Molecular Detection of kdr and superkdr Mutation Sites and Analysis of the Binding Modes of Pyrethroid Insecticides with Voltage-Gated Sodium Channels in the Plant Bug Lygus pratensis (Hemiptera: Miridae)
This study identified genetic mutations linked to resistance to pyrethroid insecticides in the plant pest Lygus pratensis. The voltage-gated sodium channel (VGSC) gene was cloned, revealing two mutations (Met918Thr and Leu1014Phe) in laboratory strains and field populations from Inner Mongolia, resu...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 2024-12, Vol.72 (49), p.27451-27465 |
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| container_issue | 49 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Zhang, Liqi Ni, Ruoyao Chen, Jing Yang, Jiale Dong, Yawen Yuchi, Zhiguang Tan, Yao |
| description | This study identified genetic mutations linked to resistance to pyrethroid insecticides in the plant pest Lygus pratensis. The voltage-gated sodium channel (VGSC) gene was cloned, revealing two mutations (Met918Thr and Leu1014Phe) in laboratory strains and field populations from Inner Mongolia, resulting in variable pyrethroid resistance. A 3D model of LpVGSC was created using homology modeling, and pyrethroid binding patterns were analyzed via molecular docking. Molecular dynamics simulations confirmed structural stability changes and binding stability of pyrethroids to VGSC sites. Mutation frequencies of homozygous and heterozygous genotypes did not exceed 40 and 20%, respectively. Toxicity tests showed high resistance to λ-cyhalothrin (LC50:401.31 ng/cm2). The kdr (L1014F) and superkdr (M918T) mutations weakened interaction forces, reducing pyrethroid binding. M918T and L1014F mutations are predicted to reduce Type I pyrethroid affinity, suggesting Type II pyrethroids may be more effective against resistant strains. These findings aid in resistance management and insecticide design. |
| doi_str_mv | 10.1021/acs.jafc.4c03416 |
| format | Article |
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The voltage-gated sodium channel (VGSC) gene was cloned, revealing two mutations (Met918Thr and Leu1014Phe) in laboratory strains and field populations from Inner Mongolia, resulting in variable pyrethroid resistance. A 3D model of LpVGSC was created using homology modeling, and pyrethroid binding patterns were analyzed via molecular docking. Molecular dynamics simulations confirmed structural stability changes and binding stability of pyrethroids to VGSC sites. Mutation frequencies of homozygous and heterozygous genotypes did not exceed 40 and 20%, respectively. Toxicity tests showed high resistance to λ-cyhalothrin (LC50:401.31 ng/cm2). The kdr (L1014F) and superkdr (M918T) mutations weakened interaction forces, reducing pyrethroid binding. M918T and L1014F mutations are predicted to reduce Type I pyrethroid affinity, suggesting Type II pyrethroids may be more effective against resistant strains. These findings aid in resistance management and insecticide design.</description><identifier>ISSN: 0021-8561</identifier><identifier>ISSN: 1520-5118</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/acs.jafc.4c03416</identifier><identifier>PMID: 39225681</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Binding Sites ; China ; food chemistry ; Food Safety and Toxicology ; genes ; Hemiptera - drug effects ; Hemiptera - genetics ; Hemiptera - metabolism ; Heteroptera - chemistry ; Heteroptera - genetics ; Heteroptera - metabolism ; heterozygosity ; homozygosity ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Insecticide Resistance - genetics ; insecticides ; Insecticides - chemistry ; Insecticides - metabolism ; Insecticides - pharmacology ; Lygus ; Molecular Docking Simulation ; molecular dynamics ; Mutation ; pests ; Protein Binding ; pyrethrins ; Pyrethrins - chemistry ; Pyrethrins - metabolism ; Pyrethrins - pharmacology ; resistance management ; sodium ; sodium channels ; toxicity ; Voltage-Gated Sodium Channels - chemistry ; Voltage-Gated Sodium Channels - genetics ; Voltage-Gated Sodium Channels - metabolism</subject><ispartof>Journal of agricultural and food chemistry, 2024-12, Vol.72 (49), p.27451-27465</ispartof><rights>2024 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-a252t-b443afab15d32800340d46ff6d06d32b720c7ae548cd2f710c8c67d78292981d3</cites><orcidid>0000-0002-8450-9888 ; 0000-0001-5990-9196 ; 0000-0003-2595-9106</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/acs.jafc.4c03416$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/acs.jafc.4c03416$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39225681$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Liqi</creatorcontrib><creatorcontrib>Ni, Ruoyao</creatorcontrib><creatorcontrib>Chen, Jing</creatorcontrib><creatorcontrib>Yang, Jiale</creatorcontrib><creatorcontrib>Dong, Yawen</creatorcontrib><creatorcontrib>Yuchi, Zhiguang</creatorcontrib><creatorcontrib>Tan, Yao</creatorcontrib><title>Molecular Detection of kdr and superkdr Mutation Sites and Analysis of the Binding Modes of Pyrethroid Insecticides with Voltage-Gated Sodium Channels in the Plant Bug Lygus pratensis (Hemiptera: Miridae)</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>This study identified genetic mutations linked to resistance to pyrethroid insecticides in the plant pest Lygus pratensis. The voltage-gated sodium channel (VGSC) gene was cloned, revealing two mutations (Met918Thr and Leu1014Phe) in laboratory strains and field populations from Inner Mongolia, resulting in variable pyrethroid resistance. A 3D model of LpVGSC was created using homology modeling, and pyrethroid binding patterns were analyzed via molecular docking. Molecular dynamics simulations confirmed structural stability changes and binding stability of pyrethroids to VGSC sites. Mutation frequencies of homozygous and heterozygous genotypes did not exceed 40 and 20%, respectively. Toxicity tests showed high resistance to λ-cyhalothrin (LC50:401.31 ng/cm2). The kdr (L1014F) and superkdr (M918T) mutations weakened interaction forces, reducing pyrethroid binding. M918T and L1014F mutations are predicted to reduce Type I pyrethroid affinity, suggesting Type II pyrethroids may be more effective against resistant strains. These findings aid in resistance management and insecticide design.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>China</subject><subject>food chemistry</subject><subject>Food Safety and Toxicology</subject><subject>genes</subject><subject>Hemiptera - drug effects</subject><subject>Hemiptera - genetics</subject><subject>Hemiptera - metabolism</subject><subject>Heteroptera - chemistry</subject><subject>Heteroptera - genetics</subject><subject>Heteroptera - metabolism</subject><subject>heterozygosity</subject><subject>homozygosity</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Insecticide Resistance - genetics</subject><subject>insecticides</subject><subject>Insecticides - chemistry</subject><subject>Insecticides - metabolism</subject><subject>Insecticides - pharmacology</subject><subject>Lygus</subject><subject>Molecular Docking Simulation</subject><subject>molecular dynamics</subject><subject>Mutation</subject><subject>pests</subject><subject>Protein Binding</subject><subject>pyrethrins</subject><subject>Pyrethrins - chemistry</subject><subject>Pyrethrins - metabolism</subject><subject>Pyrethrins - pharmacology</subject><subject>resistance management</subject><subject>sodium</subject><subject>sodium channels</subject><subject>toxicity</subject><subject>Voltage-Gated Sodium Channels - chemistry</subject><subject>Voltage-Gated Sodium Channels - genetics</subject><subject>Voltage-Gated Sodium Channels - metabolism</subject><issn>0021-8561</issn><issn>1520-5118</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1vEzEQhi0EoqFw54R8LBIbbO961-HWBmgrJaJSgevKsWcTl4299YdQ_iM_Cu8mcEPiZHnmmXcsPwi9pmROCaPvpQrzB9mpeaVIWdH6CZpRzkjBKRVP0YxkphC8pmfoRQgPhBDBG_IcnZULxngt6Az9WrseVOqlxx8hgorGWew6_EN7LK3GIQ3gx8s6RTk1702EMPUurewPwYSRjzvAV8ZqY7d47TRMxbuDh7jzzmh8a8MYrszY-mniDn93fZRbKK5lBI3vnTZpj5c7aS30ARs7Rd710kZ8lbZ4ddimgAefaTvuvLiBvRkiePkBr403WsLbl-hZJ_sAr07nOfr2-dPX5U2x-nJ9u7xcFZJxFotNVZWykxvKdckEyT9HdFV3Xa1JnSubhhHVSOCVUJp1DSVKqLrRjWALthBUl-fo4pg7ePeYIMR2b4KCPj8WXAptSXnFKrEo2X-gWVLDa1JmlBxR5V0IHrp28GYv_aGlpB11t1l3O-puT7rzyJtTetrsQf8d-OM3A--OwDTqks_Kwr_zfgOJCbiI</recordid><startdate>20241211</startdate><enddate>20241211</enddate><creator>Zhang, Liqi</creator><creator>Ni, Ruoyao</creator><creator>Chen, Jing</creator><creator>Yang, Jiale</creator><creator>Dong, Yawen</creator><creator>Yuchi, Zhiguang</creator><creator>Tan, Yao</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0002-8450-9888</orcidid><orcidid>https://orcid.org/0000-0001-5990-9196</orcidid><orcidid>https://orcid.org/0000-0003-2595-9106</orcidid></search><sort><creationdate>20241211</creationdate><title>Molecular Detection of kdr and superkdr Mutation Sites and Analysis of the Binding Modes of Pyrethroid Insecticides with Voltage-Gated Sodium Channels in the Plant Bug Lygus pratensis (Hemiptera: Miridae)</title><author>Zhang, Liqi ; Ni, Ruoyao ; Chen, Jing ; Yang, Jiale ; Dong, Yawen ; Yuchi, Zhiguang ; Tan, Yao</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a252t-b443afab15d32800340d46ff6d06d32b720c7ae548cd2f710c8c67d78292981d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>China</topic><topic>food chemistry</topic><topic>Food Safety and Toxicology</topic><topic>genes</topic><topic>Hemiptera - drug effects</topic><topic>Hemiptera - genetics</topic><topic>Hemiptera - metabolism</topic><topic>Heteroptera - chemistry</topic><topic>Heteroptera - genetics</topic><topic>Heteroptera - metabolism</topic><topic>heterozygosity</topic><topic>homozygosity</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Insecticide Resistance - genetics</topic><topic>insecticides</topic><topic>Insecticides - chemistry</topic><topic>Insecticides - metabolism</topic><topic>Insecticides - pharmacology</topic><topic>Lygus</topic><topic>Molecular Docking Simulation</topic><topic>molecular dynamics</topic><topic>Mutation</topic><topic>pests</topic><topic>Protein Binding</topic><topic>pyrethrins</topic><topic>Pyrethrins - chemistry</topic><topic>Pyrethrins - metabolism</topic><topic>Pyrethrins - pharmacology</topic><topic>resistance management</topic><topic>sodium</topic><topic>sodium channels</topic><topic>toxicity</topic><topic>Voltage-Gated Sodium Channels - chemistry</topic><topic>Voltage-Gated Sodium Channels - genetics</topic><topic>Voltage-Gated Sodium Channels - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Liqi</creatorcontrib><creatorcontrib>Ni, Ruoyao</creatorcontrib><creatorcontrib>Chen, Jing</creatorcontrib><creatorcontrib>Yang, Jiale</creatorcontrib><creatorcontrib>Dong, Yawen</creatorcontrib><creatorcontrib>Yuchi, Zhiguang</creatorcontrib><creatorcontrib>Tan, Yao</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Liqi</au><au>Ni, Ruoyao</au><au>Chen, Jing</au><au>Yang, Jiale</au><au>Dong, Yawen</au><au>Yuchi, Zhiguang</au><au>Tan, Yao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Detection of kdr and superkdr Mutation Sites and Analysis of the Binding Modes of Pyrethroid Insecticides with Voltage-Gated Sodium Channels in the Plant Bug Lygus pratensis (Hemiptera: Miridae)</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>2024-12-11</date><risdate>2024</risdate><volume>72</volume><issue>49</issue><spage>27451</spage><epage>27465</epage><pages>27451-27465</pages><issn>0021-8561</issn><issn>1520-5118</issn><eissn>1520-5118</eissn><abstract>This study identified genetic mutations linked to resistance to pyrethroid insecticides in the plant pest Lygus pratensis. The voltage-gated sodium channel (VGSC) gene was cloned, revealing two mutations (Met918Thr and Leu1014Phe) in laboratory strains and field populations from Inner Mongolia, resulting in variable pyrethroid resistance. A 3D model of LpVGSC was created using homology modeling, and pyrethroid binding patterns were analyzed via molecular docking. Molecular dynamics simulations confirmed structural stability changes and binding stability of pyrethroids to VGSC sites. Mutation frequencies of homozygous and heterozygous genotypes did not exceed 40 and 20%, respectively. Toxicity tests showed high resistance to λ-cyhalothrin (LC50:401.31 ng/cm2). The kdr (L1014F) and superkdr (M918T) mutations weakened interaction forces, reducing pyrethroid binding. M918T and L1014F mutations are predicted to reduce Type I pyrethroid affinity, suggesting Type II pyrethroids may be more effective against resistant strains. These findings aid in resistance management and insecticide design.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>39225681</pmid><doi>10.1021/acs.jafc.4c03416</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-8450-9888</orcidid><orcidid>https://orcid.org/0000-0001-5990-9196</orcidid><orcidid>https://orcid.org/0000-0003-2595-9106</orcidid></addata></record> |
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| subjects | Animals Binding Sites China food chemistry Food Safety and Toxicology genes Hemiptera - drug effects Hemiptera - genetics Hemiptera - metabolism Heteroptera - chemistry Heteroptera - genetics Heteroptera - metabolism heterozygosity homozygosity Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - metabolism Insecticide Resistance - genetics insecticides Insecticides - chemistry Insecticides - metabolism Insecticides - pharmacology Lygus Molecular Docking Simulation molecular dynamics Mutation pests Protein Binding pyrethrins Pyrethrins - chemistry Pyrethrins - metabolism Pyrethrins - pharmacology resistance management sodium sodium channels toxicity Voltage-Gated Sodium Channels - chemistry Voltage-Gated Sodium Channels - genetics Voltage-Gated Sodium Channels - metabolism |
| title | Molecular Detection of kdr and superkdr Mutation Sites and Analysis of the Binding Modes of Pyrethroid Insecticides with Voltage-Gated Sodium Channels in the Plant Bug Lygus pratensis (Hemiptera: Miridae) |
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