GEPHE SUMMARY
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Gephebase Gene
Entry Status
Published
GepheID
GP00002454
Main curator
Courtier
PHENOTYPIC CHANGE
Trait Category
Trait State in Taxon A
Plutella xylostella - sensitive
Trait State in Taxon B
Plutella xylostella - resistant
Ancestral State
Taxon A
Taxonomic Status
Taxon A
Latin Name
Common Name
diamondback moth
Synonyms
diamondback moth; cabbage moth; Plutella xylostella (Linnaeus, 1758); Putella xylostella
Rank
species
Lineage
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a; Pancrustacea; Hexapoda; Insecta; Dicondylia; Pterygota; Neoptera; Holometabola; Amphiesmenoptera; Lepidoptera; Glossata; Neolepidoptera; Heteroneura; Ditrysia; Yponomeutoidea; Plutellidae; Plutella
Parent
NCBI Taxonomy ID
is Taxon A an Infraspecies?
No
Taxon B
Latin Name
Common Name
diamondback moth
Synonyms
diamondback moth; cabbage moth; Plutella xylostella (Linnaeus, 1758); Putella xylostella
Rank
species
Lineage
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a; Pancrustacea; Hexapoda; Insecta; Dicondylia; Pterygota; Neoptera; Holometabola; Amphiesmenoptera; Lepidoptera; Glossata; Neolepidoptera; Heteroneura; Ditrysia; Yponomeutoidea; Plutellidae; Plutella
Parent
NCBI Taxonomy ID
is Taxon B an Infraspecies?
No
GENOTYPIC CHANGE
Generic Gene Name
Ace
Synonyms
AcChE; ace; ACE; ace-2; ache; AchE; AChE; CG17907; CHE; dAChE; dmAChE; DmAChE; Dmel\CG17907; Dm_ace; FBgn0000024; l(3)26; l(3)87Ed
String
Sequence Similarities
Belongs to the type-B carboxylesterase/lipase family.
GO - Molecular Function
GO:0042803 : protein homodimerization activity
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GO - Biological Process
GO:0006581 : acetylcholine catabolic process
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GO - Cellular Component
GO:0005886 : plasma membrane
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UniProtKB
Drosophila melanogaster
Drosophila melanogaster
Mutation #1
Presumptive Null
Molecular Type
Aberration Type
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
A298S and G324A
Experimental Evidence
Taxon A | Taxon B | Position | |
---|---|---|---|
Codon | - | - | - |
Amino-acid | Ala | Ser | 298 |
Main Reference
Authors
Lee DW; Choi JY; Kim WT; Je YH; Song JT; Chung BK; Boo KS; Koh YH
Abstract
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.
Additional References
Mutation #2
Presumptive Null
Molecular Type
Aberration Type
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
A298S and G324A
Experimental Evidence
Taxon A | Taxon B | Position | |
---|---|---|---|
Codon | - | - | - |
Amino-acid | Gly | Ala | 324 |
Main Reference
Authors
Lee DW; Choi JY; Kim WT; Je YH; Song JT; Chung BK; Boo KS; Koh YH
Abstract
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.
Additional References
RELATED GEPHE
EXTERNAL LINKS
COMMENTS
See also https://www.sciencedirect.com/science/article/abs/pii/S1226861512000295
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