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Liurong Fang
Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, China

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Review
Published: 13 June 2021 in Viruses
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Coronavirus accessory proteins are a unique set of proteins whose genes are interspersed among or within the genes encoding structural proteins. Different coronavirus genera, or even different species within the same coronavirus genus, encode varying amounts of accessory proteins, leading to genus- or species-specificity. Though accessory proteins are dispensable for the replication of coronavirus in vitro, they play important roles in regulating innate immunity, viral proliferation, and pathogenicity. The function of accessory proteins on virus infection and pathogenesis is an area of particular interest. In this review, we summarize the current knowledge on accessory proteins of several representative coronaviruses that infect humans or animals, including the emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), with an emphasis on their roles in interaction between virus and host, mainly involving stress response, innate immunity, autophagy, and apoptosis. The cross-talking among these pathways is also discussed.

ACS Style

Puxian Fang; Liurong Fang; Huichang Zhang; Sijin Xia; Shaobo Xiao. Functions of Coronavirus Accessory Proteins: Overview of the State of the Art. Viruses 2021, 13, 1139 .

AMA Style

Puxian Fang, Liurong Fang, Huichang Zhang, Sijin Xia, Shaobo Xiao. Functions of Coronavirus Accessory Proteins: Overview of the State of the Art. Viruses. 2021; 13 (6):1139.

Chicago/Turabian Style

Puxian Fang; Liurong Fang; Huichang Zhang; Sijin Xia; Shaobo Xiao. 2021. "Functions of Coronavirus Accessory Proteins: Overview of the State of the Art." Viruses 13, no. 6: 1139.

Short communication
Published: 18 May 2021 in Biochemical and Biophysical Research Communications
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This is the first study to clone duck CCCH-type zinc finger antiviral protein (duZAP) from Jingjiang duck (Anas platyrhynchos). Full-length duZAP cDNA was 2154 bp and encoded a 717-amino acid polypeptide containing four highly conserved CCCH-type finger motifs, a WWE domain and a poly (ADP-ribose) polymerase (PARP) domain. duZAP was expressed in multiple duck tissues, with the highest mRNA expression in the spleen. Overexpression of duZAP in duck embryo fibroblast cells (DEFs) led to activation of the transcription factors IRF1 and NF-κB, and induction of IFN-β. Analysis of deletion mutants revealed that both the WWE and PARP domains of duZAP were essential for activating the IFN-β promoter. Knockdown of duZAP in DEFs significantly reduced poly (I:C)- and duck Tembusu virus (DTMUV)-induced IFN-β activation. Our findings further the understanding of the role of duZAP in the duck innate immune response.

ACS Style

Rongrong Zhang; Yan He; Xinyu Zhu; Guoyuan Wen; Qingping Luo; Tengfei Zhang; Qin Lu; Shudan Liu; Shaobo Xiao; Liurong Fang; Huabin Shao. Molecular characterization and functional analysis of duck CCCH-type zinc finger antiviral protein (ZAP). Biochemical and Biophysical Research Communications 2021, 561, 52 -58.

AMA Style

Rongrong Zhang, Yan He, Xinyu Zhu, Guoyuan Wen, Qingping Luo, Tengfei Zhang, Qin Lu, Shudan Liu, Shaobo Xiao, Liurong Fang, Huabin Shao. Molecular characterization and functional analysis of duck CCCH-type zinc finger antiviral protein (ZAP). Biochemical and Biophysical Research Communications. 2021; 561 ():52-58.

Chicago/Turabian Style

Rongrong Zhang; Yan He; Xinyu Zhu; Guoyuan Wen; Qingping Luo; Tengfei Zhang; Qin Lu; Shudan Liu; Shaobo Xiao; Liurong Fang; Huabin Shao. 2021. "Molecular characterization and functional analysis of duck CCCH-type zinc finger antiviral protein (ZAP)." Biochemical and Biophysical Research Communications 561, no. : 52-58.

Journal article
Published: 26 April 2021 in Veterinary Microbiology
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Porcine epidemic diarrhea virus (PEDV) is a reemerging Alphacoronavirus that causes lethal diarrhea in piglets. Coronavirus nonstructural protein 13 (nsp13) encodes helicase, which plays pivotal roles during viral replication by unwinding viral RNA. However, the biochemical characterization of PEDV nsp13 remains largely unknown. In this study, PEDV nsp13 was expressed in Escherichia coli and purified. The recombinant nsp13 possessed ATPase and helicase activities for binding and unwinding dsDNA/RNA substrates with 5′-overhangs, and Mg2+ and Mn2+ were critical for its ATPase and helicase activities. PEDV nsp13 also unwound dsDNA into ssDNA in the pH from 6.0–9.0, and used energy from all nucleoside triphosphates and deoxynucleoside triphosphates. Site-directed mutagenesis demonstrated that Lys289 (K289) of PEDV nsp13 was essential for its ATPase and helicase activities. These results provide new insights into the biochemical properties of PEDV nsp13, which is a potential target for developing antiviral drugs.

ACS Style

Jie Ren; Zhen Ding; Puxian Fang; Shaobo Xiao; Liurong Fang. ATPase and helicase activities of porcine epidemic diarrhea virus nsp13. Veterinary Microbiology 2021, 257, 109074 .

AMA Style

Jie Ren, Zhen Ding, Puxian Fang, Shaobo Xiao, Liurong Fang. ATPase and helicase activities of porcine epidemic diarrhea virus nsp13. Veterinary Microbiology. 2021; 257 ():109074.

Chicago/Turabian Style

Jie Ren; Zhen Ding; Puxian Fang; Shaobo Xiao; Liurong Fang. 2021. "ATPase and helicase activities of porcine epidemic diarrhea virus nsp13." Veterinary Microbiology 257, no. : 109074.

Brief report
Published: 25 January 2021 in Archives of Virology
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Enteric coronaviruses (CoVs) are major pathogens that cause diarrhea in piglets. To date, four porcine enteric CoVs have been identified: transmissible gastroenteritis virus (TGEV), porcine epidemic diarrhea virus (PEDV), porcine deltacoronavirus (PDCoV), and HKU2-like porcine enteric alphacoronavirus (PEAV). In this study, we investigated the replicative capacity of these four enteric CoVs in LLC-PK1 cells, a porcine kidney cell line. The results showed that LLC-PK1 cells are susceptible to all four enteric CoVs, particularly to TGEV and PDCoV infections, indicating that LLC-PK1 cells can be applied to porcine enteric CoV research in vitro, particularly for coinfection studies.

ACS Style

Wenwen Xiao; Xunlei Wang; Jing Wang; Puxian Fang; Shaobo Xiao; Liurong Fang. Replicative capacity of four porcine enteric coronaviruses in LLC-PK1 cells. Archives of Virology 2021, 166, 935 -941.

AMA Style

Wenwen Xiao, Xunlei Wang, Jing Wang, Puxian Fang, Shaobo Xiao, Liurong Fang. Replicative capacity of four porcine enteric coronaviruses in LLC-PK1 cells. Archives of Virology. 2021; 166 (3):935-941.

Chicago/Turabian Style

Wenwen Xiao; Xunlei Wang; Jing Wang; Puxian Fang; Shaobo Xiao; Liurong Fang. 2021. "Replicative capacity of four porcine enteric coronaviruses in LLC-PK1 cells." Archives of Virology 166, no. 3: 935-941.

Journal article
Published: 08 December 2020 in Veterinary Microbiology
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The ubiquitin-proteasome system (UPS) plays a vital role in cellular protein homeostasis by ensuring protein quality control and maintaining a critical level of important regulatory proteins. Thus, it is not surprising that the functional UPS is manipulated by viruses to assist in viral propagation. Porcine reproductive and respiratory syndrome virus (PRRSV) is an economically significant swine disease that has been devastating the swine industry worldwide. However, the role of UPS in PRRSV infection is unknown. In this study, we found that treatment with the proteasome inhibitor MG132 significantly inhibited PRRSV proliferation in a dose-dependent manner. The anti-PRRSV effect of MG132 was most significant in the middle stage of the PRRSV lifecycle, which is achieved via inhibition of viral attachment and replication. Interestingly, the expression of poly-ubiquitin was drastically decreased and the accumulation of free-ubiquitin was obviously elevated in the middle stage of PRRSV infection. Furthermore, the ectopic expression of ubiquitin in MG132-treated cells partially reversed the inhibitory effect of MG132 on PRRSV proliferation. Taken together, these results suggest that PRRSV manipulates UPS to promote self-proliferation by cheating or taking advantage of the host proteasome, degrading intracellular poly-ubiquitin and increasing the accumulation of free ubiquitin.

ACS Style

Yu Pang; Mao Li; Yanrong Zhou; Wei Liu; Ran Tao; Hejin Zhang; Shaobo Xiao; Liurong Fang. The ubiquitin proteasome system is necessary for efficient proliferation of porcine reproductive and respiratory syndrome virus. Veterinary Microbiology 2020, 253, 108947 .

AMA Style

Yu Pang, Mao Li, Yanrong Zhou, Wei Liu, Ran Tao, Hejin Zhang, Shaobo Xiao, Liurong Fang. The ubiquitin proteasome system is necessary for efficient proliferation of porcine reproductive and respiratory syndrome virus. Veterinary Microbiology. 2020; 253 ():108947.

Chicago/Turabian Style

Yu Pang; Mao Li; Yanrong Zhou; Wei Liu; Ran Tao; Hejin Zhang; Shaobo Xiao; Liurong Fang. 2020. "The ubiquitin proteasome system is necessary for efficient proliferation of porcine reproductive and respiratory syndrome virus." Veterinary Microbiology 253, no. : 108947.

Journal article
Published: 29 September 2020 in Journal of Virology
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Currently, the active-site residues and substrate specificities of 3C-like protease (3CL pro ) differ among nidoviruses, and the detailed catalytic mechanism remains largely unknown. Here, porcine torovirus (PToV) 3CL pro cleaves 12 sites in the polyproteins, including its N- and C-terminal self-processing sites. Unlike coronaviruses and arteriviruses, PToV 3CL pro employed His53 and Ser160 as the active-site residues that recognize a glutamine (Gln) at the P1 position. Surprisingly, mutations of P1-Gln impaired the C-terminal self-processing but did not affect N-terminal self-processing. The “noncanonical” substrate specificity for its N-terminal self-processing was attributed to the phenylalanine (Phe) residue at the P4 position in the N-terminal site. Furthermore, a double glycine (neutral) substitution at the putative P4-Phe-binding residues (P62G/L185G) abolished the cleavage activity of PToV 3CL pro suggested the potential hydrophobic force between the PToV 3CL pro and P4-Phe side chains.

ACS Style

Shangen Xu; Junwei Zhou; Yingjin Chen; Xue Tong; Zixin Wang; Jiahui Guo; Jiyao Chen; Liurong Fang; Dang Wang; Shaobo Xiao. Characterization of Self-Processing Activities and Substrate Specificities of Porcine Torovirus 3C-Like Protease. Journal of Virology 2020, 94, 1 .

AMA Style

Shangen Xu, Junwei Zhou, Yingjin Chen, Xue Tong, Zixin Wang, Jiahui Guo, Jiyao Chen, Liurong Fang, Dang Wang, Shaobo Xiao. Characterization of Self-Processing Activities and Substrate Specificities of Porcine Torovirus 3C-Like Protease. Journal of Virology. 2020; 94 (20):1.

Chicago/Turabian Style

Shangen Xu; Junwei Zhou; Yingjin Chen; Xue Tong; Zixin Wang; Jiahui Guo; Jiyao Chen; Liurong Fang; Dang Wang; Shaobo Xiao. 2020. "Characterization of Self-Processing Activities and Substrate Specificities of Porcine Torovirus 3C-Like Protease." Journal of Virology 94, no. 20: 1.

Journal article
Published: 04 August 2020 in Scientific Reports
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During viral infection, the host cell synthesizes high amounts of viral proteins, which often causes stress to the endoplasmic reticulum (ER). To manage abnormal ER stress, mammalian cells trigger a response called the unfolded protein response (UPR). Previous studies have indicated that porcine reproductive and respiratory syndrome virus (PRRSV), an Arterivirus that has been devastating the swine industry worldwide, can induce ER stress and activate UPR, however, the activation pathways and the biological significance requires further investigation. In this study, we demonstrated that, among the three types of UPR pathways, PRRSV infection induced PERK and IRE1 pathways, but not the ATF6 pathway. Furthermore, the induction of UPR promoted PRRSV replication. We also found that PRRSV-induced UPR, particularly the PERK pathway, was involved in the induction of autophagy, a cellular degradation process that can alleviate cell stress. Besides, we also provided insights into the ER stress-mediated apoptosis in response to PRRSV infection. PRRSV infection induced the expression of the transcription factor CHOP, which activated caspase 3 and PARP led to ER stress-mediated apoptosis. Using 3-Methyladenine (3-MA) to inhibit autophagy, the increased ER stress and cell apoptosis were observed in the PRRSV infected cell. Taken together, our results revealed the associations of ER stress, autophagy, and apoptosis during PRRSV infection, helping us to further understand how PRRSV interacts with host cells.

ACS Style

Quangang Chen; Yanjuan Men; Dang Wang; Deqin Xu; Suyan Liu; Shaobo Xiao; Liurong Fang. Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis. Scientific Reports 2020, 10, 1 -13.

AMA Style

Quangang Chen, Yanjuan Men, Dang Wang, Deqin Xu, Suyan Liu, Shaobo Xiao, Liurong Fang. Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis. Scientific Reports. 2020; 10 (1):1-13.

Chicago/Turabian Style

Quangang Chen; Yanjuan Men; Dang Wang; Deqin Xu; Suyan Liu; Shaobo Xiao; Liurong Fang. 2020. "Porcine reproductive and respiratory syndrome virus infection induces endoplasmic reticulum stress, facilitates virus replication, and contributes to autophagy and apoptosis." Scientific Reports 10, no. 1: 1-13.

Journal article
Published: 16 July 2020 in Journal of Virology
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Interferon (IFN)-stimulated gene (ISG) induction through IFN signaling is important to create an antiviral state and usually directly inhibits virus infection. The present study first demonstrated that PDCoV nsp5 can cleave mRNA-decapping enzyme 1a (DCP1A) to attenuate its antiviral activity. Furthermore, cleaving DCP1A is a common characteristic of nsp5 proteins from different coronaviruses (CoVs), which represents a common immune evasion mechanism of CoVs. Previous evidence showed that CoV nsp5 cleaves the NF-κB essential modulator and signal transducer and activator of transcription 2. Taken together, CoV nsp5 is a potent IFN antagonist because it can simultaneously target different aspects of the host IFN system, including IFN production and signaling and effector molecules.

ACS Style

Xinyu Zhu; Jiyao Chen; Liyuan Tian; Yanrong Zhou; Shangen Xu; Siwen Long; Dang Wang; Liurong Fang; Shaobo Xiao. Porcine Deltacoronavirus nsp5 Cleaves DCP1A To Decrease Its Antiviral Activity. Journal of Virology 2020, 94, 1 .

AMA Style

Xinyu Zhu, Jiyao Chen, Liyuan Tian, Yanrong Zhou, Shangen Xu, Siwen Long, Dang Wang, Liurong Fang, Shaobo Xiao. Porcine Deltacoronavirus nsp5 Cleaves DCP1A To Decrease Its Antiviral Activity. Journal of Virology. 2020; 94 (15):1.

Chicago/Turabian Style

Xinyu Zhu; Jiyao Chen; Liyuan Tian; Yanrong Zhou; Shangen Xu; Siwen Long; Dang Wang; Liurong Fang; Shaobo Xiao. 2020. "Porcine Deltacoronavirus nsp5 Cleaves DCP1A To Decrease Its Antiviral Activity." Journal of Virology 94, no. 15: 1.

Journal article
Published: 02 July 2020 in Veterinary Microbiology
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Porcine deltacoronavirus (PDCoV) is a novel swine enteropathogenic coronavirus that causes watery diarrhea, vomiting and mortality in nursing piglets. Type III interferons (IFN-λs) are the major antiviral cytokines in intestinal epithelial cells, the target cells in vivo for PDCoV. In this study, we found that PDCoV infection remarkably inhibited Sendai virus-induced IFN-λ1 production by suppressing transcription factors IRF and NF-κB in IPI-2I cells, a line of porcine intestinal mucosal epithelial cells. We also confirmed that PDCoV infection impeded the activation of IFN-λ1 promoter stimulated by RIG-I, MDA5 and MAVS, but not by TBK1 and IRF1. Although the expression levels of IRF1 and MAVS were not changed, PDCoV infection resulted in reduction of the number of peroxisomes, the platform for MAVS to activate IRF1, and subsequent type III IFN production. Taken together, our study demonstrates that PDCoV suppresses type III IFN responses to circumvent the host’s antiviral immunity.

ACS Style

Shudan Liu; Puxian Fang; Wenting Ke; Jing Wang; Xunlei Wang; Shaobo Xiao; Liurong Fang. Porcine deltacoronavirus (PDCoV) infection antagonizes interferon-λ1 production. Veterinary Microbiology 2020, 247, 108785 -108785.

AMA Style

Shudan Liu, Puxian Fang, Wenting Ke, Jing Wang, Xunlei Wang, Shaobo Xiao, Liurong Fang. Porcine deltacoronavirus (PDCoV) infection antagonizes interferon-λ1 production. Veterinary Microbiology. 2020; 247 ():108785-108785.

Chicago/Turabian Style

Shudan Liu; Puxian Fang; Wenting Ke; Jing Wang; Xunlei Wang; Shaobo Xiao; Liurong Fang. 2020. "Porcine deltacoronavirus (PDCoV) infection antagonizes interferon-λ1 production." Veterinary Microbiology 247, no. : 108785-108785.

Short communication
Published: 06 May 2020 in Biochemical and Biophysical Research Communications
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DEAD (Asp-Glu-Ala-Asp) box RNA helicase 3 (DDX3X) is demonstrated to have crucial functions in the antiviral immune response. To our knowledge, little information focuses on the function of duck DDX3X. In this study, duck DDX3X (duDDX3X) was cloned and its role in the type I interferon (IFN) signaling pathway was investigated using duck embryo fibroblast (DEF) cells. Full-length duDDX3X cDNA encodes 652 amino acid residues and contains a DEADc domain and a HELICc domain. According to tissue distribution analysis, duDDX3X mRNA was widely expressed in different tissues, especially the spleen and the liver. Overexpression of duDDX3X in DEF cells induced IFN-β by activating transcription factors IRF1 and NF-κB. Knockdown of duDDX3X in DEF cells with siRNA significantly reduced IFN-β expression induced by poly(I:C), a double-stranded RNA (dsRNA) analog. Our results demonstrated that duck DDX3X was involved in the dsRNA-mediated type I IFN signaling pathway in DEF cells.

ACS Style

Rongrong Zhang; Honglin Wang; Xinyu Zhu; Shudan Liu; Zui Wang; Qin Lu; Huabin Shao; Shaobo Xiao; Liurong Fang. Molecular cloning and functional characterization of duck DEAD (Asp-Glu-Ala-Asp) box RNA helicase 3 (DDX3X). Biochemical and Biophysical Research Communications 2020, 527, 496 -502.

AMA Style

Rongrong Zhang, Honglin Wang, Xinyu Zhu, Shudan Liu, Zui Wang, Qin Lu, Huabin Shao, Shaobo Xiao, Liurong Fang. Molecular cloning and functional characterization of duck DEAD (Asp-Glu-Ala-Asp) box RNA helicase 3 (DDX3X). Biochemical and Biophysical Research Communications. 2020; 527 (2):496-502.

Chicago/Turabian Style

Rongrong Zhang; Honglin Wang; Xinyu Zhu; Shudan Liu; Zui Wang; Qin Lu; Huabin Shao; Shaobo Xiao; Liurong Fang. 2020. "Molecular cloning and functional characterization of duck DEAD (Asp-Glu-Ala-Asp) box RNA helicase 3 (DDX3X)." Biochemical and Biophysical Research Communications 527, no. 2: 496-502.

Journal article
Published: 23 December 2019 in Veterinary Microbiology
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Complement component 1, q subcomponent binding protein (C1QBP) is a receptor for the globular heads of C1q and modulates various biological processes including infection, inflammation, autoimmunity, and cancer. In our previous study to identify differentially expressed secretory proteins in Marc-145 cells infected with porcine reproductive and respiratory syndrome virus (PRRSV), mass spectrum data showed that C1QBP was secreted after PRRSV infection. However, the biological significance of secreted C1QBP remains unclear. In this study, we confirmed that PRRSV infection promoted C1QBP secretion in Marc-145 cells and porcine alveolar macrophages (PAMs), the target cells of PRRSV in vivo. Knockdown of endogenous C1QBP decreased PRRSV-induced inflammatory responses. The purified recombinant porcine C1QBP (poC1QBP) had proinflammatory effects. The exogenous addition of poC1QBP significantly enhanced PRRSV-induced inflammatory responses and abolished the inhibitory effects mediated by poC1QBP-knockdown. Taken together, these results demonstrate that PRRSV infection promotes poC1QBP secretion that enhances inflammatory responses.

ACS Style

Yang Li; Ying Wei; Wanjun Hao; Wenkai Zhao; Yanrong Zhou; Dang Wang; Shaobo Xiao; Liurong Fang. Porcine reproductive and respiratory syndrome virus infection promotes C1QBP secretion to enhance inflammatory responses. Veterinary Microbiology 2019, 241, 108563 .

AMA Style

Yang Li, Ying Wei, Wanjun Hao, Wenkai Zhao, Yanrong Zhou, Dang Wang, Shaobo Xiao, Liurong Fang. Porcine reproductive and respiratory syndrome virus infection promotes C1QBP secretion to enhance inflammatory responses. Veterinary Microbiology. 2019; 241 ():108563.

Chicago/Turabian Style

Yang Li; Ying Wei; Wanjun Hao; Wenkai Zhao; Yanrong Zhou; Dang Wang; Shaobo Xiao; Liurong Fang. 2019. "Porcine reproductive and respiratory syndrome virus infection promotes C1QBP secretion to enhance inflammatory responses." Veterinary Microbiology 241, no. : 108563.

Journal article
Published: 10 December 2019 in Viruses
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Lipids play a crucial role in the replication of porcine reproductive and respiratory syndrome virus (PRRSV), a porcine virus that is endemic throughout the world. However, little is known about the effect of fatty acids (FAs), a type of vital lipid, on PRRSV infection. In this study, we found that treatment with a FA biosynthetic inhibitor significantly inhibited PRRSV propagation, indicating the necessity of FAs for optimal replication of PRRSV. Further study revealed that 5′-adenosine monophosphate (AMP)-activated protein kinase (AMPK), a key kinase antagonizing FA biosynthesis, was strongly activated by PRRSV and the pharmacological activator of AMPK exhibited anti-PRRSV activity. Additionally, we found that acetyl-CoA carboxylase 1 (ACC1), the first rate-limiting enzyme in the FA biosynthesis pathway, was phosphorylated (inactive form) by PRRSV-activated AMPK, and active ACC1 was required for PRRSV proliferation, suggesting that the PRRSV infection induced the activation of the AMPK–ACC1 pathway, which was not conducive to PRRSV replication. This work provides new evidence about the mechanisms involved in host lipid metabolism during PRRSV infection and identifies novel potential antiviral targets for PRRSV.

ACS Style

Siwen Long; Yanrong Zhou; Dongcheng Bai; Wanjun Hao; Bohan Zheng; Shaobo Xiao; Liurong Fang. Fatty Acids Regulate Porcine Reproductive and Respiratory Syndrome Virus Infection via the AMPK-ACC1 Signaling Pathway. Viruses 2019, 11, 1145 .

AMA Style

Siwen Long, Yanrong Zhou, Dongcheng Bai, Wanjun Hao, Bohan Zheng, Shaobo Xiao, Liurong Fang. Fatty Acids Regulate Porcine Reproductive and Respiratory Syndrome Virus Infection via the AMPK-ACC1 Signaling Pathway. Viruses. 2019; 11 (12):1145.

Chicago/Turabian Style

Siwen Long; Yanrong Zhou; Dongcheng Bai; Wanjun Hao; Bohan Zheng; Shaobo Xiao; Liurong Fang. 2019. "Fatty Acids Regulate Porcine Reproductive and Respiratory Syndrome Virus Infection via the AMPK-ACC1 Signaling Pathway." Viruses 11, no. 12: 1145.

Journal article
Published: 22 October 2019 in Virology
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Ionic calcium (Ca2+) is a versatile intracellular second messenger that plays important roles in cellular physiological and pathological processes. Porcine deltacoronavirus (PDCoV) is an emerging enteropathogenic coronavirus that causes serious vomiting and diarrhea in suckling piglets. In this study, the role of Ca2+ to PDCoV infection was investigated. PDCoV infection was found to upregulate intracellular Ca2+ concentrations of IPI-2I cells. Chelating extracellular Ca2+ by EGTA inhibited PDCoV replication, and this inhibitory effect was overcome by replenishment with CaCl2. Treatment with Ca2+ channel blockers, particularly the L-type Ca2+ channel blocker diltiazem hydrochloride, inhibited PDCoV infection significantly. Mechanistically, diltiazem hydrochloride reduces PDCoV infection by inhibiting the replication step of the viral replication cycle. Additionally, knockdown of CACNA1S, the L-type Ca2+ voltage-gated channel subunit, inhibited PDCoV replication. The combined results demonstrate that PDCoV modulates calcium influx to favor its replication.

ACS Style

Dongcheng Bai; Liurong Fang; Sijin Xia; Wenting Ke; Jing Wang; Xiaoli Wu; Puxian Fang; Shaobo Xiao. Porcine deltacoronavirus (PDCoV) modulates calcium influx to favor viral replication. Virology 2019, 539, 38 -48.

AMA Style

Dongcheng Bai, Liurong Fang, Sijin Xia, Wenting Ke, Jing Wang, Xiaoli Wu, Puxian Fang, Shaobo Xiao. Porcine deltacoronavirus (PDCoV) modulates calcium influx to favor viral replication. Virology. 2019; 539 ():38-48.

Chicago/Turabian Style

Dongcheng Bai; Liurong Fang; Sijin Xia; Wenting Ke; Jing Wang; Xiaoli Wu; Puxian Fang; Shaobo Xiao. 2019. "Porcine deltacoronavirus (PDCoV) modulates calcium influx to favor viral replication." Virology 539, no. : 38-48.

Journal article
Published: 15 October 2019 in Journal of Virology
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CH25H has received significant attention due to its broad antiviral activity, which it mediates by catalyzing the production of 25HC. Most studies have focused on the antiviral mechanisms of CH25H; however, whether viruses also actively regulate CH25H expression has not yet been reported. Previous studies demonstrated that pCH25H inhibits PRRSV replication not only via production of 25HC but also by ubiquitination and degradation of viral nonstructural protein 1α. In this study, we expanded on previous work and found that PRRSV actively degrades pCH25H through the ubiquitin-proteasome pathway. PRRSV E protein, a viral structural protein, is involved in this process. This study reveals a novel mechanism of interaction between virus and host during PRRSV infection.

ACS Style

Wenting Ke; Liurong Fang; Ran Tao; Yang Li; Huiyuan Jing; Dang Wang; Shaobo Xiao. Porcine Reproductive and Respiratory Syndrome Virus E Protein Degrades Porcine Cholesterol 25-Hydroxylase via the Ubiquitin-Proteasome Pathway. Journal of Virology 2019, 93, 1 .

AMA Style

Wenting Ke, Liurong Fang, Ran Tao, Yang Li, Huiyuan Jing, Dang Wang, Shaobo Xiao. Porcine Reproductive and Respiratory Syndrome Virus E Protein Degrades Porcine Cholesterol 25-Hydroxylase via the Ubiquitin-Proteasome Pathway. Journal of Virology. 2019; 93 (20):1.

Chicago/Turabian Style

Wenting Ke; Liurong Fang; Ran Tao; Yang Li; Huiyuan Jing; Dang Wang; Shaobo Xiao. 2019. "Porcine Reproductive and Respiratory Syndrome Virus E Protein Degrades Porcine Cholesterol 25-Hydroxylase via the Ubiquitin-Proteasome Pathway." Journal of Virology 93, no. 20: 1.

Journal article
Published: 01 August 2019 in Journal of Virology
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The nidovirus-specific endoribonuclease (NendoU) encoded by PRRSV nonstructural protein 11 (nsp11) is a unique NendoU of nidoviruses that infect vertebrates; thus, it is an attractive target for the development of antinidovirus drugs. Previous studies have revealed that the NendoU of nidoviruses, including porcine reproductive and respiratory syndrome virus (PRRSV) and human coronavirus 229E (HCoV-229E), acts as a type I interferon (IFN) antagonist. Here, for the first time, we demonstrated that overexpression of PRRSV nsp11 also inhibits IFN signaling by targeting the C-terminal interferon regulatory factor (IRF) association domain of IRF9. This interaction impaired the ability of IRF9 to form the transcription factor complex IFN-stimulated gene factor 3 (ISGF3) and to act as a signaling protein of IFN signaling. Collectively, our data identify IRF9 as a natural target of PRRSV NendoU and reveal a novel mechanism evolved by an arterivirus to counteract innate immune signaling.

ACS Style

Dang Wang; Jiyao Chen; Chaoliang Yu; Xinyu Zhu; Shangen Xu; Liurong Fang; Shaobo Xiao. Porcine Reproductive and Respiratory Syndrome Virus nsp11 Antagonizes Type I Interferon Signaling by Targeting IRF9. Journal of Virology 2019, 93, 1 .

AMA Style

Dang Wang, Jiyao Chen, Chaoliang Yu, Xinyu Zhu, Shangen Xu, Liurong Fang, Shaobo Xiao. Porcine Reproductive and Respiratory Syndrome Virus nsp11 Antagonizes Type I Interferon Signaling by Targeting IRF9. Journal of Virology. 2019; 93 (15):1.

Chicago/Turabian Style

Dang Wang; Jiyao Chen; Chaoliang Yu; Xinyu Zhu; Shangen Xu; Liurong Fang; Shaobo Xiao. 2019. "Porcine Reproductive and Respiratory Syndrome Virus nsp11 Antagonizes Type I Interferon Signaling by Targeting IRF9." Journal of Virology 93, no. 15: 1.

Journal article
Published: 15 June 2019 in Journal of Virology
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The arterivirus nsp4-encoded 3C-like protease (3CL pro ) plays an important role in virus replication and immune evasion, making it an attractive target for antiviral therapeutics. Previous work suggested that PRRSV nsp4 suppresses type I IFN production by cleaving NEMO at a single site. In contrast, the present study demonstrates that both EAV and PRRSV nsp4 cleave NEMO at multiple sites and that this strategy is essential for disruption of type I IFN production. Moreover, we reveal that EAV nsp4 also cleaves NEMO at glutamine 205 (Q205), which is not targeted by PRRSV nsp4. Notably, targeting a glutamine in NEMO for cleavage has been observed only with picornavirus 3C proteases (3C pro ) and coronavirus 3CL pro . In aggregate, our work expands knowledge of the innate immune evasion mechanisms associated with NEMO cleavage by arterivirus nsp4 and describes a novel substrate recognition characteristic of EAV nsp4.

ACS Style

Jiyao Chen; Dang Wang; Zheng Sun; Li Gao; Xinyu Zhu; Jiahui Guo; Shangen Xu; Liurong Fang; Kui Li; Shaobo Xiao. Arterivirus nsp4 Antagonizes Interferon Beta Production by Proteolytically Cleaving NEMO at Multiple Sites. Journal of Virology 2019, 93, 1 .

AMA Style

Jiyao Chen, Dang Wang, Zheng Sun, Li Gao, Xinyu Zhu, Jiahui Guo, Shangen Xu, Liurong Fang, Kui Li, Shaobo Xiao. Arterivirus nsp4 Antagonizes Interferon Beta Production by Proteolytically Cleaving NEMO at Multiple Sites. Journal of Virology. 2019; 93 (12):1.

Chicago/Turabian Style

Jiyao Chen; Dang Wang; Zheng Sun; Li Gao; Xinyu Zhu; Jiahui Guo; Shangen Xu; Liurong Fang; Kui Li; Shaobo Xiao. 2019. "Arterivirus nsp4 Antagonizes Interferon Beta Production by Proteolytically Cleaving NEMO at Multiple Sites." Journal of Virology 93, no. 12: 1.

Journal article
Published: 14 April 2019 in Veterinary Microbiology
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Swine enteric coronavirus (CoV) is an important group of pathogens causing diarrhea in piglets. At least four kinds of swine enteric CoVs have been identified, including transmissible gastroenteritis virus (TGEV), porcine epidemic diarrhea virus (PEDV), porcine deltacoronavirus (PDCoV), and the emerging HKU2-like porcine enteric alphacoronavirus (PEAV). The small intestines, particularly the jejunum and ileum, are the most common targets of these four CoVs in vivo, and co-infections by these CoVs are frequently observed in clinically infected pigs. This study was conducted to investigate the susceptibility of the porcine ileum epithelial cell line, IPI-2I, to different swine enteric CoVs. We found that IPI-2I cells are highly susceptible to TGEV, PDCoV, and PEAV, as demonstrated by cytopathic effect and virus multiplication. However, only a small number of cells could be infected by PEDV, possibly due to the heterogeneity of IPI-2I cells. A homogeneous cell line, designated IPI-FX, obtained from IPI-2I cells by sub-cloning with limited serial dilutions, was found to be highly susceptible to PEDV. Furthermore, IPI-FX cells were also highly susceptible to TGEV, PDCoV, as well as PEAV. Thus, this sub-cloned IPI-FX cell line is an ideal cell model to study the mechanisms of infection, particularly co-infections of swine enteric CoVs.

ACS Style

Xunlei Wang; Liurong Fang; Shudan Liu; Wenting Ke; Dang Wang; Guiqing Peng; Shaobo Xiao. Susceptibility of porcine IPI-2I intestinal epithelial cells to infection with swine enteric coronaviruses. Veterinary Microbiology 2019, 233, 21 -27.

AMA Style

Xunlei Wang, Liurong Fang, Shudan Liu, Wenting Ke, Dang Wang, Guiqing Peng, Shaobo Xiao. Susceptibility of porcine IPI-2I intestinal epithelial cells to infection with swine enteric coronaviruses. Veterinary Microbiology. 2019; 233 ():21-27.

Chicago/Turabian Style

Xunlei Wang; Liurong Fang; Shudan Liu; Wenting Ke; Dang Wang; Guiqing Peng; Shaobo Xiao. 2019. "Susceptibility of porcine IPI-2I intestinal epithelial cells to infection with swine enteric coronaviruses." Veterinary Microbiology 233, no. : 21-27.

Article
Published: 01 September 2018 in Journal of Virology
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Coronaviruses cause widespread respiratory, gastrointestinal, and central nervous system diseases in humans and other animals, threatening human health and causing economic loss. Coronavirus nsp9, a member of the replication complex, is an important RNA binding subunit in the RNA-synthesizing machinery of all coronaviruses. However, the mechanisms of the dimerization and nucleic acid binding of nsp9 remain elusive. In this study we determined the nsp9 crystal structures of PDCoV and PEDV. We first found that the N-finger of nsp9 from PDCoV plays a critical role in dimerization. Meanwhile, PEDV nsp9 is distinguished by the presence of a disulfide bond in the dimer interface. This study provides a structural and functional basis for understanding the mechanism of dimerization and shows that the diverse dimerization modes of coronavirus nsp9 proteins enhance their nucleic acid binding affinity. Importantly, these findings may provide a new insight for antiviral drug development.

ACS Style

Zhe Zeng; Feng Deng; Ke Shi; Gang Ye; Gang Wang; Liurong Fang; Shaobo Xiao; Zhenfang Fu; Guiqing Peng. Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity. Journal of Virology 2018, 92, e00692-18 .

AMA Style

Zhe Zeng, Feng Deng, Ke Shi, Gang Ye, Gang Wang, Liurong Fang, Shaobo Xiao, Zhenfang Fu, Guiqing Peng. Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity. Journal of Virology. 2018; 92 (17):e00692-18.

Chicago/Turabian Style

Zhe Zeng; Feng Deng; Ke Shi; Gang Ye; Gang Wang; Liurong Fang; Shaobo Xiao; Zhenfang Fu; Guiqing Peng. 2018. "Dimerization of Coronavirus nsp9 with Diverse Modes Enhances Its Nucleic Acid Binding Affinity." Journal of Virology 92, no. 17: e00692-18.

Journal article
Published: 15 August 2018 in Journal of Virology
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Viruses are obligate parasites, and the production of progeny viruses relies strictly on the host translation machinery. Therefore, the efficient modulation of host mRNA translation benefits viral replication, spread, and evolution. In this study, we provide evidence that porcine reproductive and respiratory syndrome virus (PRRSV) infection induces host translation shutoff and that the viral nonstructural protein nsp2 is associated with this process. Many viruses induce host translation shutoff by phosphorylating eukaryotic initiation factor 2α (eIF2α). However, PRRSV nsp2 does not induce eIF2α phosphorylation but attenuates the mTOR signaling pathway, another pathway regulating the host cell translational machinery. We also found that PRRSV-induced host translation shutoff was partly reversed by eliminating the effects of eIF2α phosphorylation or reactivating the mTOR pathway, indicating that PRRSV infection induces both eIF2α phosphorylation-dependent and -independent host translation shutoff.

ACS Style

Yang Li; Liurong Fang; Yanrong Zhou; Ran Tao; Dang Wang; Shaobo Xiao. Porcine Reproductive and Respiratory Syndrome Virus Infection Induces both eIF2α Phosphorylation-Dependent and -Independent Host Translation Shutoff. Journal of Virology 2018, 92, 1 .

AMA Style

Yang Li, Liurong Fang, Yanrong Zhou, Ran Tao, Dang Wang, Shaobo Xiao. Porcine Reproductive and Respiratory Syndrome Virus Infection Induces both eIF2α Phosphorylation-Dependent and -Independent Host Translation Shutoff. Journal of Virology. 2018; 92 (16):1.

Chicago/Turabian Style

Yang Li; Liurong Fang; Yanrong Zhou; Ran Tao; Dang Wang; Shaobo Xiao. 2018. "Porcine Reproductive and Respiratory Syndrome Virus Infection Induces both eIF2α Phosphorylation-Dependent and -Independent Host Translation Shutoff." Journal of Virology 92, no. 16: 1.

Journal article
Published: 01 August 2018 in Journal of Virology
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Porcine deltacoronavirus (PDCoV) has recently emerged as an enteric pathogen that can cause serious vomiting and diarrhea in suckling piglets. The first outbreak of PDCoV occurred in the United States in 2014 and was followed by reports of PDCoV in South Korea, China, Thailand, Lao People's Democratic Republic, and Vietnam, leading to economic losses for pig farms and posing a considerable threat to the swine industry worldwide. Our previous studies have shown that PDCoV encodes three accessory proteins, NS6, NS7, and NS7a, but the functions of these proteins in viral replication, pathogenesis, and immune regulation remain unclear. Here, we found that ectopic expression of accessory protein NS6 significantly inhibits Sendai virus-induced interferon beta (IFN-β) production as well as the activation of transcription factors IRF3 and NF-κB. Interestingly, NS6 does not impede the IFN-β promoter activation mediated via key molecules in the RIG-I-like receptor (RLR) signaling pathway, specifically RIG-I, MDA5, and their downstream molecules MAVS, TBK1, IKKε, and IRF3. Further analyses revealed that NS6 is not an RNA-binding protein; however, it interacts with RIG-I/MDA5. This interaction attenuates the binding of double-stranded RNA by RIG-I/MDA5, resulting in the reduction of RLR-mediated IFN-β production. Taken together, our results demonstrate that ectopic expression of NS6 antagonizes IFN-β production by interfering with the binding of RIG-I/MDA5 to double-stranded RNA, revealing a new strategy employed by PDCoV accessory proteins to counteract the host innate antiviral immune response. IMPORTANCE Coronavirus accessory proteins are species specific, and they perform multiple functions in viral pathogenicity and immunity, such as acting as IFN antagonists and cell death inducers. Our previous studies have shown that PDCoV encodes three accessory proteins. Here, we demonstrated for the first time that PDCoV accessory protein NS6 antagonizes IFN-β production by interacting with RIG-I and MDA5 to impede their association with double-stranded RNA. This is an efficient strategy of antagonizing type I IFN production by disrupting the binding of host pattern recognition receptors (PRRs) and pathogen-associated molecular patterns (PAMPs). These findings deepen our understanding of the function of accessory protein NS6, and they may direct us toward novel therapeutic targets and lead to the development of more effective vaccines against PDCoV infection.

ACS Style

Puxian Fang; Liurong Fang; Jie Ren; Yingying Hong; Xiaorong Liu; Yunyang Zhao; Dang Wang; Guiqing Peng; Shaobo Xiao. Porcine Deltacoronavirus Accessory Protein NS6 Antagonizes Interferon Beta Production by Interfering with the Binding of RIG-I/MDA5 to Double-Stranded RNA. Journal of Virology 2018, 92, e00712-18 .

AMA Style

Puxian Fang, Liurong Fang, Jie Ren, Yingying Hong, Xiaorong Liu, Yunyang Zhao, Dang Wang, Guiqing Peng, Shaobo Xiao. Porcine Deltacoronavirus Accessory Protein NS6 Antagonizes Interferon Beta Production by Interfering with the Binding of RIG-I/MDA5 to Double-Stranded RNA. Journal of Virology. 2018; 92 (15):e00712-18.

Chicago/Turabian Style

Puxian Fang; Liurong Fang; Jie Ren; Yingying Hong; Xiaorong Liu; Yunyang Zhao; Dang Wang; Guiqing Peng; Shaobo Xiao. 2018. "Porcine Deltacoronavirus Accessory Protein NS6 Antagonizes Interferon Beta Production by Interfering with the Binding of RIG-I/MDA5 to Double-Stranded RNA." Journal of Virology 92, no. 15: e00712-18.