| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6292188 | Experimental Parasitology | 2011 | 6 Pages |
Aspartic proteases are important virulence factors for pathogens and are recognized as attractive drug targets. Seven aspartic proteases (ASPs) have been identified in Toxoplasma gondii genome. Bioinformatics and phylogenetic analyses regroup them into five monophyletic groups. Among them, TgASP1, a coccidian specific aspartic protease related to the food vacuole plasmepsins, is associated with the secretory pathway in non-dividing cells and relocalizes in close proximity to the nascent inner membrane complex (IMC) of daughter cells during replication. Despite a potential role for TgASP1 in IMC formation, the generation of a conventional knockout of the TgASP1 gene revealed that this protease is not required for T. gondii tachyzoite survival or for proper IMC biogenesis.
Graphical abstractTgASPl is not indispensable for Toxoplasma gondii tachyzoites in vitro development.Download full-size imageHighlights⺠In this study, we examine the function of an aspartic protease, ASP1, in Toxoplasma gondii. ⺠TgASP1 is not essential for tachyzoites stages. ⺠TgASP1 substrate and function still need to be elucidated.
