Abstract
UDP-Galactopyranose mutase (UGM) is a unique flavin-dependent enzyme that catalyzes the conversion of UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf). The product of this reaction is the precursor to Galf, a major component of the cell wall and of cell surface glycoproteins and glycolipids in many eukaryotic and prokaryotic human pathogens. The function of UGM is important in the virulence of fungi, parasites, and bacteria. Its role in virulence and its absence in humans suggest that UGM is an ideal drug target. Significant structural and mechanistic information has been accumulated on the prokaryotic UGMs; however, in the past few years the research interest has shifted to UGMs from eukaryotic human pathogens such as fungi and protozoan parasites. It has become clear that UGMs from prokaryotic and eukaryotic organisms have different structural and mechanistic features. The amino acid sequence identity between these two classes of enzymes is low, resulting in differences in oligomeric states, substrate binding, active site flexibility, and interaction with redox partners. However, the unique role of the flavin cofactor in catalysis is conserved among this enzyme family. In this review, recent findings on eukaryotic UGMs are discussed and presented in comparison with prokaryotic UGMs.
Highlights
Vector-borne diseases like Chagas disease and leishmaniasis are caused by parasitic human pathogens and are a major health burden in many developing countries
It has recently been shown that galactofuranose (Galf), a sugar not found in humans, plays an important role in cell wall biosynthesis in A. fumigatus and many bacteria and is a major component of the cell surface matrix of Trypanosoma cruzi and Leishmania major, the causative agents of Chagas disease and leishmaniasis, respectively
Galf is important for cell wall biosynthesis and cell surface glycan structures in bacteria, fungi, and parasites
Summary
Vector-borne diseases like Chagas disease and leishmaniasis are caused by parasitic human pathogens and are a major health burden in many developing countries. It has recently been shown that galactofuranose (Galf), a sugar not found in humans, plays an important role in cell wall biosynthesis in A. fumigatus and many bacteria and is a major component of the cell surface matrix of Trypanosoma cruzi and Leishmania major, the causative agents of Chagas disease and leishmaniasis, respectively. An increase from 0.3% to 5.8% in IPA infections in patients admitted to intensive care units (ICUs) has been reported in recent years, and has been accompanied by a high mortality rate (50-70%) [27,28] This demonstrates the need for new anti-fungal drugs to combat Aspergillus infections
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