(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 > Auchenorrhyncha: NE > Fulgoromorpha: NE > Fulgoroidea: NE > Delphacidae: NE > Delphacinae: NE > Nilaparvata: NE > Nilaparvata lugens: NE
F/Y330S : Cloning of the acetylcholinesterase 1 gene and identification of point mutations putatively associated with carbofuran resistance in Nilaparvata lugens F331C/I332L : Point mutations in acetylcholinesterase 1 associated with chlorpyrifos resistance in the brown planthopper, Nilaparvata lugens Stal F331C : Point mutations in acetylcholinesterase 1 associated with chlorpyrifos resistance in the brown planthopper, Nilaparvata lugens Stal F331H/I332L : Cloning of the acetylcholinesterase 1 gene and identification of point mutations putatively associated with carbofuran resistance in Nilaparvata lugens G119A : Cloning of the acetylcholinesterase 1 gene and identification of point mutations putatively associated with carbofuran resistance in Nilaparvata lugens G119S : Point mutations in acetylcholinesterase 1 associated with chlorpyrifos resistance in the brown planthopper, Nilaparvata lugens Stal I332L : Point mutations in acetylcholinesterase 1 associated with chlorpyrifos resistance in the brown planthopper, Nilaparvata lugens Stal
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 MVVHTTKGRVRGVTLTASTGKQVDAWLGIPYAQKPIGPLRFRHPRPPDRW DHGHDSHILNTTQLPNSCVQIIDTLFGDFPGSTMWNPNTPVSEDCLYMNV VVPRPRPKQAAVMVWIFGGGFYSGTSTLDVYDHRTLVAEENVILVSMQYR VASLGFLYFDTAEVPGNAGLFDQMMALQWVHDNIAAFGGNPRNVTLFGES AGAVSVSLHLLSPLSRNLFSQAIMQSGSPTAPWAIISRDESILRGLRLAE AMGCPHNRSEIAEATECLRRMNASDLVENEWGTLGICEFPFVPIVDGTFL DDHPHRSLATKNFKKTNILMGSNTEEGYYFIFYHLTELFRNEENVYVNRD EFLQAVRELNPYVNNVARQAIVFEYTDWLNPDDPIRNRDALDKMVGDYQF TCNVNELAHRYADTGNNVYMYLFKHRSLSNPWPSWTGVMHGDEISYVFGE PLDPNKSFQPAEIELSRRMMRYWANFAKTGNPSVSEDGTWTATYWPVHTA YGREFLTLDVNSTATGRGPRLKQCAFWKKYLPQLLSSTSPPQPSPPPPAK DICASSATLQSPGSATLLLLLATLCPLLATLWPLLATLWSSLATLSSTSL HASSWPLLASSSPILATLWPLHATLWPLPASLWPLHATLWPSLATTLVAT HHLPHRSTMPSIY
References
Title: Cloning of the acetylcholinesterase 1 gene and identification of point mutations putatively associated with carbofuran resistance in Nilaparvata lugens Kwon DH, Cha DJ, Kim YH, Lee SW, Lee SH Ref: Pesticide Biochemistry and Physiology, 103:94, 2012 : PubMed
Molecular mechanisms of carbofuran resistance in the brown planthopper, Nilaparvata lugens Stl, were investigated. A carbofuran-resistant strain (CAS) showed approximately 45.5- and 15.1-fold resistance compared with a susceptible strain (SUS) and a non-selected field strain (FM), respectively. Activities of the esterase and mixed-function oxidase were approximately 2.8- and 1.6-fold higher, respectively, in the CAS strain than in the SUS strain, suggesting that these enzymes play a minor role in carbofuran resistance. Interestingly, the insensitivity of acetylcholinesterase (AChE) to carbofuran was approximately 5.5- and 3.7-fold higher in the CAS strain compared to the SUS and FM strains, respectively, indicating that AChE insensitivity is associated with carbofuran resistance. Western blot analysis identified two kinds of AChEs, of which the type-1 AChE (encoded from Nlace1, which is paralogous to the Drosophila AChE gene) was determined to be the major catalytic AChE in N. lugens. The open reading frame of Nlace1 is composed of 1989 bp (approximately 74 kD) and revealed 52.5% and 24.3% amino acid sequence identities to those of Nephotettix cincticeps and Drosophila melanogaster, respectively. Screening of point mutations identified four amino acid substitutions (G119A, F/Y330S, F331H and H332L) in the CAS strain that likely contribute to AChE insensitivity. The frequencies of these mutations were well correlated with resistance levels, confirming that they are associated with reduced sensitivity to carbofuran in N. lugens. These point mutations can be useful as genetic markers for monitoring resistance levels in field populations of N. lugens.
Title: Molecular characterization of two acetylcholinesterase genes from the brown planthopper, Nilaparvata lugens (Hemiptera: Delphacidae) Li BL, Chen W, Liu L, Zhang XC, Bao YY, Cheng JA, Zhu ZR, Zhang CX Ref: Pesticide Biochemistry and Physiology, 102:198, 2012 : PubMed
Acetylcholinesterase (AChE), which is encoded by the ace gene, catalyzes the hydrolysis of the neurotransmitter acetylcholine to terminate nerve impulses at the postsynaptic membrane. AChE is a primary target of many insecticides including organophosphates (OP) and carbamates (CB). In this study, full-length cDNA sequences of two ace genes (Nlace1 and Nlace2) were sequenced from the brown planthopper (BPH) Nilaparvata lugens, the most destructive insect pest of rice crops. Nlace1 cDNA is 2842 nucleotides long and contains an ORF potentially encoding a 790 amino acid peptide. Nlace2 cDNA is 2852 bp in length and contains an ORF that potentially encodes a 672 amino acid peptide. NlAChE1 has an identity of 40% with NlAChE2 at the amino acid sequence level. Phylogenetic analysis of 59 AChEs from 32 animal species showed that NlAChE1 is most closely related to AChE1s from Blattella germanica and Nephotettix cincticeps, while NlAChE2 is most closely related to AChE2 from N. cincticeps. Quantitative RT-PCR analysis showed that Nlace1 is expressed at a much higher level than Nlace2 in all developmental stages and tissues, demonstrating that NlAChE1 may be the dominant AChE form of the two enzymes. This result will help reveal the resistance mechanism of N. lugens to organophosphorous and carbamate insecticides and promote development of more selective insecticides targeting the main NlAChE1.
