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Insecticide resistance in Bemisia tabaci from Cyprus

Insect Science 2011年第1期18卷 30-39页

作者： Vassilis Vassiliou Maria Emmanouilidou Andreas Perrakis Evangelia Morou John Vontas anastasia tsagkarakou Emmanouil Roditakis Agricultural Research Institute Nicosia Cyprus Faculty of Biotechnology and Appfied Biology Department of Biology University of Crete Herakfion Greece National Agricultural Research Foundation (N.AG.RE.F.) Plant Protection Institute of Heraklion Heraklion Greece

A comprehensive study on the Bemisia tabaci （biotype B） resistance to neonicotinoid insecticides imidacloprid, acetamiprid and thiamethoxam, and pyrethroid bifenthrin was conducted in Cyprus. The resistance level to eight field-collected B. tabaci populations was investigated. The activities of enzymes involved in metabolic detoxification and the frequencies ofpyrethroid and organophosphates target site resistance mutations were determined. Moderate to high levels of resistance were detected for imidacloprid （re- sistance factor [RF] 77-392） and thiamethoxam （RF 50-164） while low resistance levels were observed for acetamiprid （RF 7-12）. Uniform responses by the Cypriot whiteflies could be observed against all neonicotinoid insecticides. No cross-resistance between the neonicotinoids was detected as well as no association with the activity of the P450 microsomal oxidases. Only imidacloprid resistance correlated with carboxylesterase activity. Low to extremely high resistance was observed for insecticide bifenthrin （RF 49 1 243） which was associated with the frequency of the resistant allele in the sodium channel gene but not with the activity of the detoxification enzymes. Finally, the F331W mutation in the acetylcholinesterase enzyme acel gene was fixed in all B. tabaci populations from Cyprus.

关键词： acetamiprid B biotype Bemisia tabaci bifenthrin Cyprus imidacloprid insecticide resistance thiamethoxam

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Assessment of the Bemisia tabaci C YP6CM l vQ transcript and protein levels in laboratory and field-derived imidacloprid-resistant insects and cross-metabolism potential of the recombinant enzyme

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Insect Science 2011年第1期18卷 23-29页

作者： Emmanouil Roditakis Evangelia Morou anastasia tsagkarakou Maria Riga Ralf Nauen Mark Paine Shai Morin John Vontas Laboratory of Entomology and Agricultural Zoology Plant Protection Institute of Heraklion National Agricultural Research Foundation Heraklion (N.AG.RE.F.) Heraklio Greece Faculty of Applied Biology and Biotechnology Department of Biology University of Crete Heraklion Greece Vector Group Liverpool School of Tropical Medicine Liverpool UK Bayer CropScience AG Research Insecticides Insect Toxicology and Resistance Monheim Germany Department of Entomology Faculty of Agricultural Food and Environmental Quality Sciences Hebrew University of Jerusalem Rehovot Israel

Over-expression of the cytochrome P450 CYP6CM1 gene has been associated with imidacloprid resistance in a number of Q and B biotype Bemisia tabaci laboratory strains from distinct geographical origins worldwide. We recently demonstrated that the Q biotype version of the CYP6CM 1 protein （CYP6CMlvQ） is capable of metabolizing imida- cloprid. Here, we show that the levels of BtCYP6CMlvQ were also elevated in laboratory- resistant strains and field-derived populations, with variable imidacloprid resistance levels, collected in Crete. High levels of CYP6CMlvQ transcripts were also determined in survivors of a heterogeneous field population, after exposure to discriminating imidacloprid dosage. Using peptide antibody-based detection assays, we demonstrated that in line with transcriptional data, the CYP6CMlvQ protein levels were higher in imidacloprid-resistant insects, which further implicates the gene as the causal factor of resistance. Finally, assess- ment of the cross-metabolism potential of CYP6CMlvQ against additional neonicotinoid molecules used for B. tabaci control revealed that clothianidin and thiacloprid, but not acetamiprid or thiamethoxam, are metabolized by the recombinant enzyme in vitro.

关键词： detoxification neonicotinoids peptide antibodies P450

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