cDNA and deduced protein sequence of acetylcholinesterase from the diamondback moth, Plutella xylostella (L.)(Lepidoptera: Plutellidae).

Ni, Xiao-yu; Tomita, Takashi; Kasai, Shinji; Kono, Yoshiaki

doi:10.1303/aez.2003.49

Cited by 18 publications

(8 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The phylogenetic tree showed that Lepidoptera and Diptera insects are two distinct groups. This is in accord with the results based on AChE sequences of Ni et al (2003). Due to the conservation of gene sequences in closely related insects, it could be used to some extent to identify the different orders of insects or animals.…”

Section: Discussionsupporting

confidence: 86%

cDNA sequence analysis of ribosomal protein S13 gene in Plutella xylostella (Lepidoptera: Plutellidae)

et al. 2005

View full text Add to dashboard Cite

Ribosomal protein S13 gene has been cloned and analyzed in many organisms, but there are few documents relating to insects. In this communication, the full-length cDNA sequence of ribosomal protein S13 gene in the diamondback moth, Plutella xylostella (Lepidoptera: Plutellidae), was determined by using PCR amplification technique. The features of the ribosomal protein S13 gene sequence were analyzed and the deduced amino acids sequence was compared with those from other insects. The results of multi-alignment of the amino acid sequences between the diamondback moth and other insect species revealed that this gene sequence is highly conserved in insects. Based on maximum likelihood method, a phylogenetic tree was constructed from 10 different species using PHYLIP software. It showed that nematode is one separate lineage and the five insect species belong to another lineage, whereas those species higher than insects form the third one. The pattern of this phylogenetic tree evidently represented the evolution of different species.

show abstract

Section: Discussionsupporting

confidence: 86%

cDNA sequence analysis of ribosomal protein S13 gene in Plutella xylostella (Lepidoptera: Plutellidae)

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Subsequently, amino acid substitutions were identified in the Cyclorrhapha fly species, Musca domestica (Huang et al, 1997;Kozaki et al, 2001;Walsh et al, 2001), Lucilia cuprina (Chen et al, 2001), and Bactrocera oleae (Vontas et al, 2002); however, no insecticide insensitivity-attributable mutation was found in Ace orthologues of the resistant strains of other insect species such as Culex pipiens (Malcolm et al, 1998), Cx. tritaeniorhynchus (Mori et al, 2001), Nephotettix cincticeps (Tomita et al, 2000) and Plutella xylostella (Ni et al, 2003). Recently, another class of AChE genes, paralogous to Ace, has been reported from the green bug, Schizaphis graminum (Gao et al, 2002) and a mosquito, Anopheles gambiae (Weill et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Differential tissue distribution of two acetylcholinesterase transcripts in the German cockroach, Blattella germanica

Mizuno

Komagata

et al. 2007

Appl. Entomol. Zool.

Self Cite

View full text Add to dashboard Cite

Recent studies have revealed that non-Cyclorrhapha insects possess two acetylcholinesterases (AChEs): Drosophila Ace-orthologous (o-Ace) and -paralogous (p-Ace) forms. In these insects, p-Ace is considered as a neural target of insecticides because mutations conferring insecticide insensitivity have been consistently identified in equivalent forms from various insects. To clarify the functional differentiation between the two AChE isoforms, we characterized the expression of two AChE genes in nerve cell-rich and -poor tissues of German cockroaches. The two AChE genes were expressed at comparable levels in both the nerve cord and head. Two AChE isoforms with mutually discriminatory fenitroxon sensitivities were exhibited in the nerve cord, indicating that o-Ace and p-Ace function in the neurons. pAce was mainly expressed in the nerve cord and head, while o-Ace was ubiquitously expressed at a comparable level. Moreover, o-Ace transcripts as well as AChE activity were detected in the fat body where no nervous tissue is observed. No AChE activity was detected in the hemolymph. These results show that p-Ace is better as an insecticidal target because of its abundant transcripts in nervous tissue. In addition, the roles of o-Ace, which is present ubiquitously without secretion into the hemolymph in insects, are discussed.

show abstract

“…5Ј RACE or 3Ј RACE were also tried with gene-specific primers of the mosquito AChE, but a specific band was not obtained. It has been reported that there are long UTR promoting erroneous fusions occur during PCR in marginal regions of the AChE gene in P. xylostella (Ni et al, 2003;Baek et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

cDNA identification and gene expression of two types of acetylcholinesterases in a cultured cell line of Aedes albopictus, compared to mosquito whole body extracts

Mizuno

Tomita

Kasai

et al. 2006

Appl. Entomol. Zool.

Self Cite

View full text Add to dashboard Cite

Two cDNA sequences containing open reading frames encoding two types of acetylcholinesterase (AChE) precursors, Ace-orthologous AChE (AO-AChE) and Ace-paralogous AChE (AP-AChE), with 635 residues and 702 residues, respectively, were determined in Aedes albopictus by PCR-based techniques. The partial and whole cDNAs for AOAChE and AP-AChE, respectively, were also sequenced from a cultured cell line of mosquito, NIAS-AeAl-2, derived from Ae. albopictus neonatal larvae. Comparing the sequences of the respective AChEs between cultured cells and mosquito whole body extracts, many nucleotide polymorphisms were found in both AChE cDNAs but only one amino acid substitution. The expression level of AChE genes in the cultured cells was low, 1/2 and 1/7 that of the mosquito body for AO-AChE and AP-AChE, respectively. The expression ratio of AO-AChE/AP-AChE was 1/2 in the cultured cells. AP-AChE genes was more highly expressed than AO-AChE genes in both cultured cells and the mosquito body. In an enzyme assay, the activity of AChE per protein in the cultured cells was 1/8 that of the mosquito body. The function of AChE in cultured cells is discussed based on the present and previous papers.

show abstract

cDNA and deduced protein sequence of acetylcholinesterase from the diamondback moth, Plutella xylostella (L.)(Lepidoptera: Plutellidae).

Cited by 18 publications

References 28 publications

cDNA sequence analysis of ribosomal protein S13 gene in Plutella xylostella (Lepidoptera: Plutellidae)

cDNA sequence analysis of ribosomal protein S13 gene in Plutella xylostella (Lepidoptera: Plutellidae)

Differential tissue distribution of two acetylcholinesterase transcripts in the German cockroach, Blattella germanica

cDNA identification and gene expression of two types of acetylcholinesterases in a cultured cell line of Aedes albopictus, compared to mosquito whole body extracts

Contact Info

Product

Resources

About