Protein disulfide isomerases (PDIs) negatively regulate ebolavirus structural glycoprotein expression in the endoplasmic reticulum (ER) via the autophagy-lysosomal pathway
Bin Wang, Jing Zhang, Xin Liu, Qingqing Chai, Xiaoran Lu, Xiaoyu Yao, Zhichang Yang, Liangliang Sun, Silas F. Johnson, Richard C. Schwartz, Yong‐Hui Zheng
Abstract
ebolavirus; sGP: soluble GP; SQSTM1/p62: sequestosome 1; ssGP: small soluble GP; TAFV: Taï Forest ebolavirus; TIZ: tizoxanide; TGN: thapsigargin; TLD: TXN (thioredoxin)-like domain; Ub: ubiquitin; UPR: unfolded protein response; VLP: virus-like particle; VSV: vesicular stomatitis virus; WB: Western blotting; WT: wild-type; XBP1: X-box binding protein 1.
Topics & Concepts
Endoplasmic reticulumBiologyEndoplasmic-reticulum-associated protein degradationCell biologyUnfolded protein responseEbolavirusProtein disulfide-isomeraseCalnexinAutophagyFoldaseCalreticulinEbola virusVirologyBiochemistryVirusApoptosisGroELEscherichia coliGeneViral Infections and Outbreaks ResearchViral Infections and VectorsMosquito-borne diseases and control