Open AccessBiogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target
Author(s) -
Moyersoen Juliette,
Choe Jungwoo,
Fan Erkang,
Hol Wim G.J.,
Michels Paul A.M.
Publication year - 2004
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1016/j.femsre.2004.06.004
Subject(s) - biogenesis , peroxisome , biology , organelle biogenesis , microbiology and biotechnology , trypanosoma brucei , microbody , organelle , biochemistry , computational biology , gene
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.