GEPHE SUMMARY Print
Gephebase Gene
Entry Status
Published
GepheID
GP00002544
Main curator
Courtier
PHENOTYPIC CHANGE
Trait Category
Trait State in Taxon A
Drosophila melanogaster - sensitive to pyrethroids
Trait State in Taxon B
Drosophila melanogaster - resistant to pyrethroids
Ancestral State
Taxon A
Taxonomic Status
Taxon A
Common Name
fruit fly
Synonyms
Sophophora melanogaster; fruit fly; Drosophila melanogaster Meigen, 1830; Sophophora melanogaster (Meigen, 1830); Drosophila melangaster
Rank
species
Lineage
Show more ... Brachycera; Muscomorpha; Eremoneura; Cyclorrhapha; Schizophora; Acalyptratae; Ephydroidea; Drosophilidae; Drosophilinae; Drosophilini; Drosophila; Sophophora; melanogaster group; melanogaster subgroup
NCBI Taxonomy ID
is Taxon A an Infraspecies?
No
Taxon B
Common Name
fruit fly
Synonyms
Sophophora melanogaster; fruit fly; Drosophila melanogaster Meigen, 1830; Sophophora melanogaster (Meigen, 1830); Drosophila melangaster
Rank
species
Lineage
Show more ... Brachycera; Muscomorpha; Eremoneura; Cyclorrhapha; Schizophora; Acalyptratae; Ephydroidea; Drosophilidae; Drosophilinae; Drosophilini; Drosophila; Sophophora; melanogaster group; melanogaster subgroup
NCBI Taxonomy ID
is Taxon B an Infraspecies?
No
GENOTYPIC CHANGE
Presumptive Null
No
Molecular Type
Aberration Type
SNP
SNP Coding Change
Nonsynonymous
Molecular Details of the Mutation
A1648V = A1494V
Experimental Evidence
Taxon A Taxon B Position
Codon - - -
Amino-acid - - -
Authors
Pittendrigh B; Reenan R; ffrench-Constant RH; Ganetzky B
Abstract
The gene para in Drosophila melanogaster encodes an alpha subunit of voltage-activated sodium channels, the presumed site of action of DDT and pyrethroid insecticides. We used an existing collection of Drosophila para mutants to examine the molecular basis of targetsite resistance to pyrethroids and DDT. Six out of thirteen mutants tested were associated with a largely dominant, 10- to 30-fold increase in DDT resistance. The amino acid lesions associated with these alleles defined four sites in the sodium channel polypeptide where a mutational change can cause resistance: within the intracellular loop between S4 and S5 in homology domains I and III, within the pore region of homology domain III, and within S6 in homology domain III. Some of these sites are analogous with those defined by knockdown resistance (kdr) and super-kdr resistance-associated mutations in houseflies and other insects, but are located in different homologous units of the channel polypeptide. We find a striking synergism in resistance levels with particular heterozygous combinations of para alleles that appears to mimic the super-kdr double mutant housefly phenotype. Our results indicate that the alleles analyzed from natural populations represent only a subset of mutations that can confer resistance. The implications for the binding site of pyrethroids and mechanisms of target-site insensitivity are discussed.
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