This article is a correction to:
gga-miR-155 Enhances Type I Interferon Expression and Suppresses Infectious Burse Disease Virus Replication via Targeting SOCS1 and TANK
Bin Wang1,2,3
Mengjiao Fu1,2,3
Yanan Liu1,2,3Yongqiang Wang1,2,3Xiaoqi Li3Hong Cao1,2,3
Shijun J. Zheng1,2,3*- 1State Key Laboratory of Agrobiotechnology and College of Veterinary Medicine, China Agricultural University, Beijing, China
- 2Key Laboratory of Animal Epidemiology of the Ministry of Agriculture, China Agricultural University, Beijing, China
- 3Department of Preventive Veterinary Medicine, College of Veterinary Medicine, China Agricultural University, Beijing, China
A Corrigendum on
gga-miR-155 Enhances Type I Interferon Expression and Suppresses Infectious Burse Disease Virus Replication via Targeting SOCS1 and TANK
by Wang, B., Fu, M., Liu, Y., Wang, Y., Li, X., Cao, H, et al. (2018). Front. Cell. Infect. Microbiol. 8:55. doi: 10.3389/fcimb.2018.00055
In the original article, there was an error as Figueroa et al. 2016 was not cited. A correction has been made to the Results section, subsection gga-miR-155 directly targets SOCS1 and TANK:
“Using TargetScan and miRanda prediction softwares, we found two putative gga-miR-155 targeted genes SOCS1 and TANK that likely modulate type I IFN signaling in DF-1 cells. Our result verified previous studies where SOCS1 was identified as a gga-mIR-155 target (Figueroa et al., 2016). It is well-known that SOCS1 and TANK are two negative regulators in immune response (Dai et al., 2006; Kawagoe et al., 2009; Fujimoto and Naka, 2010; Huang et al., 2015). Thus, it is logical to examine the effect of gga-miR-155 on the expressions of these two potential target molecules. To examine whether gga-miR-155 directly target seed regions in SOCS1 and TANK as predicted, we constructed firefly luciferase reporter pGL3-3′UTR-WT (SOCS1) and pGL3-3′UTR-WT (TANK) containing the predicted target site in the 3′UTR, and four mutant vectors pGL3-3′UTR-Mut (SOCS1), pGL3-3′UTR-Mut1 (TANK), pGL3-3′UTR-Mut2 (TANK) and pGL3-3′UTR-Mut1,2 (TANK) with mutations of four nucleotides in the seed region (Figure 5A), and transfected DF-1 cells with these reporter gene plasmids and miRNA mimics. We found that gga-miR-155 significantly inhibited the luciferase activities of pGL3-3′UTR-WT (SOCS1) and pGL3-3′UTR-WT (TANK), but not pGL3-3′UTR-Mut (SOCS1) or pGL3-3′UTR-Mut (TANK) (Figures 5B,C). To rule out the possibility that gga-miR-155 might have potential target sites in IBDV genomic RNA, we examined the IBDV genomic RNA sequence and found a predicted target in IBDV Lx strain vp4 gene using targetScan and miRanda. However, gga-miR-155 didn't have any effect on luciferase activity of pGL3-3′UTR-WT (vp4) (Figure 5D). Furthermore, overexpression of gga-miR-155 reduced the expressions of SOCS1 and TANK by around 2 folds in cells at both mRNA and protein levels (Figures 6A–D). It was previously found that gga-miR-155 targets SOCS1 (Figueroa et al., 2016), and our data not only confirmed this finding but also indicated the involvement of gga-miR-155 in targeting another host protein TANK. Thus, both SOCS1 and TANK are targeted and regulated by gga-miR-155.”
Secondly, the first sentence of the Discussion section, paragraph 3 was rephrased in order to clarify its meaning:
“The interaction between hsa-miR-155 and SOCS1 has been reported in mammalian cells (Jiang et al., 2010), and gga-miR-155 has been previously shown to target SOCS1 (Figueroa et al., 2016). However, gga-miR-155's targeting chicken SOCS1 still needs to be testified, considering that similarity of amino acid sequences of chicken SOCS1 (GenBank accession no. NM001137648.1) with human SOCS1 (GenBank accession no. DQ086801.1) is only around 60.6%. Our data show that gga-miR-155 markedly suppressed SOCS1 expression. TANK plays versatile roles in innate immune signaling. On one hand, TANK serves as an adaptor bridging TRAF3 with TBK1 and IKKϵ, which promotes phosphorylation and activation of IRF3/IRF7 as well as induction of NF-κB activation, leading to efficient type I IFN production (Guo and Cheng, 2007; Ryzhakov and Randow, 2007). On the other hand, TANK has also been shown to act as a negative regulator of Toll-like receptor (TLRs) (Kawagoe et al., 2009; Wang et al., 2015). In this study, our data show that TANK serves as a negative regulator for type I interferon expression in chicken cells.”
Also, the type of primer used for SOCS1 RT-qPCR was missing. The correct ones were synthesized by Sangon Biotech. A correction has been made to the Materials and Methods section, subsection RNA isolation and quantitative real-time PCR (qRT-PCR) analysis:
“Total RNA and miRNA were prepared from DF-1 cells using EASYspin Plus kit or RNA mini kit (aidlab Biotechnology, China) per the manufacturer's instructions. mRNAs were reversely transcribed with primescriptTM RT Reagent kit (Takara). Quantitative RT-PCR analysis was performed using Tli RnaseH Plus (Takara) on LightCycler 480II (Roche, USA). Specific primers for chicken IFN-α (chIFN-α) (5′-CCA GCA CCT CGA GCA AT-3′ and 5′-GGC GCT GTA ATC GTT GTC T-3′), chicken IFN-β (chIFN-β) (5′-GCC TCC AGC TCC TTC AGA ATA CG-3′ and 5′-CTG GAT CTG GTT GAG GAG GCT GT-3′), chicken IRF3 (chIF3) (5′-GCT CTC TGA CTC TTT CAA CCT CTT-3′ and 5′-AAT GCT GCT CTT TTC TCC TCT G-3′), and chicken GAPDH (5′-TGC CAT CAC AGC CAC ACA GAA G-3′ and 5′-ACT TTC CCC ACA GCC TTA GCA G-3′) were designed with reference to previous publications (Li et al., 2007; Abdul-Careem et al., 2008; Liu et al., 2010). Specific primers for chicken SOCS1 (5′- CTC GCA AGC GGA TTT CAG TAG-3′, 5′- GGG CTC AGA CTT CAG CTT CTC-3′) were designed and synthesized by Sangon Biotech (Shanghai, China). GAPDH gene was utilized as the reference gene. All quantitative real-time PCR experiments were performed in triplicate. The PCR was performed in a 20 μl volume containing 1 μl of cDNA, 10 μl of 2 × SYBR green Premix Ex Taq (TaKaRa), and a 0.4 μM of each gene-specific primers. Thermal cycling parameters were as follows: 94°C for 2 min; 40 cycles of 94°C for 20 s, 55°C for 20 s, and 72°C for 20 s; and 1 cycle of 95°C for 30 s, 60°C for 30 s, and 95°C for 30 s. The final step was to obtain a melt curve for the PCR products to determine the specificity of the amplification. qRT-PCR analysis of gga-miR-155 was performed with RT-PCR Quantitation Kit (GenePharma, China).”
Finally, the source of the SOCS1 antibody was also missing. A correction has been made to the Materials and Methods section, subsection Western Blot analysis:
“Chicken socs1 gene was cloned from DF-1 cells using the specific primes 5′- CGC GGA TCC ATG GTA GCG CAC AGC AAG GTG-3′ (sense), and 5′- ACG CGT CGA CG TTA GAT CTG AAA CGG GAA GGA-3′ (anti-sense) with reference to the sequence in GenBank (accession no.NM_001137648.1). Chicken socs1 gene was then subcloned into pET-28a vector. The pET-28a-socs1 recombinant plasmid was used to transform E. coli BL21, and SOCS1-his recombinant protein was expressed at 37°C and purified by a protein purification kit (Ni Sepharose™ 6 Fast Flow, GE Company, USA) per the manufacturer's instructions. To develop polyclonal antibody against SOCS1, BALB/c mice were immunized with SOCS1-his recombinant protein. After immunization, anti-SOCS1 polyclonal antibody was obtained from the sera of BALB/c mice vaccinated with SOCS1-his recombinant protein. For detection of TANK in DF-1 cells, cell lysates were prepared using a non-denaturing lysis buffer (50 nM Tris-HCl, pH 8.0, 150 nM NaCl, 1% TritonX-100, 5 nM EDTA, 10% glycerol, 10 nM dithiothreitol, 1 × complete cocktail protease inhibitor). The cell lysates were boiled with 6 × SDS loading buffer for 10 min and fractionated by electrophoresis on 12% SDS-polyacrylamide gels, and resolved proteins were transferred onto polyvinylidene difluoride (PVDF) membranes. After blocking with 5% skimmed milk, the membranes were incubated with anti-TANK or anti-GAPDH antibody, followed by HRP-conjugated anti-Mouse secondary antibody. Blots were developed using an enhanced chemiluminesence (ECL) kit per the manufacturer's instruction.”
The authors apologize for these errors and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.
References
Abdul-Careem, M. F., Hunter, B. D., Lee, L. F., Fairbrother, J. H., Haghighi, H. R., Read, L., et al. (2008). Host responses in the bursa of Fabricius of chickens infected with virulent Marek's disease virus. Virology 379, 256–265. doi: 10.1016/j.virol.2008.06.027
Dai, X., Sayama, K., Yamasaki, K., Tohyama, M., Shirakata, Y., Hanakawa, Y., et al. (2006). SOCS1-negative feedback of STAT1 activation is a key pathway in the dsRNA-induced innate immune response of human keratinocytes. J. Invest. Dermatol. 126, 1574–1581. doi: 10.1038/sj.jid.5700294
Figueroa, T., Boumart, I., Coupeau, D., and Rasschaert, D. (2016). Hyperediting by ADAR1 of a new herpesvirus lncRNA during the lytic phase of the oncogenic Marek's disease virus. J. Gen. Virol. 97, 2973–2988. doi: 10.1099/jgv.0.000606
Fujimoto, M., and Naka, T. (2010). SOCS1, a Negative Regulator of Cytokine Signals and TLR Responses, in Human Liver Diseases. Gastroenterol. Res. Pract. 2010:470468. doi: 10.1155/2010/470468
Guo, B., and Cheng, G. (2007). Modulation of the interferon antiviral response by the TBK1/IKKi adaptor protein TANK. J. Biol. Chem. 282, 11817–11826. doi: 10.1074/jbc.M700017200
Huang, L., Liu, Q., Zhang, L., Zhang, Q., Hu, L., Li, C., et al. (2015). Encephalomyocarditis Virus 3C Protease Relieves TRAF Family Member-associated NF-kappaB Activator (TANK) Inhibitory Effect on TRAF6-mediated NF-kappaB Signaling through Cleavage of TANK. J. Biol. Chem. 290, 27618–27632. doi: 10.1074/jbc.M115.660761
Jiang, S., Zhang, H. W., Lu, M. H., He, X. H., Li, Y., Gu, H., et al. (2010). MicroRNA-155 functions as an OncomiR in breast cancer by targeting the suppressor of cytokine signaling 1 gene. Cancer Res. 70, 3119–3127. doi: 10.1158/0008-5472.CAN-09-4250
Kawagoe, T., Takeuchi, O., Takabatake, Y., Kato, H., Isaka, Y., Tsujimura, T., et al. (2009). TANK is a negative regulator of Toll-like receptor signaling and is critical for the prevention of autoimmune nephritis. Nat. Immunol. 10, 965–972. doi: 10.1038/ni.1771
Li, Y. P., Handberg, K. J., Juul-Madsen, H. R., Zhang, M. F., and Jorgensen, P. H. (2007). Transcriptional profiles of chicken embryo cell cultures following infection with infectious bursal disease virus. Arch. Virol. 152, 463–478. doi: 10.1007/s00705-006-0878-9
Liu, H., Zhang, M., Han, H., Yuan, J., and Li, Z. (2010). Comparison of the expression of cytokine genes in the bursal tissues of the chickens following challenge with infectious bursal disease viruses of varying virulence. Virol. J. 7:364. doi: 10.1186/1743-422X-7-364
Ryzhakov, G., and Randow, F. (2007). SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK. EMBO J. 26, 3180–3190. doi: 10.1038/sj.emboj.7601743
Wang, W., Huang, X., Xin, H. B., Fu, M., Xue, A., and Wu, Z. H. (2015). TRAF Family Member-associated NF-kappaB Activator (TANK) Inhibits Genotoxic Nuclear Factor kappaB Activation by Facilitating Deubiquitinase USP10-dependent Deubiquitination of TRAF6 Ligase. J. Biol. Chem. 290, 13372–13385. doi: 10.1074/jbc.M115.643767
Keywords: microRNA, type I IFN, IBDV, SOCS, TANK
Citation: Wang B, Fu M, Liu Y, Wang Y, Li X, Cao H and Zheng SJ (2020) Corrigendum: gga-miR-155 Enhances Type I Interferon Expression and Suppresses Infectious Burse Disease Virus Replication via Targeting SOCS1 and TANK. Front. Cell. Infect. Microbiol. 10:324. doi: 10.3389/fcimb.2020.00324
Received: 26 September 2019; Accepted: 28 May 2020;
Published: 15 July 2020.
Edited and reviewed by: Santanu Bose, Washington State University, United States
Copyright © 2020 Wang, Fu, Liu, Wang, Li, Cao and Zheng. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
*Correspondence: Shijun J. Zheng, sjzheng@cau.edu.cn