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Protein disulfide isomerase PDI8 is indispensable for parasite growth and associated with secretory protein processing in Toxoplasma gondii
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Protein disulfide isomerase PDI8 is indispensable for parasite growth and associated with secretory protein processing in Toxoplasma gondii
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Journal Article
Protein disulfide isomerase PDI8 is indispensable for parasite growth and associated with secretory protein processing in Toxoplasma gondii
2024
Overview
Apicomplexans, a phylum of intracellular parasites, encompass various zoonotic pathogens, including Plasmodium , Cryptosporidium , Toxoplasma , and Babesia , causing a significant economic burden on human populations. These parasites exhibit hypersensitivity to disruptions in endoplasmic reticulum (ER) redox homeostasis, necessitating the presence of ER-localized thioredoxin (Trx) superfamily proteins, particularly protein disulfide isomerase (PDI), for proper oxidative folding. However, the functional characteristics of ER-localized PDI proteins in Toxoplasma gondii remain largely unexplored. In this study, we identified two ER-localized proteins, namely, TgPDI8 and TgPDI6, and demonstrated the indispensable role of TgPDI8 in parasite survival. Through a comprehensive multi-omics analysis, we elucidated the crucial role of TgPDI8 in the processing of secretory proteins in T. gondii . Additionally, we introduced a novel ER-anchored TurboID method to label and identify canonical secretory proteins in T. gondii . This research opens up new avenues for understanding oxidative folding and the secretory pathway in apicomplexan parasites, laying the groundwork for future advancements in antiparasitic drug development.
Publisher
American Society for Microbiology
Subject
/ CRISPR
/ Endoplasmic Reticulum - metabolism
/ Genetics and Molecular Biology
/ Genomes
/ Humans
/ invasion
/ Protein Disulfide-Isomerases - genetics
/ Protein Disulfide-Isomerases - metabolism
/ Protozoa
/ Protozoan Proteins - genetics
/ Protozoan Proteins - metabolism
