Biosynthesis of Galactofuranose in Kinetoplastids: Novel Therapeutic Targets for Treating Leishmaniasis and Chagas' Disease
Author(s) -
Michelle Oppenheimer,
Ana Lisa Valenciano,
Pablo Sobrado
Publication year - 2011
Publication title -
enzyme research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.439
H-Index - 39
eISSN - 2090-0406
pISSN - 2090-0414
DOI - 10.4061/2011/415976
Subject(s) - chagas disease , trypanosoma cruzi , leishmaniasis , disease , virology , leishmania , biology , medicine , immunology , computational biology , parasite hosting , computer science , world wide web
Cell surface proteins of parasites play a role in pathogenesis by modulating mammalian cell recognition and cell adhesion during infection. β-Galactofuranose (Galf) is an important component of glycoproteins and glycolipids found on the cell surface of Leishmania spp. and Trypanosoma cruzi. β-Galf-containing glycans have been shown to be important in parasite-cell interaction and protection against oxidative stress. Here, we discuss the role of β-Galf in pathogenesis and recent studies on the Galf-biosynthetic enzymes: UDP-galactose 4′ epimerase (GalE), UDP-galactopyranose mutase (UGM), and UDP-galactofuranosyl transferase (GalfT). The central role in Galf formation, its unique chemical mechanism, and the absence of a homologous enzyme in humans identify UGM as the most attractive drug target in the β-Galf-biosynthetic pathway in protozoan parasites
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