The acetycholinesterase gene ofAnopheles stephensi

Hall, Lucinda M. C.; Malcolm, C. A.

doi:10.1007/bf00712805

Cited by 69 publications

(40 citation statements)

References 24 publications

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“…3. The sequence shows a high degree of amino acid identity with that previously reported for both Anopheles stephensi (87%) [25] and Drosophila melanogaster (64%) [24].…”

Section: Cloning and Sequence Analysis Of Aedes Ace Genesupporting

confidence: 66%

“…3) is also hydrophilic and interestingly, exhibits complete amino acid identity. This hydrophilic insertion appears to be unique to insect acetylcholinesterases and is absent in both nematode Ace-1 [27] and vertebrate cholinesterase sequences [28][29][30][31][32][33][34][35], lending support to the hypothesis that proteolytic cleavage of the AChE precursor protein could be a common mechanism in insects [25,26]. Boxed residues indicate sequence identity.…”

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 91%

“…A 308-bp fragment of the Aedes Ace gene, encompassing most of the coding region between the histidine and glutamic acid residues of the catalytic triad, was amplified using degenerate primers based on knowledge of conserved regions of insect AChE sequence data [24][25][26]. This fragment was used to probe an adult eDNA library at high stringency.…”

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 99%

“…The three conserved residues equivalent to those constituting the catalytic triad in Torpedo AChE are found in positions corresponding to those likely to constitute the catalytic triad in other invertebrate AChE sequences [24][25][26][27]. These residues, relative to the equivalent residues in Drosophila Ace gene are: serine258(276), glutamate387(405) and histidine 501(518).…”

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 99%

“…This peptide motif is common to all vertebrate [28][29][30][31][32][33][34][35] and invertebrate [24][25][26][27] cholinesterases studied to date. As noted by Hall and Malcolm [25], both the putative signal peptide domain and C-terminus of the insect AChE protein are [25,26] is the hydrophilic region located between Arg-148 and Pro-180 in Drosophila ACHE, where endoproteolytic cleavage of the 75KDa precursor protein into two non-covalently linked polypeptides takes place [37]. Although lacking sequence homology with the Drosophila hydrophilic peptide, the corresponding region in the two mosquito AChE peptide sequences (Fig.…”

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 99%

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Cloning, sequencing and functional expression of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti

1995

FEBS Letters

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“…3. The sequence shows a high degree of amino acid identity with that previously reported for both Anopheles stephensi (87%) [25] and Drosophila melanogaster (64%) [24].…”

Section: Cloning and Sequence Analysis Of Aedes Ace Genesupporting

confidence: 66%

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 91%

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 99%

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 99%

Section: Cloning and Sequence Analysis Of Aedes Ace Genementioning

confidence: 99%

See 3 more Smart Citations

Cloning, sequencing and functional expression of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti

1995

FEBS Letters

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Diagnosis and characterization of insecticide-insensitive acetylcholinesterase in three populations of the sweetpotato whiteflyBemisia tabaci

1998

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A biochemical approach was used to characterize acetylcholinesterase (AChE) insecticide insensitivity in several sweetpotato whitefly (Bemisia tabaci; SPW) populations. Discriminating doses of insecticide were established to differentiate between sensitive and insensitive SPW strains and to genotype individual whitefly. This technique was then used to examine the frequency of insensitive AChE alleles in several SPW populations and to isolate a line homozygous for insensitive AChE from a heterogenous B‐type population. Inheritance of putative altered AChE genotypes was consistent with the proposed haplo‐diploid status of B. tabaci. This biochemical diagnostic was also employed to determine the role of insensitive AChE in the observed resistance profiles of several laboratory populations subjected to different selection regimes. In keeping with previous studies on insecticide resistance in SPW, resistance does not appear to be uniquely associated with the B‐type but rather with SPW populations found in crop systems. © 1998 SCI.

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Two cholinesterase activities and genes are present in amphioxus

et al. 1997

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To obtain information about the evolution of the cholinesterases, acetylcholines‐terase (AChE) and butyrylcholinesterase (BuChE) in the vertebrates, we investigated the cholinesterase (ChE) activity of the cephalochordate amphioxus (Branchiostoma floridae and Branchiostoma lanceolatum). On the basis of evidence from enzymology, pharmacology, and molecular biology, we conclude that amphioxus possesses two ChE activities and two ChE genes. Two covalent inhibitors of cholinesterases were able to pharmacologically isolate the two activities as drug‐sensitive ChE and drug‐resistant ChE. Kinetically, in terms of substrate specificity, the drug‐sensitive ChE resembles vertebrate AChE, and the drug‐resistant ChE resembles the BuChE of cartilaginous and bony fish or the intermediate ChE of protostome invertebrates. We also used the polymerase chain reaction with degenerate oligonucleotide primers and genomic DNA to obtain clones of 1,574 and 1,011 bp corresponding to two cholinesterase genes from amphioxus, which we designated as ChE1 and ChE2. ChE2 codes for an enzyme with an acyl‐binding pocket sequence, a portion of the protein that plays an important role in determining substrate specificity, typical of invertebrate ChE. ChE1, which contains a 503‐bp intron, encodes a protein with a novel acyl binding site. Phylogenetic analysis of the sequences suggests that the two genes are a result of a duplication event in the lineage leading to amphioxus. We discuss the relevance of our results to the evolution of the cholinesterases in the chordates. Previously, we reported that amphioxus contained a single cholinesterase activity with properties intermediate to AChE and BuChE (Pezzementi et al. [1991] In: Cholinesterases: Structure, Function, Mechanism, Genetics and Cell Biology. J. Massoulié et al., eds. ACS: Washington, D.C., pp. 24–31). J. Exp. Zool. 277:213–229, 1997. © 1997 Wiley‐Liss, Inc.

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The acetycholinesterase gene ofAnopheles stephensi

Cited by 69 publications

References 24 publications

Cloning, sequencing and functional expression of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti

Cloning, sequencing and functional expression of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti

Diagnosis and characterization of insecticide-insensitive acetylcholinesterase in three populations of the sweetpotato whiteflyBemisia tabaci

Two cholinesterase activities and genes are present in amphioxus

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