The nepenthesin insert in the Plasmodium falciparum aspartic protease plasmepsin V is necessary for enzyme function.

ABSTRACT: Plasmepsin V (PM V) is a pepsin-like aspartic protease essential for growth of the malarial parasite Plasmodium falciparum. Previous work has shown PM V to be an endoplasmic reticulum-resident protease that processes parasite proteins destined for export into the host cell. Depletion or inhibition of the enzyme is lethal during asexual replication within red blood cells as well as during the formation of sexual stage gametocytes. The structure of the Plasmodium vivax PM V has been characterized by X-ray crystallography, revealing a canonical pepsin fold punctuated by structural features uncommon to secretory aspartic proteases; however, the function of this unique structure is unclear. Here, we used parasite genetics to probe these structural features by attempting to rescue lethal PM V de

SUBMITTER: Polino AJ 

PROVIDER: S-EPMC9478907 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature