Liposcelis paeta isolate WZ, HZ, NY acetylcholinesterase 1
Comment
Residue 202 is G in WZ and HZ and E in NY, Residue 441 (Torpedo_number 236) is V in WZ and HZ and I in NY, Residue 605 (Torpedo_number 400) is L in WZ and HZ and F in NY, Residue 674 (Torpedo_number 469) is L in WZ and HZ and M in NY, Residue 759 is N in WZ and NY and S in HZ long n-term sequence not included
(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 > Psocodea: NE > Psocoptera: NE > Troctomorpha: NE > Nanopsocetae: NE > Liposcelidae: NE > Liposcelis: NE > Liposcelis paeta: 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 MEYGERSSDMLAEGSLDLSWKDGVEFGSRDKDIEREREVKDDFHHVGQKN EEDPLIITTAKGKIHGITLAAATGKLEDAWLGIPYAQKPLGNLRFRHPRP VERWDPEILNTTKLPNSCMQILDTVFGDFPGATMWNPNTPLSEDCLYINV VAPKPRPKKAAVMVWIFGGGFYSGTATLDVYDPKTLVSEEKVIVVSMQYR IASLGFLFFDTPDVPGNAGLFDQLMALQWVHDNIHAFGGNPHNVTLFGES AGAVSVSTHLLSPLSRNLFSQAIMESGSPTAPWAIVSREESILRGLRLAE AVGCPHDKSQIKAVIECLRNTNASVLVDNEWGTLGICEFPFVPVIDGSFL DETPQKSLANKNFKKTNILMGSNTEEGYYFIIYYLTELLRKEENVYVNRD EFLQAVRELNPYINNVARQAIIFEYTDWLNPDDPVRNRDALDKMVGDYHL TCNVNEFAHRYAETGNNVYMYYFKHRSAANPWPSWTGVMHGDEINYVFGE PLNPKKNYQPQEKILSKRLMRYWANFAKTGNPSMSEDGTWTDVYWPVHTP FGREYLTLAVNNTSTGRGPRLKQCAFWKKYLPQLVAVTANLNSKNPQPCA SSTNEMFGVVSFDVFTLIIISKVPRHTILQ
References
Title: Cloning and characterization of acetylcholinesterase 1 genes from insecticide-resistant field populations of Liposcelis paeta Pearman (Psocoptera: Liposcelididae) Wu S, Li M, Tang PA, Felton GW, Wang JJ Ref: Insect Biochemistry & Molecular Biology, 40:415, 2010 : PubMed
The psocid, Liposcelis paeta Pearman, is an increasingly important polyphagous pest of stored products worldwide. Intensive use of organophosphorous insecticides for pest control has facilitated resistance development in psocids in China. Three insecticide-resistant field populations of L. paeta were collected from Nanyang city of Henan Province (NY), and Wuzhou (WZ) and Hezhou (HZ) cities of Guangxi Province, China. Previous studies have shown that psocids have different susceptibilities to insecticides. In addition, their AChE susceptibilities to paraoxon-ethyl and demeton-S-methyl also differed from each other. Acetylcholinesterase 1, which is one of the major targets for organophosphate insecticides, has been fully cloned and sequenced from these populations of L. paeta. Comparison of both nucleotide and deduced amino acid sequences revealed nucleotide polymorphisms among L. paeta ace 1 genes from different populations, but none of these polymorphisms correspond to the active sites in AChE 1 from other insects. The results of comparative quantitative real-time PCR indicated that the relative expression level of HZ ace 1 gene was the highest among three populations, which was 1.20 and 1.02-fold higher than those of NY and WZ populations, respectively. This may due to an epigenetic inheritance phenomenon, which allows organisms to respond to a particular environment through changes in gene expression.
Title: Comparison of acetylcholinesterase from three field populations of Liposcelis paeta Pearman (Psocoptera: Liposcelididae): Implications of insecticide resistance Ren Y, Wei X-Q, Wu S, Dou W, Wang J-J Ref: Pesticide Biochemistry and Physiology, 90:196, 2008 : PubMed
The toxicological and biochemical characteristics of acetylcholinesterases (AChE) in Liposcelis paeta Pearman were investigated in three field populations collected from Nanyang city of Henan Province (NY), Wuzhou (WZ) and Hezhou (HZ) Cities of Guangxi Province, China. The result of bioassay showed that the LC50s of the NY (281.4802 mg/m2) and the WZ (285.0655 mg/m2) to dichlorvos were 1.156-fold and 1.171-fold higher than that of the HZ (243.5197 mg/m2), respectively. Compared to NY population, the activity per insect and the specific activity of AChE in WZ and HZ populations were significantly higher, and significant kinetic differences among the three populations were also observed. The apparent Michaelis-Menten constant (Km) for acetylthiocholine iodide (ATChI) was obviously lower in NY than that in WZ and HZ populations, indicating a higher affinity to the substrate ATChI in the NY population. The affinity to the substrate ATChI between WZ and HZ population was also significantly different. As for Vmax, the values of WZ and HZ populations were significantly greater when compared to that for NY population, suggesting a possible over expression of AChE in the former two populations. The inhibition studies of AChE indicated that paraoxon-ethyl, demeton-S-methyl, carbaryl, and eserine all possessed some inhibitory effects on AChE in L. paeta. The results of I50S suggested that when compared to the other two populations, while AChE from HZ population was less sensitive to paraoxon-ethyl and demeton-S-methyl. The contradiction with the result of the bioassay might be due to the different insecticides used in the bioassay. Although both carbaryl and eserine had excellent inhibitory effects, there was no significant difference among the three populations. The statistical analysis of the bimolecular rate constants (ki) was consistent with the above situation that carbamates expressed remarkable inhibitory effects. It was noticeable that NY population was most sensitive to carbaryl while least to eserine. The differences in AChE among three populations may attribute to the difference in control practices for psocids between Henan and Guangxi Provinces.
