Endoplasmic reticulum protein homeostasis in Plasmodium

Protein homeostasis in the endoplasmic reticulum (ER) of Plasmodium refers to the coordinated activities of ER-resident chaperones, proteases, and enzymes that ensure correct folding, trafficking, and export of proteins during the parasite life cycle[2][5][6]. Key components include the ER chaperone BiP (PfHSP70-2), which maintains protein folding and assists in exporting virulence factors; the calcium-binding protein PfERC, essential for protease maturation and parasite egress; the protease plasmepsin V, which processes export signals for effector protein delivery; and ER acetyltransferases required for N-terminal acetylation. Disruption of ER protein homeostasis by stress, mutation, or inhibition induces unfolded protein response and can lead to parasite death, making components of this pathway attractive drug targets. However, the term as given ("Endoplasmic reticulum protein homeostasis in Plasmodium") is not scientifically precise for a single molecule or receptor; information should be mapped to individual proteins (e.g., PfHSP70-2, PfERC, plasmepsin V) for structured annotation[2][3][5][6][9].

Other names

ER stress response in PlasmodiumPlasmodium ER proteostasisPlasmodium ER protein quality controlPlasmodium unfolded protein response

Inhibition of ER chaperones disrupts parasite protein folding, induces lethal proteotoxic stress, and blocks parasite development[3][5]. Inhibition of ER proteases blocks protein export, reducing virulence factor delivery and parasite survival[6]. Modulation of unfolded protein response can reduce parasite fitness[1].