(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 > Holometabola: NE > Diptera: NE > Nematocera: NE > Culicomorpha: NE > Culicoidea: NE > Culicidae: NE > Culicinae: NE > Aedini: NE > Aedes: NE > Stegomyia: NE > Aedes aegypti: NE
F105S/F350Y : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity F105S/G285A/F350Y : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity F105S/G285A : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity F105S : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity F350Y : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity G285A/F350Y : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity G285A : Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity
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 MKMSAVVRLCCNMISLLLCITVISPVYGIFDRLVVQTSSGPIRGRSTMVL GREVHVFNGVPFAKPPVDGLRFRKPVPAEPWHGVLDATRLPPSCIQERYE YFPGFAGEEMWNPNTNVSEDCLYLNIWVPTKTRLRHGRGLNFGNNDYFQD DDDFQRQHQSKGGLAMLVWIYGGGFMSGTSTLDVYNAEMLAAVGNVIVAS MQYRVGSFGFFYLAPYLNDDDAPGNVGLWDQALAIRWLKENAKAFGGDPD LITLFGESAGGSSVSLHLLSPVTRGLSRRGILQSGTLNAPWSHMSAEKAL SVAEALIDDCNCNVTLLKDNPNYVMNCMRNVDAKTISVQQWNSYSGILGF PSAPTIDGVFMTADPMTMLREANLEGVEILVGSNRDEGTYFLLYDFIDYF EKDAATSLPRDKFLEIMNTIFSKASEPEREAIIFQYTGWESGNDGYQNQQ QVGRSVGDHFFICPTNEFALGLAERGASVYYYYFTHRTSTSLWGEWMGVL HGDEVEYIFGQPMNVSMQYRQRERDLSRRMVLSVSEFARSGNPALEGEHW PVYTKENPIYFIFNAEGEDDLRGEKYGRGPMATACAFWNDFLPRLRAWSV PPKSSCNILEQTSAATILYVDIKIVTVLMVFILVRLY
We present a draft sequence of the genome of Aedes aegypti, the primary vector for yellow fever and dengue fever, which at approximately 1376 million base pairs is about 5 times the size of the genome of the malaria vector Anopheles gambiae. Nearly 50% of the Ae. aegypti genome consists of transposable elements. These contribute to a factor of approximately 4 to 6 increase in average gene length and in sizes of intergenic regions relative to An. gambiae and Drosophila melanogaster. Nonetheless, chromosomal synteny is generally maintained among all three insects, although conservation of orthologous gene order is higher (by a factor of approximately 2) between the mosquito species than between either of them and the fruit fly. An increase in genes encoding odorant binding, cytochrome P450, and cuticle domains relative to An. gambiae suggests that members of these protein families underpin some of the biological differences between the two mosquito species.
Title: Site-directed mutagenesis of an acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti confers insecticide insensitivity Vaughan A, Rocheleau T, Ffrench-Constant R Ref: Experimental Parasitology, 87:237, 1997 : PubMed
Insecticide resistance is a serious problem facing the effective control of insect vectors of disease. Insensitive acetylcholinesterase (AChE) confers resistance to organophosphorus (OP) and carbamate insecticides and is a widespread resistance mechanism in vector mosquitoes. Although the point mutations that underlie AChE insensitivity have been described from Drosophila, the Colorado potato beetle, and house flies, no resistance associated mutations have been documented from mosquitoes to date. We are therefore using a cloned acetylcholinesterase gene from the yellow fever mosquito Aedes aegypti as a model in which to perform site directed mutagenesis in order to understand the effects of potential resistance associated mutations. The same resistance associated amino-acid replacements as found in other insects also confer OP and carbamate resistance to the mosquito enzyme. Here we describe the levels of resistance conferred by different combinations of these mutations and the effects of these mutations on the kinetics of the AChE enzyme. Over-expression of these constructs in baculovirus will facilitate purification of each of the mutant enzymes and a more detailed analysis of their associated inhibition kinetics.
A degenerate PCR strategy was used to isolate a fragment of the acetylcholinesterase gene (Ace) homolog from Aedes aegypti and screen for a cDNA clone containing the complete open reading frame of the gene. The predicted amino acid sequence of the Aedes gene shares 64% identity with Ace from Drosophila and 87% identity with the acetylcholinesterase gene from another mosquito species Anopheles stephensi. High levels of expression of the Aedes gene were achieved by infection of Sf21 cells with a recombinant baculovirus containing the Aedes Ace cDNA. The catalytic properties and sensitivity of the recombinant enzyme to insecticide inhibition are described and discussed in relation to the role of insensitive AChE in conferring resistance to organophosphorus and carbamate insecticides.
