Plasmepsin V gives plasmodium license to kill

When mosquitoes develop in the erythrocytes, they employ hundreds of their protein to terrorize a red blood cell. These proteins then change the mechanics of the cytoskeleton, the way nutrients are taken in by the RBC and also they alter its mechanical stability. 

Proteins destined for export are synthesized in the endoplasmic reticulum (ER) and cleaved at a conserved (PEXEL) motif, which allows translocation into the host cell via an ATP-driven translocon called the PTEX complex. We report that plasmepsin V, an ER aspartic protease with distant homology to the mammalian processing enzyme BACE, recognizes the PEXEL motif and cleaves it at the correct site. This enzyme is essential for parasite viability and ER residence is essential for its function. We propose that plasmepsin V is the PEXEL protease and is an attractive enzyme for antimalarial drug development.

 

 Research paper

Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte

Ilaria Russo^1,2, Shalon Babbitt^1,3, Vasant Muralidharan^1,3, Tamira Butler¹, Anna Oksman¹ & Daniel E. Goldberg¹