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Cloning of a Glutathione Transferase Superfamily Gene in Leishmania
Author(s) -
Mckenzie Nerissa,
Pitula Joseph,
Hearne Jennifer
Publication year - 2011
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.25.1_supplement.lb83
Subject(s) - heme , glutathione , leishmania , cloning (programming) , biochemistry , biology , glutathione s transferase , gene , enzyme , genetics , computer science , programming language , parasite hosting , world wide web
Leishmaniasis is a tropical disease that afflicts approximately 12 million of the world's population. Its causative agent is the parasitic protozoan Leishmania, a member of the Trypanosomatidea family. In contrast to other eukaryotes, members of the Trypanosomatidea family lack a complete heme biosynthetic pathway; therefore, they must acquire heme exogenously. The mechanism of heme scavenging may be accomplished through its coordination with glutathione (GSH) via membrane associated proteins in eicosanoid and glutathione metabolism (MAPEG), members of the glutathione transferase (GST) superfamily. It is known that Macaca fascicularis microsomal prostaglandin E synthase type 2 (mPGES‐2), a MAPEG GST, binds GSH. The enzyme‐glutathione complex then has the potential to form a coordination bond with heme. Previously, our laboratory reported the presence of a suspected GST in L. tarentolae (GST1). Here, we show that a second GST, GST2, also exists in Leishmania. Identification of GST2 was accomplished using genomic searches. PCR amplification of the homolog in L. tarentolae employed primers designed on the basis of the identified gene, LmjF26.1540. We are now expressing the recombinant protein to characterize its activity. Because Leishmania lack a complete heme biosynthetic pathway, the exploitation of its heme dependency is a key target for chemotherapeutic intervention.