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Correction: Genome Instability & Disease (2022) 3:83–87 https://doi.org/10.1007/s42764-022-00064-3
In Fig. 1’s image caption, pATR distribution pattern displayed nuclear enlarged accumulations (red) in ASFV infected cells (green), should be corrected to: pATR distribution pattern displayed nuclear enlarged accumulations (red) in PRRSV infected cells (green);
Protein expression levels of specific DNA damage key sensor detected using phospho-specific antibodies ant-H2AX (Ser139) by western blot analysis, along a 60 h time-course of PRRSV-infected MARC-145 cells (MOI of 0.5), should be corrected to: Protein expression levels of specific DNA damage key sensor detected using phospho-specific antibodies anti-H2AX (Ser139) by western blot analysis, along a 60 h time-course of PRRSV-infected MARC-145 cells (MOI of 0.5);
Inhibition of ATR kinase activity induced by VE-821 at 20 µmM or ATM kinase activity induced by KU55933 at 10 µmM modulated PRRSV protein synthesis, should be corrected to: Inhibition of ATR kinase activity induced by VE-821 at 20 µM or ATM kinase activity induced by KU55933 at 10 µM modulated PRRSV protein synthesis.
The correct caption for Fig. 1 should be:
Fig. 1 ATM and ATR promote PRRSV replication in MARC-145 cells. a Effects of ATM, and ATR inhibitors on PRRSV replication in MARC-145 cells. MARC-145 cells were pretreated with different working concentrations of KU55933, AZD6738 and VE-821 for 2 h prior to PRRSV infection (MOI 0.5). As a control, cells were infected with the same dose of PRRSV without the inhibitor treatment. To determine if there were a synergistic effect between ATMi and ATRi during PRRSV infection, KU55933 and AZD6738 or VE-821 were added simultaneously in MARC-145 cells. PRRSV titers were determined on MARC-145 cells as TCID50 based on the Reed–Muench method at a different indicated timepoint. Statistical significance was evaluated by determining p-values. ns, p > 0.05; *p < 0.05; **p < 0.01, ***p < 0.001. b Protein expression levels of specific DNA damage key sensor detected using phospho-specific antibodies anti-H2AX (Ser139) by western blot analysis, along a 60 h time-course of PRRSV-infected MARC-145 cells (MOI of 0.5). Increased levels of H2AX phosphorylated forms were detected, starting at 8 h post-infection (hpi). PRRSV N protein expression was used as control for the viral infection time-course. β-actin expression was used as a loading control. c PRRSV infection elicits ATR and ATM pathway. Western blot analyses of ATM, ATR, phosphorylated ATM, phosphorylated ATR and γH2AX in PRRSV-infected MARC-145 cells are shown. MARC-145 cells were infected with PRRSV (MOI 0.5) at the indicated timepoints. Cells were lysed and analyzed by Western blot with specific antibodies. β-actin served as a loading control. Viral replication was confirmed by Western analysis of N protein with anti-PRRSV N monoclonal antibodies. d ATM or ATR inhibition by specific inhibitors disrupt PRRSV protein synthesis in MARC-145 cells. Inhibition of ATR kinase activity induced by VE-821 at 20 µM or ATM kinase activity induced by KU55933 at 10 µM modulated PRRSV protein synthesis. Expression levels of a N protein were severely reduced. Mock-infected cells were used as a control group in immunoblot analysis. e The interaction between ATR and PRRSV was analyzed by Co-immunoprecipitation. The lysate was subjected to immunoprecipitation with ATR or PRRSV N protein antibody, respectively. f PRRSV alters nuclear localization of ATR and ATM kinases hijacks the phosphorylated ATR to promote virus replication. pATR distribution pattern displayed nuclear enlarged accumulations (red) in PRRSV infected cells (green). DAPI stained nuclear DNA (blue). Mock-infected was used as negative control for ATR activation in immunofluorescence studies. Representative confocal images showing that PRRSV infection in MARC-145 cells. MARC-145 cells were mock-infected or infected with PRRSV (MOI 0.5). Cells were fixed and immunostained with specific antibodies at 48 hpi. Red represents ATR, pATR, ATM, ST/Q (phospho-ATM/ATR substrate) and γH2AX, green represents PRRSV(N), and blue (DAPI) represents cell nucleus. Scale bars = 5 μm
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Li, P., Xu, C., Zhang, X. et al. Correction: Single-stranded RNA viruses activate and hijack host apical DNA damage response kinases for efficient viral replication. GENOME INSTAB. DIS. 5, 48–49 (2024). https://doi.org/10.1007/s42764-024-00121-z
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DOI: https://doi.org/10.1007/s42764-024-00121-z