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4. BECN1-dependent CASP2 incomplete autophagy induction by binding to rabies virus phosphoprotein

Author

Liu, Juan, Wang, Hailong, Gu, Jinyan, Deng, Tingjuan, Yuan, Zhuangchuan, Hu, Boli, Xu, Yunbin, Yan, Yan, Zan, Jie, Liao, Min, DiCaprio, Erin, Li, Jianrong, Su, Shuo, and Zhou, Jiyong

Subjects
Biochemistry and Cell Biology, Biological Sciences, Biodefense, Emerging Infectious Diseases, Prevention, Infectious Diseases, Vaccine Related, Infection, Good Health and Well Being, Animals, Autophagosomes, Autophagy, Beclin-1, Caspase 2, Mice, Models, Biological, Molecular Chaperones, Phosphoproteins, Proto-Oncogene Proteins c-akt, Rabies, Rabies virus, Signal Transduction, TOR Serine-Threonine Kinases, Viral Structural Proteins, Virus Replication, autophagy, BECN1, CASP2-dependent pathway, RABV, viral protein P, Biochemistry & Molecular Biology, Biochemistry and cell biology
Abstract

Autophagy is an essential component of host immunity and used by viruses for survival. However, the autophagy signaling pathways involved in virus replication are poorly documented. Here, we observed that rabies virus (RABV) infection triggered intracellular autophagosome accumulation and results in incomplete autophagy by inhibiting autophagy flux. Subsequently, we found that RABV infection induced the reduction of CASP2/caspase 2 and the activation of AMP-activated protein kinase (AMPK)-AKT-MTOR (mechanistic target of rapamycin) and AMPK-MAPK (mitogen-activated protein kinase) pathways. Further investigation revealed that BECN1/Beclin 1 binding to viral phosphoprotein (P) induced an incomplete autophagy via activating the pathways CASP2-AMPK-AKT-MTOR and CASP2-AMPK-MAPK by decreasing CASP2. Taken together, our data first reveals a crosstalk of BECN1 and CASP2-dependent autophagy pathways by RABV infection.

Published
2017

12. TRAF6 autophagic degradation by avibirnavirus VP3 inhibits antiviral innate immunity via blocking NFKB/NF-κB activation

Author

Deng, Tingjuan, Hu, Boli, Wang, Xingbo, Ding, Shuxiang, Lin, Lulu, Yan, Yan, Peng, Xiran, Zheng, Xiaojuan, Liao, Min, Jin, Yulan, Dong, Weiren, Gu, Jinyan, and Zhou, Jiyong

Subjects
viruses, Cell Biology, Molecular Biology
Abstract

Ubiquitination is an important reversible post-translational modification. Many viruses hijack the host ubiquitin system to enhance self-replication. In the present study, we found that Avibirnavirus VP3 protein was ubiquitinated during infection and supported virus replication by ubiquitination. Mass spectrometry and mutation analysis showed that VP3 was ubiquitinated at residues K73, K135, K158, K193, and K219. Virus rescue showed that ubiquitination at sites K73, K193, and K219 on VP3 could enhance the replication abilities of infectious bursal disease virus (IBDV), and that K135 was essential for virus survival. Binding of the zinc finger domain of TRAF6 (TNF receptor associated factor 6) to VP3 mediated K11- and K33-linked ubiquitination of VP3, which promoted its nuclear accumulation to facilitate virus replication. Additionally, VP3 could inhibit TRAF6-mediated NFKB/NF-κB (nuclear factor kappa B) activation and IFNB/IFN-β (interferon beta) production to evade host innate immunity by inducing TRAF6 autophagic degradation in an SQSTM1/p62 (sequestosome 1)-dependent manner. Our findings demonstrated a macroautophagic/autophagic mechanism by which Avibirnavirus protein VP3 blocked NFKB-mediated IFNB production by targeting TRAF6 during virus infection, and provided a potential drug target for virus infection control. Abbreviations: ATG: autophagy related; BafA1: bafilomycin A1; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; Cas9: CRISPR-associated protein 9; CHX: cycloheximide; Co-IP: co-immunoprecipitation; CRISPR: clustered regularly interspaced short palindromic repeats; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GST: glutathione S-transferase; IBDV: infectious bursal disease virus; IF: indirect immunofluorescence; IFNB/IFN-β: interferon beta; mAb: monoclonal antibody; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MOI: multiplicity of infection; MS: mass spectrometry; NFKB/NF-κB: nuclear factor kappa B; NBR1: NBR1 autophagy cargo receptor; OPTN: optineurin; pAb: polyclonal antibody; PRRs: pattern recognition receptors; RNF125: ring finger protein 125; RNF135/Riplet: ring finger protein 135; SQSTM1/p62: sequestosome 1; TAX1BP1: tax1 binding protein1; TCID50: 50% tissue culture infective dose; TRAF3: TNF receptor associated factor 3; TRAF6: TNF receptor associated factor 6; TRIM25: tripartite motif containing 25; Ub: ubiquitin; Wort: wortmannin; WT: wild type.

Published
2022
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13. TRAF6 autophagic degradation by avibirnavirus VP3 inhibits antiviral innate immunity via blocking NFKB/NF-κB activation

Author

Deng, Tingjuan, primary, Hu, Boli, additional, Wang, Xingbo, additional, Ding, Shuxiang, additional, Lin, Lulu, additional, Yan, Yan, additional, Peng, Xiran, additional, Zheng, Xiaojuan, additional, Liao, Min, additional, Jin, Yulan, additional, Dong, Weiren, additional, Gu, Jinyan, additional, and Zhou, Jiyong, additional

Published
2022
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17. TRAF6 autophagic degradation by avibirnavirusVP3 inhibits antiviral innate immunity via blocking NFKB/NF-κB activation

Author

Deng, Tingjuan, Hu, Boli, Wang, Xingbo, Ding, Shuxiang, Lin, Lulu, Yan, Yan, Peng, Xiran, Zheng, Xiaojuan, Liao, Min, Jin, Yulan, Dong, Weiren, Gu, Jinyan, and Zhou, Jiyong

Abstract

ABSTRACTUbiquitination is an important reversible post-translational modification. Many viruses hijack the host ubiquitin system to enhance self-replication. In the present study, we found that AvibirnavirusVP3 protein was ubiquitinated during infection and supported virus replication by ubiquitination. Mass spectrometry and mutation analysis showed that VP3 was ubiquitinated at residues K73, K135, K158, K193, and K219. Virus rescue showed that ubiquitination at sites K73, K193, and K219 on VP3 could enhance the replication abilities of infectious bursal disease virus (IBDV), and that K135 was essential for virus survival. Binding of the zinc finger domain of TRAF6 (TNF receptor associated factor 6) to VP3 mediated K11- and K33-linked ubiquitination of VP3, which promoted its nuclear accumulation to facilitate virus replication. Additionally, VP3 could inhibit TRAF6-mediated NFKB/NF-κB (nuclear factor kappa B) activation and IFNB/IFN-β (interferon beta) production to evade host innate immunity by inducing TRAF6 autophagic degradation in an SQSTM1/p62 (sequestosome 1)-dependent manner. Our findings demonstrated a macroautophagic/autophagic mechanism by which Avibirnavirusprotein VP3 blocked NFKB-mediated IFNB production by targeting TRAF6 during virus infection, and provided a potential drug target for virus infection control.Abbreviations:ATG: autophagy related; BafA1: bafilomycin A1; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; Cas9: CRISPR-associated protein 9; CHX: cycloheximide; Co-IP: co-immunoprecipitation; CRISPR: clustered regularly interspaced short palindromic repeats; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; GST: glutathione S-transferase; IBDV: infectious bursal disease virus; IF: indirect immunofluorescence; IFNB/IFN-β: interferon beta; mAb: monoclonal antibody; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MOI: multiplicity of infection; MS: mass spectrometry; NFKB/NF-κB: nuclear factor kappa B; NBR1: NBR1 autophagy cargo receptor; OPTN: optineurin; pAb: polyclonal antibody; PRRs: pattern recognition receptors; RNF125: ring finger protein 125; RNF135/Riplet: ring finger protein 135; SQSTM1/p62: sequestosome 1; TAX1BP1: tax1 binding protein1; TCID50: 50% tissue culture infective dose; TRAF3: TNF receptor associated factor 3; TRAF6: TNF receptor associated factor 6; TRIM25: tripartite motif containing 25; Ub: ubiquitin; Wort: wortmannin; WT: wild type.

Published
2022
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21. PDPK1 regulates autophagosome biogenesis by binding to PIK3C3

Author

Hu, Boli, primary, Zhang, Yina, additional, Deng, Tingjuan, additional, Gu, Jinyan, additional, Liu, Juan, additional, Yang, Hui, additional, Xu, Yuting, additional, Yan, Yan, additional, Yang, Fan, additional, Zhang, Heng, additional, Jin, Yulan, additional, and Zhou, Jiyong, additional

Published
2020
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31. Binding of AvibirnavirusVP3 to the PIK3C3-PDPK1 complex inhibits autophagy by activating the AKT-MTOR pathway

Author

Zhang, Yina, Hu, Boli, Li, Yahui, Deng, Tingjuan, Xu, Yuting, Lei, Jing, and Zhou, Jiyong

Abstract

ABSTRACTMacroautophagy/autophagy is a host natural defense response. Viruses have developed various strategies to subvert autophagy during their life cycle. Recently, we revealed that autophagy was activated by binding of Avibirnavirusto cells. In the present study, we report the inhibition of autophagy initiated by PIK3C3/VPS34 via the PDPK1-dependent AKT-MTOR pathway. Autophagy detection revealed that viral protein VP3 triggered inhibition of autophagy at the early stage of Avibirnavirusreplication. Subsequent interaction analysis showed that the CC1 domain of VP3 disassociated PIK3C3-BECN1 complex by direct interaction with BECN1 and blocked autophagosome formation, while the CC3 domain of VP3 disrupted PIK3C3-PDPK1 complex via directly binding to PIK3C3 and inhibited both formation and maturation of autophagosome. Furthermore, we found that PDPK1 activated AKT-MTOR pathway for suppressing autophagy via binding to AKT. Finally, we proved that CC3 domain was critical for role of VP3 in regulating replication of Avibirnavirusthrough autophagy. Taken together, our study identified that AvibirnavirusVP3 links PIK3C3-PDPK1 complex to AKT-MTOR pathway and inhibits autophagy, a critical step for controlling virus replication.AbbreviationsATG14/Barkor: autophagy related 14; BECN1: beclin 1; CC: coiled-coil; ER: endoplasmic reticulum; hpi: hours post-infection; IBDV: infectious bursal disease virus; IP: co-immunoprecipitation; mAb: monoclonal antibody; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MOI: multiplicity of infection; MTOR: mechanistic target of rapamycin kinase; PDPK1: 3-phosphoinositid-dependent protein kinase-1; PIK3C3/VPS34: phosphatidylinositol 3-kinase catalytic subunit type 3; PtdIns3K: phosphatidylinositol 3-kinase; PtdIns3P: phosphatidylinositol-3-phosphate; SQSTM1: sequestosome 1; vBCL2: viral BCL2 apoptosis regulator.

Published
2020
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43. [Effects of host proteins interacting with non-structural protein nsp9 of porcine epidemic diarrhea virus on viral replication].

Author

Shi Z, Wu J, Zhu Y, Zhou J, and Hu B

Subjects
Animals, Swine, Virus Replication, Proteins, Porcine epidemic diarrhea virus genetics, Swine Diseases
Abstract

Porcine epidemic diarrhea virus (PEDV) is a highly pathogenic virus that can cause acute intestinal infectious diseases in both piglets and fattening pigs. The virus encodes at least 16 non-structural proteins, including nsp9, which has been shown to bind to single-stranded RNA. However, its function and mechanism remain unclear. In this study, we aimed to identify potential host proteins that interact with PEDV nsp9 using immunoprecipitation combined with mass spectrometry. The interactions were then confirmed by co-immunoprecipitation (Co-IP) and confocal laser scanning fluorescence techniques. The results showed that nsp9 interacts with HSPA8, Tollip, HSPA9 and TOMM70. Among them, overexpression of HSPA8 resulted in caused first upregulated and then down-regulated expression of nsp9, and promoted the proliferation of PEDV. Overexpression of Tollip significantly upregulated the expression of nsp9 and inhibited the proliferation of PEDV. Overexpression of TOMM70 significantly reduced the expression of nsp9, but did not show significant effect on the proliferation of PEDV. Overexpression of HSPA9 did not show significant effect on the expression of nsp9 and the proliferation of PEDV. These findings may facilitate further investigating the role of nsp9-interacting proteins in PEDV infection.

Published
2023
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44. [Identification of host proteins interacting with African swine fever virus inner envelope protein p17].

Author

Zhong G, Deng T, Xu K, Ni W, Wang P, Hu B, and Zhou J

Subjects
Animals, Open Reading Frames, Swine, Viral Proteins genetics, Viral Proteins metabolism, African Swine Fever, African Swine Fever Virus genetics, African Swine Fever Virus metabolism
Abstract

African swine fever virus (ASFV) infection leads to a mortality rate of up to 100%, causing devastating disasters to the pig industry. Understanding the ASFV infection and replication is therefore of great importance. ASFV has more than 150 open reading frames, among which the inner coat protein p17 encoded by the D117L gene is involved in the formation of the icosahedral structure of the virus. However, little is known about the mechanism how p17 regulates host cell function. In this study, the potential host proteins interacting with ASFV p17 were screened by immunoprecipitation technique combined with protein profiling analysis. The interactions of p17 with mitochondrial membrane protein TOMM70 and heat shock protein HSPA8 were confirmed by co-immunoprecipitation technique and laser confocal experiments. This study provides important information for further exploring the function of p17 during ASFV infection.

Published
2022
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