Biogenesis of peroxisomes and glycosomes: Trypanosomatid glycosome assembly is a promising new drug target

Juliette Moyersoen, Jungwoo Choe, Erkang Fan, Wim G.J. Hol, Paul A.M. Michels

Research output: Contribution to journalReview articlepeer-review

91 Scopus citations


In trypanosomatids (Trypanosoma and Leishmania), protozoa responsible for serious diseases of mankind in tropical and subtropical countries, core carbohydrate metabolism including glycolysis is compartmentalized in peculiar peroxisomes called glycosomes. Proper biogenesis of these organelles and the correct sequestering of glycolytic enzymes are essential to these parasites. Biogenesis of glycosomes in trypanosomatids and that of peroxisomes in other eukaryotes, including the human host, occur via homologous processes involving proteins called peroxins, which exert their function through multiple, transient interactions with each other. Decreased expression of peroxins leads to death of trypanosomes. Peroxins show only a low level of sequence conservation. Therefore, it seems feasible to design compounds that will prevent interactions of proteins involved in biogenesis of trypanosomatid glycosomes without interfering with peroxisome formation in the human host cells. Such compounds would be suitable as lead drugs against trypanosomatid-borne diseases.

Original languageEnglish
Pages (from-to)603-643
Number of pages41
JournalFEMS Microbiology Reviews
Issue number5
StatePublished - Nov 2004


  • Drug design
  • Glycosome and peroxisome biogenesis
  • Peroxin
  • Protein-protein interaction
  • Trypanosomatids


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