(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 > Yponomeutoidea: NE > Plutellidae: NE > Plutella: NE > Plutella xylostella: NE
A201S : Identification and characterization of ace1-type acetylcholinesterase likely associated with organophosphate resistance in Plutella xylostella A441G : Identification and characterization of ace1-type acetylcholinesterase likely associated with organophosphate resistance in Plutella xylostella D131G : Mutations of acetylcholinesterase1 contribute to prothiofos-resistance in Plutella xylostella (L.) F386V : Amino acid substitutions and intron polymorphism of acetylcholinesterase1 associated with mevinphos resistance in diamondback moth, Plutella xylostella (L.) G227A : Identification and characterization of ace1-type acetylcholinesterase likely associated with organophosphate resistance in Plutella xylostella
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 MRALLAVLCAAAAAAGASAGAHEHRARHHAPEHAYPPPPYRGHGEAVRYN PELDTILPRLDHETSSRRAKYADKHDDYRARERLDAPQADQPALGPDDDD PLVVRTRKGRVRGITLTAATGKKVDAWFGIPYAQKPIGDLRFRHPRPVEN WGDEILNATTLPHSCVQIIDTVFGDFPGAMMWNPNTDMQEDCLYINIVTP RPRPKNAAVMLWVFGGGFYSGTATLDVYDPKILVSEEKIVYVSMQYRVAS LGFLFFDTPDVPGNAGLFDQLMALQWVKDNIQYFGGNPHNVTLFGESSGA VSVSLHLLSPLSRNMFSQAIMQSAAASAPWAIISREESVIRGIRLAEAVH CPHSKTDMGPMIECLRKKSADELVNNEWGTLGICEFPFVPIIDGSFLDEM PIRSLAHQNFKKTNILMGSNTEEGYYFILYYLTELFPKEENVGISREQYL QAVRELNPYVNDVARQAIVFEYTDWLNPDDPIRNRNALDKMVGDYHFTCG VNEFAHRYAETGNNVYTYYYKHRSKNNPWPSWTGVMHGDEINYVFGEPSN PGKNYSPEEVEFSKTIMRYWANFARTGNPSQSPNGELTKVHWPVHTAFGR EHLSLSANSSGTVDHGLRVKQCAFWQKYLPQLIAATSKPEPPKNCTSSAE APRASYHVLGLAVVAAVSFSQKTIVKLII
References
Title: Trade-off between thermal tolerance and insecticide resistance in Plutella xylostella Zhang LJ, Wu ZL, Wang KF, Liu Q, Zhuang HM, Wu G Ref: Ecol Evol, 5:515, 2015 : PubMed
Fitness costs associated with resistance to insecticides have been well documented, usually at normal temperature conditions, in many insect species. In this study, using chlorpyrifos-resistant homozygote (RR) and chlorpyrifos-susceptible homozygote (SS) of resistance ace1 allele of Plutella xylostella (DBM), we confirmed firstly that high temperature experience in pupal stage influenced phenotype of wing venation in insecticide-resistant and insecticide-susceptible Plutella xylostella, and SS DBM showed significantly higher thermal tolerance and lower damages of wing veins under heat stress than RR DBM. As compared to SS DBM, RR DBM displayed significantly lower AChE sensitivity to chlorpyrifos, higher basal GSTs activity and P450 production at 25 degrees C, but higher inhibitions on the enzyme activities and P450 production as well as reduced resistance to chlorpyrifos under heat stress. Furthermore, RR DBM displayed significantly higher basal expressions of hsp69s, hsp72s, hsp20,hsp90,Apaf-1, and caspase-7 at 25 degrees C, but lower induced expressions of hsps and higher induced expressions of Apaf-1,caspase-9, and caspase-7 under heat stress. These results suggest that fitness costs of chlorpyrifos resistance in DBM may partly attribute to excess consumption of energy caused by over production of detoxification enzymes and hsps when the proteins are less demanded at conducive environments but reduced expressions when they are highly demanded by the insects to combat environmental stresses, or to excess expressions of apoptotic genes under heat stress, which results in higher apoptosis. The evolutionary and ecological implications of these findings at global warming are discussed.
Title: Mutations of acetylcholinesterase1 contribute to prothiofos-resistance in Plutella xylostella (L.) Lee DW, Choi JY, Kim WT, Je YH, Song JT, Chung BK, Boo KS, Koh YH Ref: Biochemical & Biophysical Research Communications, 353:591, 2007 : PubMed
Insensitive acetylcholinesterase (AChE) is involved in the resistance of organophosphorous and carbamate insecticides. We cloned a novel full-length AChE cDNA encoding ace1 gene from adult heads of the diamondback moth (DBM, Plutella xylostella). The ace1 gene encoding 679 amino acids has conserved motifs including catalytic triad, choline-binding site and acyl pocket. Northern blot analysis revealed that the ace1 gene was expressed much higher than the ace2 in all examined body parts. The biochemical properties of expressed AChEs showed substrate specificity for acetylthiocholine iodide and inhibitor specificity for BW284C51 and eserine. Three mutations of AChE1 (D229G, A298S, and G324A) were identified in the prothiofos-resistant strain, two of which (A298S and G324A) were expected to be involved in the prothiofos-resistance through three-dimensional modeling. In vitro functional expression of AChEs in Sf9 cells revealed that only resistant AChE1 is less inhibited with paraoxon, suggesting that resistant AChE1 is responsible for prothiofos-resistance.
Title: Identification and characterization of ace1-type acetylcholinesterase likely associated with organophosphate resistance in Plutella xylostella Baek JH, Kim JI, Lee DW, Chung BK, Miyata T, Lee SH Ref: Pesticide Biochemistry and Physiology, 81:164, 2005 : PubMed
Insensitive acetylcholinesterase (AChE) was determined to be primarily involved in a prothiofos-resistant (PR) strain of diamondback moth (DBM, Plutella xylostella L.), as judged by the AChE inhibition assay using paraoxon, where the PR strain exhibited ca. 26-fold increased I50 value. Extensive sequence analysis of the previously reported ace2-type DBM AChE gene revealed no difference between the susceptible and PR strains. To elucidate the molecular basis of the prothiofos resistance mechanism mediated by insensitive AChE, we cloned and characterized a second AChE gene from DBM. The deduced amino acid sequence of the novel AChE showed the highest homology to ace1, the second copy of insect ace, and was determined in fact as the predominant AChE in DBM compared to the ace2-type with 13- to 250-fold higher transcription levels depending on different tissues. Sequence comparison of the ace1-type cDNA between the susceptible and PR strains of DBM revealed that a total of three amino acid substitutions are closely associated with the PR strain. Among these, the Gly227Ala mutation, exclusively present in the PR strain, was located at the same position of the organophosphate resistance-conferring Gly-to-Ala mutation on the ace2 of the fruit fly and house fly. This finding suggests that the Gly227Ala mutation along with two other ones on the ace1 are likely responsible for the AChE insensitivity in DBM.
