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Quantitative Proteomics Analysis of PDI8 Depletion in Toxoplasma gondii

ABSTRACT: Protein disulfide isomerase, containing thioredoxin (Trx) domains, serves as a vital enzyme responsible for oxidative protein folding (the formation, reduction, and isomerization of disulfide bonds in newly synthesized proteins) in the endoplasmic reticulum (ER). In this study, we identified TgPDI8, an ER-localized PDI protein in Toxoplasma gondii. Conditional knockdown of TgPDI8 resulted in a significant growth defect. To investigate the impact of TgPDI8 on protein expression, we assessed proteomic changes following the knockdown of TgPDI8.

ORGANISM(S): Toxoplasma Gondii Rh-88

SUBMITTER: Hongjuan Peng

PROVIDER: PXD053468 | iProX | Fri Jun 28 00:00:00 BST 2024

REPOSITORIES: iProX

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Protein disulfide isomerase PDI8 is indispensable for parasite growth and associated with secretory protein processing in <i>Toxoplasma gondii</i>.

Wang Chaoyue C Sun Pei P Jia Yonggen Y Tang Xinming X Liu Xianyong X Suo Xun X Peng Hongjuan H

mBio 20240820 9

Protein disulfide isomerase, containing thioredoxin (Trx) domains, serves as a vital enzyme responsible for oxidative protein folding (the formation, reduction, and isomerization of disulfide bonds in newly synthesized proteins) in the endoplasmic reticulum (ER). However, the role of ER-localized PDI proteins in parasite growth and their interaction with secretory proteins remain poorly understood. In this study, we identified two ER-localized PDI proteins, TgPDI8 and TgPDI6, in <i>Toxoplasma go ...[more]

PMID: 39162526

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