subunits - chemistry ; Protein Subunits - genetics ; Protein Subunits - metabolism ; Pyridines ; Structure-Activity Relationship ; succinate dehydrogenase ; Succinate Dehydrogenase - chemistry ; Succinate Dehydrogenase - genetics ; Succinate Dehydrogenase - metabolism</subject><ispartof>Environmental microbiology, 2014-07, Vol.16 (7), p.2253-2266</ispartof><rights>2013 Society for Applied Microbiology and John Wiley & Sons Ltd</rights><rights>2015 INIST-CNRS</rights><rights>2013 Society for Applied Microbiology and John Wiley & Sons Ltd.</rights><rights>Copyright © 2014 Society for Applied Microbiology and John Wiley & Sons Ltd</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0003-4683-0803 ; 0000-0002-1246-246X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2F1462-2920.12282$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1462-2920.12282$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=28750307$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24119086$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-02638457$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Lalève, Anaïs</creatorcontrib><creatorcontrib>Gamet, Stéphanie</creatorcontrib><creatorcontrib>Walker, Anne‐Sophie</creatorcontrib><creatorcontrib>Debieu, Danièle</creatorcontrib><creatorcontrib>Toquin, Valérie</creatorcontrib><creatorcontrib>Fillinger, Sabine</creatorcontrib><title>Site‐directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B from Botrytis cinerea highlights different roles in enzyme activity and inhibitor binding</title><title>Environmental microbiology</title><addtitle>Environ Microbiol</addtitle><description>Carboxamide fungicides target succinate dehydrogenase (SDH). Recent field monitoring studies have identified Botrytis cinerea isolates resistant to one or several SDH inhibitors (SDHIs) with amino acid substitutions in the SDH B subunit. We confirmed, by site‐directed mutagenesis of the sdhB gene, that each of the mutations identified in field strains conferred resistance to boscalid in B. cinerea, and in some cases cross‐resistance to other SDHIs (fluopyram, carboxin). Enzyme inhibition studies showed that the studied modifications (SdhB_P225T/L/F, N230I, H272Y/R/L) affected the inhibition of SDH activity by SDHIs, directly contributing to resistance. Our results confirm the importance of H272, P225 and N230 for carboxamide binding. Modifications of P225 and N230 conferred resistance to the four carboxamides tested (boscalid, fluopyram, carboxin, bixafen). Modifications of H272 had differential effects on the susceptibility of SDH to SDHIs. SdhBᴴ²⁷²ᴸ, affected susceptibility to all SDHIs, SdhBᴴ²⁷²ᴿ conferred resistance to all SDHIs tested except fluopyram, and SdhBᴴ²⁷²Y conferred fluopyram hypersensitivity. Affinity‐binding studies with radiolabelled fluopyram revealed strong correlations among the affinity of SDHIs for SDH, SDH inhibition and in vivo growth inhibition in the wild type. The sdhBᴴ²⁷²Y mutation did not affect SDH and respiration activities, whereas all the other mutations affected respiration by decreasing SDH activity.</description><subject>Amino Acid Substitution</subject><subject>Animal, plant and microbial ecology</subject><subject>Benzamides</subject><subject>Biological and medical sciences</subject><subject>Biphenyl Compounds</subject><subject>boscalid</subject><subject>Botrytis - drug effects</subject><subject>Botrytis - enzymology</subject><subject>Botrytis - genetics</subject><subject>Botrytis cinerea</subject><subject>Carboxin</subject><subject>Dehydrogenases</subject><subject>Drug Resistance, Fungal - genetics</subject><subject>enzyme activity</subject><subject>enzyme inhibition</subject><subject>Enzyme Inhibitors</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungicides, Industrial</subject><subject>General aspects</subject><subject>genes</subject><subject>growth retardation</subject><subject>hypersensitivity</subject><subject>Life Sciences</subject><subject>Microbial ecology</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>monitoring</subject><subject>Mutagenesis</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Mycology</subject><subject>Niacinamide - analogs & derivatives</subject><subject>Protein Binding</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>Pyridines</subject><subject>Structure-Activity Relationship</subject><subject>succinate dehydrogenase</subject><subject>Succinate Dehydrogenase - chemistry</subject><subject>Succinate Dehydrogenase - genetics</subject><subject>Succinate Dehydrogenase - metabolism</subject><issn>1462-2912</issn><issn>1462-2920</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNktFuFCEUhidGY2v12jslMSaauArMMMNctk3tNm6rSa1NvCEMnNmhzjAVmOp45SP4RD6MTyKzu66JV5IQ4PD9hwP8SfKQ4Jcktlcky-mMljQuKeX0VrK7jdzezgndSe55f4UxKdIC3012aEZIiXm-m_w8NwF-ff-hjQMVQKNuCHIJFrzxqK9RaAC9o5S9QGc0xUhajea0oMhFQA-wYvyglLEyANLQjNr1US89xHg1WBPQAapd36GDPrgxxLQRBgcSNWbZtLEHj7Sp6xizAbm-jVmNRWC_jR0gqYK5MWFcHW1sYyoTeocqY7Wxy_vJnVq2Hh5sxr3k4vXR-8P5bPH2-ORwfzGrs6KgM8lxrjgoxVOKGS8ZUwUhUOWYcpZypfIMGJSZZpXmoLOMpSojukxzCTqvZbqXPF_nbWQrrp3ppBtFL42Y7y_EFMM0T3nGihsS2Wdr9tr1n-MTBdEZr6BtpYV-8IIwRnLCKc7-A81ozmKRPKJP_kGv-sHZeOmJIiUreTpRjzbUUHWgt6X--fAIPN0A0ivZ1k5aZfxfjhcMp7iIHFtzX0wL43afYDH5TkzOEpPLxMp34uj0ZDWJutlaZ3yAr1uddJ9EHs3HxOXZsWDkzell8eFcfIz84zVfy17IpYu1XJxTTLJoVsYKlqe_AYi14ek</recordid><startdate>201407</startdate><enddate>201407</enddate><creator>Lalève, Anaïs</creator><creator>Gamet, Stéphanie</creator><creator>Walker, Anne‐Sophie</creator><creator>Debieu, Danièle</creator><creator>Toquin, Valérie</creator><creator>Fillinger, Sabine</creator><general>Blackwell Science</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Wiley Subscription Services, Inc</general><general>Society for Applied Microbiology and Wiley-Blackwell</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QH</scope><scope>7QL</scope><scope>7ST</scope><scope>7T7</scope><scope>7TN</scope><scope>7U9</scope><scope>7UA</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H94</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>SOI</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-4683-0803</orcidid><orcidid>https://orcid.org/0000-0002-1246-246X</orcidid></search><sort><creationdate>201407</creationdate><title>Site‐directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B from Botrytis cinerea highlights different roles in enzyme activity and inhibitor binding</title><author>Lalève, Anaïs ; Gamet, Stéphanie ; Walker, Anne‐Sophie ; Debieu, Danièle ; Toquin, Valérie ; Fillinger, Sabine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f4772-a806c8ecc832058955c711eb6028538cc64e5e94d5bd8ed4453c41d936aed6fa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Substitution</topic><topic>Animal, plant and microbial ecology</topic><topic>Benzamides</topic><topic>Biological and medical sciences</topic><topic>Biphenyl Compounds</topic><topic>boscalid</topic><topic>Botrytis - drug effects</topic><topic>Botrytis - enzymology</topic><topic>Botrytis - genetics</topic><topic>Botrytis cinerea</topic><topic>Carboxin</topic><topic>Dehydrogenases</topic><topic>Drug Resistance, Fungal - genetics</topic><topic>enzyme activity</topic><topic>enzyme inhibition</topic><topic>Enzyme Inhibitors</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungicides, Industrial</topic><topic>General aspects</topic><topic>genes</topic><topic>growth retardation</topic><topic>hypersensitivity</topic><topic>Life Sciences</topic><topic>Microbial ecology</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>monitoring</topic><topic>Mutagenesis</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Mycology</topic><topic>Niacinamide - analogs & derivatives</topic><topic>Protein Binding</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>Pyridines</topic><topic>Structure-Activity Relationship</topic><topic>succinate dehydrogenase</topic><topic>Succinate Dehydrogenase - chemistry</topic><topic>Succinate Dehydrogenase - genetics</topic><topic>Succinate Dehydrogenase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lalève, Anaïs</creatorcontrib><creatorcontrib>Gamet, Stéphanie</creatorcontrib><creatorcontrib>Walker, Anne‐Sophie</creatorcontrib><creatorcontrib>Debieu, Danièle</creatorcontrib><creatorcontrib>Toquin, Valérie</creatorcontrib><creatorcontrib>Fillinger, Sabine</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Aqualine</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Oceanic Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Water Resources Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Environmental microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lalève, Anaïs</au><au>Gamet, Stéphanie</au><au>Walker, Anne‐Sophie</au><au>Debieu, Danièle</au><au>Toquin, Valérie</au><au>Fillinger, Sabine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Site‐directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B from Botrytis cinerea highlights different roles in enzyme activity and inhibitor binding</atitle><jtitle>Environmental microbiology</jtitle><addtitle>Environ Microbiol</addtitle><date>2014-07</date><risdate>2014</risdate><volume>16</volume><issue>7</issue><spage>2253</spage><epage>2266</epage><pages>2253-2266</pages><issn>1462-2912</issn><eissn>1462-2920</eissn><abstract>Carboxamide fungicides target succinate dehydrogenase (SDH). Recent field monitoring studies have identified Botrytis cinerea isolates resistant to one or several SDH inhibitors (SDHIs) with amino acid substitutions in the SDH B subunit. We confirmed, by site‐directed mutagenesis of the sdhB gene, that each of the mutations identified in field strains conferred resistance to boscalid in B. cinerea, and in some cases cross‐resistance to other SDHIs (fluopyram, carboxin). Enzyme inhibition studies showed that the studied modifications (SdhB_P225T/L/F, N230I, H272Y/R/L) affected the inhibition of SDH activity by SDHIs, directly contributing to resistance. Our results confirm the importance of H272, P225 and N230 for carboxamide binding. Modifications of P225 and N230 conferred resistance to the four carboxamides tested (boscalid, fluopyram, carboxin, bixafen). Modifications of H272 had differential effects on the susceptibility of SDH to SDHIs. SdhBᴴ²⁷²ᴸ, affected susceptibility to all SDHIs, SdhBᴴ²⁷²ᴿ conferred resistance to all SDHIs tested except fluopyram, and SdhBᴴ²⁷²Y conferred fluopyram hypersensitivity. Affinity‐binding studies with radiolabelled fluopyram revealed strong correlations among the affinity of SDHIs for SDH, SDH inhibition and in vivo growth inhibition in the wild type. The sdhBᴴ²⁷²Y mutation did not affect SDH and respiration activities, whereas all the other mutations affected respiration by decreasing SDH activity.</abstract><cop>Oxford</cop><pub>Blackwell Science</pub><pmid>24119086</pmid><doi>10.1111/1462-2920.12282</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0003-4683-0803</orcidid><orcidid>https://orcid.org/0000-0002-1246-246X</orcidid></addata></record> |
| fulltext | fulltext |
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| ispartof | Environmental microbiology, 2014-07, Vol.16 (7), p.2253-2266 |
| issn | 1462-2912 1462-2920 |
| language | eng |
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| source | Wiley Online Library - AutoHoldings Journals; MEDLINE |
| subjects | Amino Acid Substitution Animal, plant and microbial ecology Benzamides Biological and medical sciences Biphenyl Compounds boscalid Botrytis - drug effects Botrytis - enzymology Botrytis - genetics Botrytis cinerea Carboxin Dehydrogenases Drug Resistance, Fungal - genetics enzyme activity enzyme inhibition Enzyme Inhibitors Enzymes Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Fungicides, Industrial General aspects genes growth retardation hypersensitivity Life Sciences Microbial ecology Microbiology Miscellaneous monitoring Mutagenesis Mutagenesis, Site-Directed Mutation Mycology Niacinamide - analogs & derivatives Protein Binding Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Pyridines Structure-Activity Relationship succinate dehydrogenase Succinate Dehydrogenase - chemistry Succinate Dehydrogenase - genetics Succinate Dehydrogenase - metabolism |
| title | Site‐directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B from Botrytis cinerea highlights different roles in enzyme activity and inhibitor binding |
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