The Aedes aegypti glutathione transferase family

In this report, we describe the glutathione transferase (GST) gene family in the dengue vector Aedes aegypti and suggest a novel role for a new class of mosquito GSTs. Twenty-six GST genes are present in Ae. aegypti, two of which are alternatively spliced to give a total of 29 transcripts for cytoso...

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Bibliographic Details
Published in:Insect biochemistry and molecular biology 2007-10, Vol.37 (10), p.1026-1035
Main Authors: Lumjuan, Nongkran, Stevenson, Bradley J., Prapanthadara, La-aied, Somboon, Pradya, Brophy, Peter M., Loftus, Brendan J., Severson, David W., Ranson, Hilary
Format: Article
Language:English
Subjects:
Aedes - enzymology
Aedes - genetics
Aedes aegypti
Alternative Splicing
Amino Acid Sequence
Animals
Anopheles gambiae
binding properties
DDT
DDT (pesticide)
Drosophila melanogaster
gene expression
Glutathione transferase
Glutathione Transferase - chemistry
Glutathione Transferase - genetics
Glutathione Transferase - metabolism
hematin binding
Heme
Hemin - metabolism
Insect Proteins - chemistry
Insect Proteins - genetics
Insect Proteins - metabolism
Insecticide resistance
Molecular Sequence Data
Multigene Family
nucleotide sequences
Phylogeny
recombinant proteins
Sequence Alignment
sequence homology
Substrate Specificity
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Summary:In this report, we describe the glutathione transferase (GST) gene family in the dengue vector Aedes aegypti and suggest a novel role for a new class of mosquito GSTs. Twenty-six GST genes are present in Ae. aegypti, two of which are alternatively spliced to give a total of 29 transcripts for cytosolic GSTs. The six classes identified in other insect species are all represented and, as in Anopheles gambiae, the majority of the mosquito GSTs belong to the insect-specific Delta and Epsilon classes with eight members each. Sixteen secure 1:1 orthologs were identified between GSTs in Ae. aegypti and An. gambiae, but only four of these have recognisable orthologs in Drosophila melanogaster. Three mosquito-specific GSTs were identified which did not belong to any previously recognised GST classes. One of these, GSTx2, has been previously implicated in conferring 1,1,1-trichloro-2,2-bis-( p-chlorophenyl)ethane (DDT) resistance in Ae. aegypti from South America. However, we found no evidence for increased levels of this GST protein in DDT/pyrethroid-resistant populations from Thailand. Furthermore, we show that the recombinant GSTX2-2 protein is unable to metabolise DDT. Interestingly, GSTX2-2 showed an affinity for hematin, and this, together with the restricted distribution of this class to haematophagous insects, may indicate a role for these enzymes in protecting mosquitoes against heme toxicity during blood feeding.
ISSN:0965-1748
1879-0240
DOI:10.1016/j.ibmb.2007.05.018