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An amino acid substitution (L925V) associated with resistance to pyrethroids in Varroa destructor
The Varroa mite, Varroa destructor, is an important pest of honeybees and has played a prominent role in the decline in bee colony numbers over recent years. Although pyrethroids such as tau-fluvalinate and flumethrin can be highly effective in removing the mites from hives, their intensive use has...
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Published in: | PloS one 2013-12, Vol.8 (12), p.e82941 |
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description | The Varroa mite, Varroa destructor, is an important pest of honeybees and has played a prominent role in the decline in bee colony numbers over recent years. Although pyrethroids such as tau-fluvalinate and flumethrin can be highly effective in removing the mites from hives, their intensive use has led to many reports of resistance. To investigate the mechanism of resistance in UK Varroa samples, the transmembrane domain regions of the V. destructor voltage-gated sodium channel (the main target site for pyrethroids) were PCR amplified and sequenced from pyrethroid treated/untreated mites collected at several locations in Central/Southern England. A novel amino acid substitution, L925V, was identified that maps to a known hot spot for resistance within the domain IIS5 helix of the channel protein; a region that has also been proposed to form part of the pyrethroid binding site. Using a high throughput diagnostic assay capable of detecting the mutation in individual mites, the L925V substitution was found to correlate well with resistance, being present in all mites that had survived tau-fluvalinate treatment but in only 8 % of control, untreated samples. The potential for using this assay to detect and manage resistance in Varroa-infected hives is discussed. |
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Although pyrethroids such as tau-fluvalinate and flumethrin can be highly effective in removing the mites from hives, their intensive use has led to many reports of resistance. To investigate the mechanism of resistance in UK Varroa samples, the transmembrane domain regions of the V. destructor voltage-gated sodium channel (the main target site for pyrethroids) were PCR amplified and sequenced from pyrethroid treated/untreated mites collected at several locations in Central/Southern England. A novel amino acid substitution, L925V, was identified that maps to a known hot spot for resistance within the domain IIS5 helix of the channel protein; a region that has also been proposed to form part of the pyrethroid binding site. Using a high throughput diagnostic assay capable of detecting the mutation in individual mites, the L925V substitution was found to correlate well with resistance, being present in all mites that had survived tau-fluvalinate treatment but in only 8 % of control, untreated samples. The potential for using this assay to detect and manage resistance in Varroa-infected hives is discussed.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0082941</identifier><identifier>PMID: 24367572</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Amino Acid Substitution ; Amino acids ; Animals ; Apis mellifera ; Bees ; Binding sites ; Biochemistry ; Chemistry ; Diagnostic systems ; Drug Resistance ; European honeybee ; Fluvalinate ; Hot spots ; Insecticides ; Insecticides - pharmacology ; Laboratories ; Management science ; Mites ; Molecular biology ; Mutation ; Polymerase Chain Reaction ; Pyrethrins - pharmacology ; Pyrethroids ; Sodium ; Sodium channels (voltage-gated) ; Studies ; Substitutes ; Trialeurodes vaporariorum ; Varroa destructor ; Varroidae - drug effects ; Varroidae - genetics ; Varroidae - metabolism ; Voltage-Gated Sodium Channels - chemistry ; Voltage-Gated Sodium Channels - genetics ; Voltage-Gated Sodium Channels - metabolism</subject><ispartof>PloS one, 2013-12, Vol.8 (12), p.e82941</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 González-Cabrera et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 González-Cabrera et al 2013 González-Cabrera et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c593t-911a3fb23cc2072878fc7ffb65278311a44286402be985df44abd8e80ac210b03</citedby><cites>FETCH-LOGICAL-c593t-911a3fb23cc2072878fc7ffb65278311a44286402be985df44abd8e80ac210b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1469304847/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1469304847?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24367572$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Smagghe, Guy</contributor><creatorcontrib>González-Cabrera, Joel</creatorcontrib><creatorcontrib>Davies, T G Emyr</creatorcontrib><creatorcontrib>Field, Linda M</creatorcontrib><creatorcontrib>Kennedy, Peter J</creatorcontrib><creatorcontrib>Williamson, Martin S</creatorcontrib><title>An amino acid substitution (L925V) associated with resistance to pyrethroids in Varroa destructor</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The Varroa mite, Varroa destructor, is an important pest of honeybees and has played a prominent role in the decline in bee colony numbers over recent years. Although pyrethroids such as tau-fluvalinate and flumethrin can be highly effective in removing the mites from hives, their intensive use has led to many reports of resistance. To investigate the mechanism of resistance in UK Varroa samples, the transmembrane domain regions of the V. destructor voltage-gated sodium channel (the main target site for pyrethroids) were PCR amplified and sequenced from pyrethroid treated/untreated mites collected at several locations in Central/Southern England. A novel amino acid substitution, L925V, was identified that maps to a known hot spot for resistance within the domain IIS5 helix of the channel protein; a region that has also been proposed to form part of the pyrethroid binding site. Using a high throughput diagnostic assay capable of detecting the mutation in individual mites, the L925V substitution was found to correlate well with resistance, being present in all mites that had survived tau-fluvalinate treatment but in only 8 % of control, untreated samples. The potential for using this assay to detect and manage resistance in Varroa-infected hives is discussed.</description><subject>Acids</subject><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Apis mellifera</subject><subject>Bees</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Chemistry</subject><subject>Diagnostic systems</subject><subject>Drug Resistance</subject><subject>European honeybee</subject><subject>Fluvalinate</subject><subject>Hot spots</subject><subject>Insecticides</subject><subject>Insecticides - pharmacology</subject><subject>Laboratories</subject><subject>Management science</subject><subject>Mites</subject><subject>Molecular biology</subject><subject>Mutation</subject><subject>Polymerase Chain Reaction</subject><subject>Pyrethrins - pharmacology</subject><subject>Pyrethroids</subject><subject>Sodium</subject><subject>Sodium channels (voltage-gated)</subject><subject>Studies</subject><subject>Substitutes</subject><subject>Trialeurodes vaporariorum</subject><subject>Varroa destructor</subject><subject>Varroidae - 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Although pyrethroids such as tau-fluvalinate and flumethrin can be highly effective in removing the mites from hives, their intensive use has led to many reports of resistance. To investigate the mechanism of resistance in UK Varroa samples, the transmembrane domain regions of the V. destructor voltage-gated sodium channel (the main target site for pyrethroids) were PCR amplified and sequenced from pyrethroid treated/untreated mites collected at several locations in Central/Southern England. A novel amino acid substitution, L925V, was identified that maps to a known hot spot for resistance within the domain IIS5 helix of the channel protein; a region that has also been proposed to form part of the pyrethroid binding site. Using a high throughput diagnostic assay capable of detecting the mutation in individual mites, the L925V substitution was found to correlate well with resistance, being present in all mites that had survived tau-fluvalinate treatment but in only 8 % of control, untreated samples. The potential for using this assay to detect and manage resistance in Varroa-infected hives is discussed.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24367572</pmid><doi>10.1371/journal.pone.0082941</doi><oa>free_for_read</oa></addata></record> |
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subjects | Acids Amino Acid Substitution Amino acids Animals Apis mellifera Bees Binding sites Biochemistry Chemistry Diagnostic systems Drug Resistance European honeybee Fluvalinate Hot spots Insecticides Insecticides - pharmacology Laboratories Management science Mites Molecular biology Mutation Polymerase Chain Reaction Pyrethrins - pharmacology Pyrethroids Sodium Sodium channels (voltage-gated) Studies Substitutes Trialeurodes vaporariorum Varroa destructor Varroidae - drug effects Varroidae - genetics Varroidae - metabolism Voltage-Gated Sodium Channels - chemistry Voltage-Gated Sodium Channels - genetics Voltage-Gated Sodium Channels - metabolism |
title | An amino acid substitution (L925V) associated with resistance to pyrethroids in Varroa destructor |
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