Eukaryotic translation initiation factor 5A and its posttranslational modifications play an important role in proliferation and potentially in differentiation of the human enteric protozoan parasite Entamoeba histolytica

The eukaryotic translation initiation factor 5A (eIF5A) is a highly conserved protein and essential in all eukaryotes. However, the specific roles of eIF5A other biological processes remain elusive. In present study, we described role eIF5A, its posttranslational modifications (PTM), biosynthetic pathway needed for PTM Entamoeba histolytica , protozoan parasite responsible amoebic dysentery liver abscess humans. E . encodes two isotypes enzymes, deoxyhypusine synthase (DHS), their PTM. Both are functional, whereas only one DHS (EhDHS1, but not EhDHS2), catalytically active. activity increased ~2000-fold when EhDHS1 was co-expressed with EhDHS2 Escherichia coli suggesting that formation heteromeric complex full enzymatic activity. 2 genes were required vitro growth trophozoites, indicated by small antisense RNA-mediated gene silencing. eIF5A2 eIF5A1 actively transcribed. Gene silencing caused compensatory induction expression gene, interchangeable also reinforcing importance eIF5As proliferation survival. Furthermore, using sibling species, invadens found upregulated during excystation, while downregulated, plays an important differentiation. Taken together, these results have underscored essentiality DHS, potentially differentiation this parasite, suggest hypusination associated represents novel rational target drug development against amebiasis.