Characterization of the malaria parasite <i>Plasmodium falciparum</i> Tepsin homolog.

ABSTRACT: Plasmodium parasites rely on the invasion of human erythrocytes for their survival. This invasion process is facilitated by specialized organelles (rhoptry, micronemes, and dense granules) housed within a distinctive structure known as the apical complex. How the apical complex is generated is still enigmatic, especially how specificity is achieved in the vesicular trafficking between the Golgi apparatus and the apical organelles, but phosphoinositide lipids might potentially be involved. Here, we describe the characterization of a putative phosphoinositide-binding protein containing an Epsin NH₂-terminal homology (ENTH) domain, Pf3D7_1459600. We show that this protein is structurally homologous to human Tepsin. Surprisingly, unlike other Tepsins, the ENTH domain of PfTep

SUBMITTER: Roucheray S 

PROVIDER: S-EPMC12323583 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature