Journal: Journal of Virology
Article Title: DEAD-box helicase gcDDX56 disrupts IRF3 nuclear import complex and promotes nuclear IRF3 degradation for enhancing GCRV replication
doi: 10.1128/jvi.01654-25
Figure Lengend Snippet: Validation of gcKPNB3 silencing efficiency and subcellular/ total protein level analyses of gcIRF3 mediated by gcDDX56 and/or gcKPNB3. ( A ) qRT-PCR analysis of gcKPNB3 silencing efficiency in CIK cells transfected with si-gcKPNB3-1, −2, or −3. ** P < 0.01. ( B ) Nuclear levels of gcIRF3 mediated by gcDDX56 and/or gcKPNB3. ( C ) Cytoplasmic levels of gcIRF3 mediated by gcDDX56 and/or gcKPNB3. ( D ) Total protein levels of endogenous IRF3 mediated by gcDDX56 and/or gcKPNB3 in GCRV-infected cells (MOI = 1) with overexpression and/or knockdown of gcDDX56 and/or gcKPNB3. Tubulin (cytoplasmic) and HDAC1 (nuclear) served as fractionation controls; GAPDH as internal control. Endogenous IRF3 was detected with anti-IRF3 antibodies. Band intensities were quantified via Image J.
Article Snippet: The anti-HA rabbit polyclonal antibody (polyAb) (#51064-2-AP), anti-GAPDH mouse monoclonal antibody (mcAb) (#60004-1-Ig), and anti-Alpha Tubulin recombinant antibody (RecAb) (#80762-1-RR) were obtained from Proteintech.
Techniques: Biomarker Discovery, Quantitative RT-PCR, Transfection, Infection, Over Expression, Knockdown, Fractionation, Control