Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation - Huang, Wei-Ru; Li, Jyun-Yi; Liao, Tsai-Ling; Yeh, Chuan-Ming; Wang, Chi-Young; Wen, Hsiao-Wei; Hu, Nien-Jen; Wu, Yi-Ying; Hsu, Chao-Yu; Chang, Yu-Kang; Chang, Ching-Dong; Nielsen, Brent L.; et al. (Veterinary microbiology, 2022)
Keywords: Animals; Avian orthoreovirus; Avian reovirus; Capsid protein; Capsid Proteins - metabolism; Chaperonin Containing TCP-1 - metabolism; Chaperonins; Core protein; fluorescent antibody technique; Immunofluorescence; Immunoprecipitation; Non-structural protein Σns; Orthoreovirus, Avian - genetics; Outer and core proteins (σC and σA); poultry; Poultry farming; precipitin tests; proteasome endopeptidase complex; Proteasome Endopeptidase Complex - metabolism; Proteasomes; Proteins; Replication; RNA-Binding Proteins - metabolism; The eukaryotic chaperonin T-complex protein-1 (TCP-1) ring complex (TRiC); Ubiquitin; Ubiquitin - metabolism; Viral Core Proteins - metabolism; viral nonstructural proteins; Viral Proteins - metabolism; Viral Regulatory and Accessory Proteins - metabolism; virus replication; Virus Replication - genetics; Viruses; HIV-1; Non-structural protein Σns; SDS; Hsp; Vero; ARV; MOI; CDK; DMRT; Avian reovirus; DMEM; Outer and core proteins (σC and σA); CCT; HEPES; HSF1A; The eukaryotic chaperonin T-complex protein-1 (TCP-1) ring complex (TRiC); TCP-1; PCR; MDRV; TRiC