Abstract
Endoplasmic reticulum stress (ER stress) can be induced when cellular protein homeostasis is damaged, and cells can activate the unfolded protein response (UPR) to restore protein homeostasis or induce cell death to facilitate the survival of the whole system. Globally, parasites are a constant threat to human health and are therefore considered a serious public health problem. Parasitic infection can cause ER stress in host cells, and parasites also possess part or all of the UPR under ER stress conditions. In this review, we aim to clarify the role of ER stress pathways and related molecules in parasites for their survival and development, the pathogenesis of parasitosis in hosts, and the artemisinin resistance of Plasmodium, which provides some potential drug design targets to inhibit survival of parasites, relieves pathological damage of parasitosis, and solves the problem of artemisinin resistance.
Highlights
Specialty section: This article was submitted to Infectious Diseases, a section of the journal Frontiers in Microbiology
Ran et al further indicated that rhoptry protein 18 (ROP18) induced apoptosis of neural cells by phosphorylating reticulon 1-C [RTN1-C, a protein localized in the endoplasmic reticulum (ER) that is preferentially expressed in the neural cells of the central nervous system (CNS) at Ser7/134 and Thr4/8/118], which led to the acetylation of Glucose-regulated proteins 78 (GRP78) and induced ER stress (An et al, 2018)
Alleviating the symptoms of malaria, preventing the recurrence of Plasmodium and inhibit the transmission of this disease; Inhibiting the invasion, replication and differentiation of T. gondii Leading to the death of chloroquine-sensitive and -resistant P. falciparum strains Kill parasites (The parasite is more susceptible to ER stress than host due to the mere presence of the protein kinase RNA-like ER kinase (PERK) pathway); Participating in the formation of P. falciparum gametophytes and the conversion of the P. berghei; Inducing programmed cell death of T. brucei; Inducing apoptosis or autophagy of T. gondii; Inhibiting the differentiation of T. gondii from tachyzoite to bradyzoite cysts; Inducing the apoptosis of Leishmania major Inhibiting the survival of parasites
Summary
The endoplasmic reticulum (ER), a vital organelle in eukaryotic cells, is the site of synthesis and processing of membrane and secretory proteins, synthesis of lipids, and storage of Ca2+ (Dolai and Adak, 2014). Many factors influence the protein homeostasis of ER, such as plasma cell differentiation (Gass et al, 2002), tunicamycin (Pahl and Baeuerle, 1995), and parasite infection (Galluzzi et al, 2017) which result in accumulated misfolded or unfolded proteins that exceed the folding capacity of ER and trigger endoplasmic reticulum stress (ER stress). Endoplasmic reticulum-associated degradation (ERAD) and unfolded protein response (UPR) are the two major quality control processes of ER stress (Bukau et al, 2006). After dissociation from Bip, IRE1α will be activated by forming IRE1α
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