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Assessment of the Bemisia tabaci CYP6CM1vQ transcript and protein levels in laboratory and field‐derived imidacloprid‐resistant insects and cross‐metabolism potential of the recombinant enzyme
Author(s) -
Roditakis Emmanouil,
Morou Evangelia,
Tsagkarakou Anastasia,
Riga Maria,
Nauen Ralf,
Paine Mark,
Morin Shai,
Vontas John
Publication year - 2011
Publication title -
insect science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 45
eISSN - 1744-7917
pISSN - 1672-9609
DOI - 10.1111/j.1744-7917.2010.01384.x
Subject(s) - imidacloprid , thiacloprid , biology , neonicotinoid , thiamethoxam , acetamiprid , clothianidin , population , cytochrome p450 , toxicology , enzyme , pesticide , biochemistry , ecology , demography , sociology
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 CYP6CM1 protein ( CYP6CM1vQ ) is capable of metabolizing imidacloprid. Here, we show that the levels of BtCYP6CM1vQ were also elevated in laboratory‐resistant strains and field‐derived populations, with variable imidacloprid resistance levels, collected in Crete. High levels of CYP6CM1vQ 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 CYP6CM1vQ protein levels were higher in imidacloprid‐resistant insects, which further implicates the gene as the causal factor of resistance. Finally, assessment of the cross‐metabolism potential of CYP6CM1vQ 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 .