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- Title
The Wolbachia endosymbiont of Brugia malayi has an active phosphoglycerate mutase: a candidate target for anti-filarial therapies.
- Authors
Jeremy Foster; Sylvine Raverdy; Mehul Ganatra; Paul Colussi; Christopher Taron; Clotilde Carlow
- Abstract
Abstract  Phosphoglycerate mutases (PGM) interconvert 2- and 3-phosphoglycerate in the glycolytic and gluconeogenic pathways. A putative cofactor-independent phosphoglycerate mutase gene (iPGM) was identified in the genome sequence of the Wolbachia endosymbiont from the filarial nematode, Brugia malayi (wBm). Since iPGM has no sequence or structural similarity to the cofactor-dependent phosphoglycerate mutase (dPGM) found in mammals, it may represent an attractive Wolbachia drug target. In the present study, wBmâiPGM cloned and expressed in Escherichia coli was mostly insoluble and inactive. However, the protein was successfully produced in the yeast Kluyveromyces lactis and the purified recombinant wBmâiPGM showed typical PGM activity. Our results provide a foundation for further development of wBmâiPGM as a promising new drug target for novel anti-filarial therapies that selectively target the endosymbiont.
- Subjects
WOLBACHIA; ENZYMES; ENDOSYMBIOSIS; FILARIAL worms; NEMATODE control; NUCLEOTIDE sequence; MOLECULAR cloning; ESCHERICHIA coli
- Publication
Parasitology Research, 2009, Vol 104, Issue 5, p1047
- ISSN
0932-0113
- Publication type
Article
- DOI
10.1007/s00436-008-1287-7