(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Holometabola: NE > Amphiesmenoptera: NE > Lepidoptera: NE > Glossata: NE > Neolepidoptera: NE > Heteroneura: NE > Ditrysia: NE > Apoditrysia: NE > Tortricoidea: NE > Tortricidae: NE > Olethreutinae: NE > Grapholitini: NE > Cydia: NE > Cydia pomonella: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MTCNTKIVITKLLVCFLLSGVRGRSWASHHDTTTSTTQTTPTTSPAPKNF HNDPLVVETKSGLVKGYAKTVMGREVHIFTGIPFAKPPLGPLRFRKPVPI EPWHGVLDATAMPNSCYQERYEYFPGFEGEEMWNPNTNISEDCLYLNIWV PQHLRVRHHQDKPLAERPKVPILVWIYGGGYMSGTATLDLYKADIMASSS DVIVASMQYRVGAFGFLYLNKFFSPGSEEAPGNMGLWDQQLAIRWIKDNA RVFGGDPDLITLFGESAGGGSVSLHMLSPEMKGLFKRGILQSGTLNAPWS WMTGERAQDIGKVLVDDCNCNSSLLSADPSLVMDCMRGVDAKTISVQQWN SYTGILGFPSAPTVDGVFLPKDPDTMMKEGSIHNTEVLLGSNQDEGTYFL LYDFLDYFEKDGPSFLQREKFLEIINTIFKDFSNIKKEAIIFQYTDWEEI TDGYLNQKMIADIVSDYFFVCPTNYFAEVLAESGVDVYYYYFTHRTSTSL WGEWMGVMHGDEMEYVFGHPLNMSLQYHTRERDLAAHIMQSFTRFALTGK PNKPEEKWPLYSRASPHYYTYTADGTSGPAGPRGPRASACAFWNDFLNRL NELERVPCDGAVTGPYSSVAGTTLPVVLLTALATTAAL
In southern Brazilian apple (Malus spp.) orchards, predominantly organophosphates are used to control the oriental fruit moth, Cydia molesta (Busck) (Lepidoptera: Tortricidae), but control failures often occur. Therefore the susceptibility of three C. molesta Brazilian populations was investigated to five insecticides of different groups and modes of action, in comparison with a susceptible laboratory strain mass reared in southern France for >10 yr. At the same time, comparative biochemical and genetic analysis were performed, assessing the activities of the detoxification enzymatic systems and sequencing a gene of insecticide molecular target to find out markers associated with resistance. The three Brazilian populations were significantly resistant to chlorpyrifos ethyl compared with the reference strain. One of the field populations that had been frequently exposed to deltamethrin treatments showed significant decreasing susceptibility to this compound, whereas none of the three populations had loss of susceptibility to tebufenozide and thiacloprid compared with the reference strain. All three populations had slight but significant increases of glutathione transferase and carboxylesterases activities and significant decrease of specific acetylcholinesterase activities compared with the reference. Only the most resistant population to chlorpyriphos exhibited a significantly higher mixed function oxidase activity than the reference. The acetylcholinesterase of females was significantly less inhibited by carbaryl in the Brazilian populations than in the reference strain (1.7-2.5-fold), and this difference was not expressed in the male moth. However, no mutation in the MACE locus was detected. These biological and molecular characterizations of adaptive response to insecticides in C. molesta provide tools for early detection of insecticide resistance in field populations of this pest.
Title: Acetylcholinesterase mutation in an insecticide-resistant population of the codling moth Cydia pomonella (L.) Cassanelli S, Reyes M, Rault M, Carlo Manicardi G, Sauphanor B Ref: Insect Biochemistry & Molecular Biology, 36:642, 2006 : PubMed
Two strains of Cydia pomonella (L.) (Lepidoptera: Tortricidae) were selected in the lab by exposure to increasing concentrations of diflubenzuron (Rdfb strain) or azinphos-methyl (Raz strain). Insecticide bioassays showed that the adults of the Rdfb strain exhibited a 2.6-fold and a 7.7-fold resistance ratio to azinphos-methyl and carbaryl, respectively compared to a susceptible strain (S) whereas the adults of the Raz strain exhibited a 6.7-fold resistance ratio to azinphos-methyl and a 130-fold resistance ratio to carbaryl. In the Raz strain, a target site resistance mechanism was suggested by the inhibition of acetylcholinesterase (AChE) activity. In fact the ki values did not discriminate the S and Rdfb strains, while the Raz strain exhibited a 1.7-fold and a 14-fold increase in ki value compared to the S strain for azinphos-methyl oxon and carbaryl, respectively. To verify this hypothesis, two cloned AChE cDNAs sequences (named cydpom-ace2 e cydpom-ace1) were compared between the susceptible and the resistant strains. No difference in the deduced amino acid sequence was found in cydpom-ace2 (orthologous to the Drosophila melanogaster AChE). In the putative cydpom-ace1 (paralogous to the Drosophila AChE), a single amino acid substitution F399V was exclusively present in the Raz strain. The F399 lined the active site of the enzyme and the F399V substitution likely could influence the accessibility of different types of inhibitors to the catalytic site of the insensitive cydpom-ace1.
