Premium
Gene expression and functional characterization of two multicopper oxidase genes in the malaria mosquito, Anopheles gambiae
Author(s) -
Lang Minglin,
Gorman Maureen J.,
Gardner Stewart G.,
Yungeberg Sandi L.,
Kanost Michael R.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.674.1
Subject(s) - multicopper oxidase , anopheles gambiae , biology , biochemistry , rna interference , gene , enzyme , laccase , gene silencing , malaria , immunology , rna
The multicopper oxidase (MCO) family of enzymes includes laccases, which oxidize a broad range of substrates including diphenols, and several oxidases with specific substrates such as iron or copper. MCOs have been implicated in a diverse set of physiological processes in fungi, plants and bacteria; however, little is known about the function of MCOs in invertebrates. Our goal is to determine the functions of MCOs in the malaria vector mosquito, Anopheles gambiae , by analyzing gene expression patterns, enzyme activity and the effect of gene silencing. MCO1 and MCO3 were upregulated in the midguts and Malpighian tubules of adult females following a blood meal, and they were upregulated in other tissues in response to an immune challenge. These results suggest that MCO1 and MCO3 may function in detoxification and/or immunity, possibly by oxidizing ferric iron. We have purified recombinant MCO1 and MCO3 and have begun to test their activity with a set of possible substrates including o‐ and p‐ diphenols, iron, tannin and flavonoids. Both enzymes oxidize diphenols, but their substrate specificities are not identical. RNAi‐mediated gene silencing will be used to determine whether the enzymes function in detoxifying iron or in defense against microbes. This work was supported by NIH Grants R03AI057816 and R01AI070864.