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Identification of a Glutathione Transferase Superfamily gene in Leishmania tarentolae
Author(s) -
OseiOwusu Nana Yaw,
Hearne Jennifer L,
Currington Rashalai,
Pitula Joseph
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.913.4
Subject(s) - heme , leishmania , biochemistry , glutathione , biology , gene , glutaredoxin , glutathione s transferase , enzyme , chemistry , parasite hosting , world wide web , computer science
Leishmaniasis is a tropical disease that is caused by the parasitic protozoa Leishmania , a member of the Trypanosomatidea family. Unlike other eukaryotes, members of the Trypanosomatidea family lack a complete heme biosynthetic pathway; therefore, they must acquire heme exogenously. The mechanisms of heme scavenging and storage remain to be fully elucidated. Here, it is revealed that one mechanism of these functions may be accomplished through the coordination of heme 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 which has the potential to form a coordination bond with heme. Therefore, it is reasonable to hypothesize that there is an enzyme similar to mPGES‐2 which scavenges free heme in promastigote Leishmania for use during its maturation. Identification of a GST superfamily member gene target gene in the L. major genome was accomplished using the Basic Local Alignment Search Tool at GeneDB. Because Leishmania lack a complete heme biosynthetic pathway, the exploitation of its heme dependency is a key target for drug discovery. Identification of this gene provides the first evidence of a GST superfamily member in Leishmania . Supported by TEDCO‐MRASC #W81XWH‐07‐2‐0055