Aedes aegypti peroxidase gene characterization and developmental expression.
The functions of insect peroxidases include detoxification, stabilization of extracellular matrices, and possible involvement in insect immunity. The current study describes the isolation of a peroxidase gene, AePox, and its cDNA from the mosquito, Aedes aegypti. AePox codes for a protein that is homologous to various heme-peroxidases from vertebrates and invertebrates, with highest identity to Drosophila melanogaster peroxidase (62%). Sequence comparison identified several functionally and structurally conserved domains in the mosquito peroxidase, including a heme environment, a calcium binding site, and five possible disulfide bridges. These results imply that AePOX may likely have a similar structure and catalytic mechanism as those described for the mammalian myeloperoxidase superfamily. Expression studies demonstrate that AePox is transcribed in mosquito larvae and pupae, but not in adults, in ovaries, or in early embryos. However, AePOX protein is present in all mosquito stages and possibly has a maturation process that is similar to that of human myeloperoxidase. Unlike most human peroxidases, the AePox gene contains a TATA box and an ecdysone response element (EcRE).
Department of Animal Health and Biomedical Sciences, 1656 Linden Dr., University of Wisconsin, Madison, WI 53706, USA.
X
X
Zhao
C T
CT
Smartt
J
J
Li
B M
BM
Christensen
D000330:Aedes / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D000595:Amino Acid Sequence; D000818:Animals; D018628:Gene Dosage; D017344:Genes, Insect; D015698:Genomic Library; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
D012333:RNA, Messenger; D010544:Peroxidases