(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 > Paraneoptera: NE > Hemiptera: NE > Sternorrhyncha: NE > Aphidomorpha: NE > Aphidoidea: NE > Aphididae: NE > Aphidinae: NE > Macrosiphini: NE > Myzus: NE > Myzus persicae: 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 MDQWLLWFSYLVASTYGLSLRHARHQSVGTPTAEEILEPQILIEDTDHVF RQRASDMFAQEPEYTEKRNLNHRRRSEFSGNQDNDFESSGETYSAYKSDD PLVIHTNKGKIRGITQAASTGKLVDAWLGIPYAKKPIGDLRFRHPRPIDR WDNTNPETILNCTTPPNTCVQIFDTLFGDFPGATMWNPNSPVSEDCLYIN VVVPKPRPQNAAVMVWIFGGGFYSGSATLDIYDPKVLVSEENVILVSMQY RVASLGFLYFDTEDVPGNAGLFDQLMALQWVHENIKLFGGNPNNVTLFGE SAGAVSVSLHLLSPLSRNLFNQAIMESGSSTAPWAILSREESYSRGLRLA RAMGCPDDRNEIHKTVECLRKANSSTMVEKEWDHVAICFFPFVPVVDGAF LDDYPQKSLSTNNFKKTNILMGSNSEEGYYSIFYYLTELFKKEENVVVSR ENFVKAIGQLNPNADAAVKSAIEFEYTDWFSPNDPEKNRNALDKMVGDYQ FTCNVNEFAHKYALTGNNVYMYYFKHRSLNNPWPKWTGVMHGDEISYVFG DPLNPNKRYEIEEIELSKKMMRYWTNFAKTGNPSKTFEGSWVTPKWPVHT AYGKEFLTLDTNNTSIGVGPRLEQCAFWKNYVPDLMAISKSMKSDKNCTT ISGGTKTYMIELSLWTIVMTTAVLML
References
Title: Pyrethroid and carbamate resistance in Czech populations of Myzus persicae (Sulzer) from oilseed rape Stara J, Hovorka T, Horska T, Zuskova E, Kocourek F Ref: Pest Manag Sci, :, 2023 : PubMed
BACKGROUND: Failures in controlling Myzus persicae by pyrethroids and carbamates have been observed in Czechia since 2018. Eleven populations collected from Czech oilseed rape fields during 2018-2021 were tested for susceptibility to 11 insecticides. The presence of a single nucleotide polymorphism (SNP) leading to knockdown resistance in M. persicae populations was screened using allelic discriminating quantitative real-time polymerase chain reaction (qPCR). The presence of mutations related with the resistance of M. persicae to pyrethroids and carbamates was detected by sequencing paratype voltage-gated sodium channel and acetylcholinesterase 2 genes, respectively. RESULTS: Resistance to alpha-cypermethrin and pirimicarb was detected in most of the tested populations. The L1014F mutation was detected in 44.5% of M. persicae individuals surviving the field-recommended dose of alpha-cypermethrin. Sequencing of partial para gene for paratype voltage-gated sodium channel detected five different SNPs leading to four amino acid substitutions (kdr L1014F; s-kdr M918L; s-kdr M918T; and L932F). No pyrethroid-sensitive genotype was detected. The S431F amino acid substitution conferring resistance to carbamates was detected in 11 of 20 individuals with different pyrethroid-resistance genotypes. CONCLUSION: Resistance of M. persicae to both pyrethroids and carbamates was detected in nine of 11 populations. High resistance of M. persicae was correlated with mutations of the sodium channel. Sulfoxaflor, flonicamid, and spirotetramat are proposed as effective compounds to control pyrethroid- and carbamate-resistant populations of M. persicae. This article is protected by copyright. All rights reserved.
Title: An amino acid substitution on the second acetylcholinesterase in the pirimicarb-resistant strains of the peach potato aphid, Myzus persicae Nabeshima T, Kozaki T, Tomita T, Kono Y Ref: Biochemical & Biophysical Research Communications, 307:15, 2003 : PubMed
cDNAs encoding two acetylcholinesterases (AChEs) were isolated from the peach potato aphid, Myzus persicae. MpAChE1 was orthologous and MpAChE2 was paralogous with the ace of Drosophila melanogaster. The deduced amino acid sequence of MpAChE1 cDNA was identical between the pirimicarb susceptible and resistant strains. However, a single amino acid substitution of Ser431Phe on MpAchE2 was found in the pirimicarb resistant strains. This substitution was located in the acyl pocket of the enzyme and was thought to alter the ligand specificity.
