scholarly journals Classical swine fever virus employs the PERK- and IRE1-dependent autophagy for viral replication in cultured cells.

Virulence ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 130-149
Author(s):  
Erpeng Zhu ◽  
Huawei Wu ◽  
Wenxian Chen ◽  
Yuwei Qin ◽  
Jiameng Liu ◽  
...  
Keyword(s):  
Viral Replication ◽  
Classical Swine Fever Virus ◽  
Cultured Cells ◽  
Classical Swine Fever ◽  
Fever Virus

scholarly journals Cellular Hsp27 interacts with classical swine fever virus NS5A protein and negatively regulates viral replication by the NF-κB signaling pathway

Virology ◽  
2018 ◽  
Vol 518 ◽  
pp. 202-209 ◽  
Author(s):  
Shifeng Ling ◽  
Mingyang Luo ◽  
Shengnan Jiang ◽  
Jiayu Liu ◽  
Chunying Ding ◽  
...  
Keyword(s):  
Viral Replication ◽  
Signaling Pathway ◽  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Ns5a Protein

Dimerisation of glycoprotein Erns of classical swine fever virus is not essential for viral replication and infection

2005 ◽  
Vol 150 (11) ◽  
pp. 2271-2286 ◽  
Author(s):  
H. G. P. van Gennip ◽  
A. T. Hesselink ◽  
R. J. M. Moormann ◽  
M. M. Hulst
Keyword(s):  
Viral Replication ◽  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Fever Virus

scholarly journals Study of reproduction cycles and yield dynamics of the classical swine fever virus in PK-15 cultured cells using a fluorescent probes technique

2000 ◽  
Vol 16 (1) ◽  
pp. 60-63 ◽  
Author(s):  
L. D. Reshetniak ◽  
E. A. Krasnobayev ◽  
E. V. Novozhilova ◽  
E. N. Zherebtsova ◽  
G. A. Popova
Keyword(s):  
Fluorescent Probes ◽  
Classical Swine Fever Virus ◽  
Cultured Cells ◽  
Classical Swine Fever ◽  
Fever Virus

scholarly journals The Unique Glycosylation at Position 986 on the E2 Glycoprotein of Classical Swine Fever Virus Is Responsible for Viral Attenuation and Protection against Lethal Challenge

2021 ◽  
Author(s):  
Yongfeng Li ◽  
Mengqi Yuan ◽  
Yuying Han ◽  
Libao Xie ◽  
Yuteng Ma ◽  
...  
Keyword(s):  
Viral Replication ◽  
Classical Swine Fever Virus ◽  
Virulent Strain ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Lethal Challenge ◽  
E2 Glycoprotein ◽  
Viral Virulence ◽  
Viral Attenuation ◽  
Highly Virulent

Classical swine fever (CSF) is an economically important disease of pigs caused by the classical swine fever virus (CSFV). The live attenuated vaccine C-strain (also called HCLV strain) against CSF was produced by multiple passages of a highly virulent strain in rabbits. However, the molecular determinants for its attenuation and protection remain unclear. In this study, we identified a unique glycosylation at position 986 ( 986 NYT 988 ) on the E2 glycoprotein Domain IV of C-strain but not ( 986 NYA 988 ) the highly virulent CSFV Shimen strain. We evaluated the infectivity, virulence, and protective efficacy of the C-strain-based mutant rHCLV-T988A lacking the glycosylation and Shimen strain mutant rShimen-A988T acquiring an additional glycosylation at position 986. rShimen-A988T showed a significantly decreased viral replication ability in SK6 cells, while rHCLV-T988A exhibited a growth kinetics indistinguishable from that of C-strain. Removal of the C-strain glycosylation site does not affect viral replication in rabbits and the attenuated phenotype in pigs. However, rShimen-A988T was attenuated and protected the pigs from a lethal challenge at 14 days post-inoculation. In contrast, the rHCLV-T988A-inoculated pigs showed transient fever, a few clinical signs, and pathological changes in the spleens upon challenge with the Shimen strain. Mechanistic investigations revealed that the unique glycosylation at position 986 influences viral spreading, alters the formation of E2 homodimers, and leads to increased production of neutralizing antibodies. Collectively, our data for the first time demonstrate that the unique glycosylation at position 986 on the E2 glycoprotein is responsible for viral attenuation and protection. IMPORTANCE Viral glycoproteins involve in infectivity, virulence, and host immune responses. Deglycosylation on the E rns , E1, or E2 glycoprotein of highly virulent classical swine fever virus (CSFV) attenuated viral virulence in pigs, indicating that the glycosylation contributes to the pathogenicity of highly virulent strain. However, the effects of the glycosylation on the C-strain E2 glycoprotein on viral infectivity in cells, viral attenuation, and protection in pigs have not been elucidated. This study demonstrates the unique glycosylation at position 986 on the C-strain E2 glycoprotein. C-strain mutant removing the glycosylation at the site provides only partial protection against CSFV challenge. Remarkably, the addition of the glycan to E2 of the highly virulent Shimen strain attenuates the viral virulence and confers complete protection against the lethal challenge in pigs. Our findings provide a new insight into the contribution of the glycosylation to the virus attenuation and protection.

scholarly journals Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the Replication of Classical Swine Fever Virus

2015 ◽  
Vol 89 (16) ◽  
pp. 8510-8524 ◽  
Author(s):  
Su Li ◽  
Jinghan Wang ◽  
Wen-Rui He ◽  
Shuo Feng ◽  
Yongfeng Li ◽  
...  
Keyword(s):  
Viral Replication ◽  
Signaling Pathway ◽  
Classical Swine Fever Virus ◽  
Nuclear Translocation ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
E2 Protein ◽  
Cellular Events ◽  
Thioredoxin 2

ABSTRACTThe E2 protein of classical swine fever virus (CSFV) is an envelope glycoprotein that is involved in virus attachment and entry. To date, the E2-interacting cellular proteins and their involvement in viral replication have been poorly documented. In this study, thioredoxin 2 (Trx2) was identified to be a novel E2-interacting partner using yeast two-hybrid screening from a porcine macrophage cDNA library. Trx2 is a mitochondrion-associated protein that participates in diverse cellular events. The Trx2-E2 interaction was further confirmed by glutathioneS-transferase (GST) pulldown,in situproximity ligation, and laser confocal assays. The thioredoxin domain of Trx2 and the asparagine at position 37 (N37) in the E2 protein were shown to be critical for the interaction. Silencing of the Trx2 expression in PK-15 cells by small interfering RNAs significantly promotes CSFV replication, and conversely, overexpression of Trx2 markedly inhibits viral replication of the wild-type (wt) CSFV and to a greater extent that of the CSFV N37D mutant, which is defective in binding Trx2. The wt CSFV but not the CSFV N37D mutant was shown to reduce the Trx2 protein expression in PK-15 cells. Furthermore, we demonstrated that Trx2 increases nuclear factor kappa B (NF-κB) promoter activity by promoting the nuclear translocation of the p65 subunit of NF-κB. Notably, activation of the NF-κB signaling pathway induced by tumor necrosis factor alpha (TNF-α) significantly inhibits CSFV replication in PK-15 cells, whereas blocking the NF-κB activation in Trx2-overexpressing cells no longer suppresses CSFV replication. Taken together, our findings reveal that Trx2 inhibits CSFV replication via the NF-κB signaling pathway.IMPORTANCEThioredoxin 2 (Trx2) is a mitochondrion-associated protein that participates in diverse cellular events, such as antioxidative and antiapoptotic processes and the modulation of transcription factors. However, little is known about the involvement of Trx2 in viral replication. Here, we investigated, for the first time, the role of Trx2 in the replication of classical swine fever virus (CSFV), a devastating pestivirus of pigs. By knockdown and overexpression, we showed that Trx2 negatively regulates CSFV replication. Notably, we demonstrated that Trx2 inhibits CSFV replication by promoting the nuclear translocation of the p65 subunit of NF-κB, a key regulator of the host's innate immunity and inflammatory response. Our findings reveal a novel role of Trx2 in the host's antiviral response and provide new insights into the complex mechanisms by which CSFV interacts with the host cell.

ARFGAP1 binds to classical swine fever virus NS5A protein and enhances CSFV replication in PK-15 cells

2021 ◽  
Vol 255 ◽  
pp. 109034
Author(s):  
Liang Zhang ◽  
Mingxing Jin ◽  
Mengzhao Song ◽  
Shanchuan Liu ◽  
Tao Wang ◽  
...  
Keyword(s):  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Ns5a Protein

Genome Variability of Classical Swine Fever Virus during the 2018–2020 Epidemic in Japan

2021 ◽  
pp. 109128
Author(s):  
Tatsuya Nishi ◽  
Katsuhiko Fukai ◽  
Tomoko Kato ◽  
Kotaro Sawai ◽  
Takehisa Yamamoto
Keyword(s):  
Classical Swine Fever Virus ◽  
Classical Swine Fever ◽  
Fever Virus ◽  
Genome Variability
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