Isolation and Characterization of Functional Leishmania Major Virulence Factor UDP-galactopyranose Mutase

Abstract

Human parasitic pathogens of the genus Leishmania are the causative agents of cutaneous, mucocutaneous, and visceral leishmaniasis. Currently, there are millions of people infected with these diseases and over 50,000 deaths occur annually. Recently, it was shown that the flavin-dependent enzyme UDP-galactopyranose mutase (UGM) is a virulence factor in Leishmania major. UGM catalyzes the conversion of UDP-galactopyranose to UDP-galactofuranose. The product, UDP-galactofuranose, is the only source of galactofuranose which is present on the cell surface of this parasite and has been implicated to be important for host-parasite interactions. The recombinant form of this enzyme was obtained in a soluble and active form. The enzyme was shown to be active only in the reduced state. A kcat value of 5±0.2s-1 and a KM value of 87±11μM were determined with UDP-galactofuranose as the substrate. Different from the dimeric bacterial and tetrameric fungal UGMs, this parasitic enzyme functions as a monomer. © 2011.

Department(s)

Chemistry

Comments

National Institutes of Health, Grant R01GM094468

Keywords and Phrases

Flavoenzymes; Galactofuranose; Leishmaniasis; Non-redox reaction; UDP-galactopyranose mutase

International Standard Serial Number (ISSN)

1090-2104; 0006-291X

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2024 Elsevier, All rights reserved.

Publication Date

15 Apr 2011

PubMed ID

21419104

Link to Full Text

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