The Wolbachia endosymbiont of Brugia malayi has an active phosphoglycerate mutase: a candidate target for anti-filarial therapies

Parasitol Res. 2009 Apr;104(5):1047-52. doi: 10.1007/s00436-008-1287-7. Epub 2008 Nov 29.


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, wBm-iPGM 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 wBm-iPGM showed typical PGM activity. Our results provide a foundation for further development of wBm-iPGM as a promising new drug target for novel anti-filarial therapies that selectively target the endosymbiont.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Brugia malayi / microbiology*
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Gene Expression
  • Kluyveromyces / genetics
  • Molecular Sequence Data
  • NAD / metabolism
  • Phosphoglycerate Mutase / genetics*
  • Phosphoglycerate Mutase / isolation & purification
  • Phosphoglycerate Mutase / metabolism*
  • Sequence Alignment
  • Wolbachia / enzymology*
  • Wolbachia / genetics


  • Bacterial Proteins
  • NAD
  • Phosphoglycerate Mutase