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CDC25B promotes influenza A virus replication by regulating the phosphorylation of nucleoprotein.
Abstract Cell division cycle 25 B (CDC25B) is a member of the CDC25 phosphatase family. It can dephosphorylate cyclin-dependent kinases and regulate the cell division cycle. Moreover, siRNA knockdown of CDC25B impairs influenza A virus (IAV) replication. Here, to further understand the regulatory mechanism of CDC25B for IAV replication, a CDC25B-knockout (KO) 293T cell line was constructed using CRISPR/Cas9. The present data indicated that the replication of IAV was decreased in CDC25B-KO cells. Additionally, CDC25B deficiency damaged viral polymerase activity, nucleoprotein (NP) self-oligomerization, and NP nucle...
Source: Virology - September 18, 2018 Category: Virology Authors: Cui L, Mahesutihan M, Zheng W, Meng L, Fan W, Li J, Ye X, Liu W, Sun L Tags: Virology Source Type: research

Small RNA-based interactions between rice and the viruses which cause the tungro disease.
Abstract Rice tungro disease is caused by a complex of two viruses, Rice tungro bacilliform virus (RTBV) and Rice tungro spherical virus (RTSV). To examine the RNAi-based defence response in rice during tungro disease, we characterized the virus-derived small RNAs and miRNAs by Deep Sequencing. We found that, while 21 nt/22 nt (nucleotide) siRNAs are predominantly produced in a continuous, overlapping and asymmetrical manner from RTBV, siRNA accumulation from RTSV were negligible. Additionally, 54 previously known miRNAs from rice, predicted to be regulating genes involved in plant defence, hormone signaling and d...
Source: Virology - August 3, 2018 Category: Virology Authors: Zarreen F, Kumar G, Johnson AMA, Dasgupta I Tags: Virology Source Type: research

The transmembrane nucleoporin Pom121 ensures efficient HIV-1 pre-integration complex nuclear import.
Abstract HIV-1 hijacks host classical cargo nuclear transportation, or nonclassical pathways by directly interacting with importin-β family proteins or nucleoporins for efficient pre-integration complex (PIC) nuclear import. Recently, an N-terminal truncated form of nucleoporin Pom121c (601-987 aa) was reported to inhibit HIV-1 replication. In contrast, we found that HIV-1 replication was significantly decreased in 293T and TZM-b1 cells with siRNA-mediated Pom121 knockdown. Quantitative PCR indicated that viral replication was impaired at the step of cDNA nuclear import. Furthermore, we found that karyopherin-β1...
Source: Virology - June 25, 2018 Category: Virology Authors: Guo J, Liu X, Wu C, Hu J, Peng K, Wu L, Xiong S, Dong C Tags: Virology Source Type: research

Cellular Hsp27 interacts with classical swine fever virus NS5A protein and negatively regulates viral replication by the NF- κB signaling pathway.
Cellular Hsp27 interacts with classical swine fever virus NS5A protein and negatively regulates viral replication by the NF-κB signaling pathway. Virology. 2018 Mar 08;518:202-209 Authors: Ling S, Luo M, Jiang S, Liu J, Ding C, Zhang Q, Guo H, Gong W, Tu C, Sun J Abstract Classical swine fever virus (CSFV) nonstructural protein NS5A is a multifunctional protein functioning in regulation of viral genome replication, protein translation and assembly by interaction with viral or host proteins. Here, heat shock protein 27 (Hsp27) has been identified as a novel binding partner of NS5A by using His tag "pu...
Source: Virology - March 8, 2018 Category: Virology Authors: Ling S, Luo M, Jiang S, Liu J, Ding C, Zhang Q, Guo H, Gong W, Tu C, Sun J Tags: Virology Source Type: research

Porcine reproductive and respiratory syndrome virus induces HMGB1 secretion via activating PKC-delta to trigger inflammatory response.
Abstract Porcine reproductive and respiratory syndrome virus (PRRSV) causes inflammatory injuries in infected pigs. PRRSV induces secretion of high mobility group box 1 (HMGB1) that enhances inflammatory response. However, the mechanism of PRRSV-induced HMGB1 secretion is unknown. Here, we discovered PRRSV induced HMGB1 secretion via activating protein kinase C-delta (PKCδ). HMGB1 secretion was positively correlated with PKCδ activation in PRRSV-infected cells in a dose and time-dependent manner. Suppression of PKCδ with inhibitor and siRNA significantly blocked PRRSV-induced HMGB1 translocation and secretion, ...
Source: Virology - March 6, 2018 Category: Virology Authors: Wang R, Yang L, Zhang Y, Li J, Xu L, Xiao Y, Zhang Q, Bai L, Zhao S, Liu E, Zhang YJ Tags: Virology Source Type: research

Aminopeptidase-N-independent entry of porcine epidemic diarrhea virus into Vero or porcine small intestine epithelial cells.
Abstract A monkey cell line Vero (ATCC CCL-81) is commonly used for porcine epidemic diarrhea virus (PEDV) propagation in vitro. However, it is still controversial whether the porcine aminopeptidase N (pAPN) counterpart on Vero cells (Vero-APN) confers PEDV entry. We found that endogenous expression of Vero-APN was undetectable in the mRNA and the protein levels in Vero cells. We cloned the partial Vero-APN gene (3340-bp) containing exons 1 to 9 from cellular DNA and subsequently generated two APN-knockout Vero cell lines by CRISPR/Cas9 approach. PEDV infection of two APN-knockout Vero cells had the same efficienc...
Source: Virology - March 1, 2018 Category: Virology Authors: Ji CM, Wang B, Zhou J, Huang YW Tags: Virology Source Type: research

Metalloprotease ADAM17 regulates porcine epidemic diarrhea virus infection by modifying aminopeptidase N.
Abstract Porcine epidemic diarrhea virus (PEDV) is a causative agent of porcine epidemic diarrhea (PED). PED, characterized by acute diarrhea, vomiting, dehydration, has caused serious economic losses in pig industry worldwide. Here, we demonstrate that activation of a disintergrin and metalloprotease 17 (ADAM17) induced the decrease of PEDV infection in HEK293 and IPEC-J2 cells and the downregulation of cell surface aminopeptidase N (APN) expression, an important entry factor for PEDV infection. Furthermore, overexpression of ADAM17 suppressed PEDV infection in HEK293 and IPEC-J2 cells, whereas ablation of ADAM17...
Source: Virology - February 20, 2018 Category: Virology Authors: Zhang J, Guo L, Yang L, Xu J, Zhang L, Feng L, Chen H, Wang Y Tags: Virology Source Type: research

B23/nucleophosmin interacts with bovine immunodeficiency virus Rev protein and facilitates viral replication.
Abstract The bovine immunodeficiency virus (BIV) Rev shuttling protein contains nuclear/nucleolar localization signals and nuclear import/export mechanisms that are novel among lentivirus Rev proteins. Several viral proteins localize to the nucleolus, which may play a role in processes that are essential to the outcome of viral replication. Although BIV Rev localizes to the nucleoli of transfected/infected cells and colocalizes with one of its major proteins, nucleophosmin (NPM1, also known as B23), the role of the nucleolus and B23 in BIV replication remains to be determined. Here, we demonstrate for the first ti...
Source: Virology - December 28, 2017 Category: Virology Authors: Passos-Castilho AM, Marchand C, Archambault D Tags: Virology Source Type: research

The eukaryotic translation initiation factor 3 subunit E binds to classical swine fever virus NS5A and facilitates viral replication.
Abstract Classical swine fever virus (CSFV) NS5A protein is a multifunctional protein, playing critical roles in viral RNA replication, translation and assembly. To further explore its functions in viral replication, interaction of NS5A with host factors was assayed using a his-tag "pull down" assay coupled with shotgun LC-MS/MS. Host protein translation initiation factor 3 subunit E was identified as a binding partner of NS5A, and confirmed by co-immunoprecipitation and co-localization analysis. Overexpression of eIF3E markedly enhanced CSFV genomic replication, viral protein expression and production of progeny ...
Source: Virology - December 7, 2017 Category: Virology Authors: Liu X, Wang X, Wang Q, Luo M, Guo H, Gong W, Tu C, Sun J Tags: Virology Source Type: research

Nuclear myosin 1 associates with papillomavirus E2 regulatory protein and influences viral replication.
We report herein that papillomavirus protein E2 binds to NM1 and co-precipitates with the WSTF and SNF2h proteins. Our data suggest that E2 associates with the cellular B-WICH complex through binding to NM1. E2 and NM1 associate via their N-terminal domains and this interaction is ATP dependent. The cellular multifunctional protein Brd4 and beta-actin are also present in the NM1-E2 complex. NM1 downregulation by siRNA increases the replication of the BPV1 and HPV5 genomes but does not affect HPV18 genome replication. These results suggest that the B-WICH complex may play a role in the papillomavirus life cycle through NM1 ...
Source: Virology - November 24, 2017 Category: Virology Authors: Sankovski E, Abroi A, Ustav M, Ustav M Tags: Virology Source Type: research

The down-regulation of casein kinase 1 alpha as a host defense response against infectious bursal disease virus infection.
In conclusion, down-regulation of CK1α during IBDV infection as a host defense response increased abundance of IFNAR1, which in turn enhanced an inhibitory effect on IBDV replication. PMID: 28988058 [PubMed - as supplied by publisher]
Source: Virology - October 4, 2017 Category: Virology Authors: Zhang L, Li H, Chen Y, Gao X, Lu Z, Gao L, Wang Y, Gao Y, Gao H, Liu C, Cui H, Zhang Y, Pan Q, Qi X, Wang X Tags: Virology Source Type: research

Protective role of Indoleamine 2,3 dioxygenase in Respiratory Syncytial Virus associated immune response in airway epithelial cells.
Abstract RSV is a major cause of severe lower respiratory infection in infants and young children. With no vaccine yet available, it is important to clarify mechanisms of disease pathogenesis. Since indoleamine-2,3-dioxygenase (IDO) is an immunomodulatory enzyme and is upregulated with RSV infection, we studied it in vivo during infection of BALB/c mice and in vitro in A549 cells. RSV infection upregulated IDO transcripts in vivo and in vitro. IDO siRNA decreased IDO transcripts ~2 fold compared to control siRNA after RSV infection but this decrease did not affect RSV replication. In the presence of IFN-γ, siRNA-...
Source: Virology - September 27, 2017 Category: Virology Authors: Rajan D, Chinnadurai R, Keefe EO, Boyoglu-Barnum S, Todd SO, Hartert TV, Galipeau J, Anderson LJ Tags: Virology Source Type: research

Porphyromonas gingivalis-mediated signaling through TLR4 mediates persistent HIV infection of primary macrophages.
Abstract Periodontal infections contribute to HIV-associated co-morbidities in the oral cavity and provide a model to interrogate the dysregulation of macrophage function, inflammatory disease progression, and HIV replication during co-infections. We investigated the effect of Porphyromonas gingivalis on the establishment of HIV infection in monocyte-derived macrophages. HIV replication in macrophages was significantly repressed in the presence of P. gingivalis. This diminished viral replication was due partly to a decrease in the expression of integrated HIV provirus. HIV repression depended upon signaling throug...
Source: Virology - September 14, 2016 Category: Virology Authors: Agosto LM, Hirnet JB, Michaels DH, Shaik-Dasthagirisaheb YB, Gibson FC, Viglianti G, Henderson AJ Tags: Virology Source Type: research

Inhibition of influenza A virus matrix and nonstructural gene expression using RNA interference.
Abstract Influenza antiviral drugs that use protein inhibitors can lose their efficacy as resistant strains emerge. As an alternative strategy, we investigated the use of small interfering RNA molecules (siRNAs) by characterizing three siRNAs (M747, M776 and M832) targeting the influenza matrix 2 gene and three (NS570, NS595 and NS615) targeting the nonstructural protein 1 and 2 genes. We also re-examined two previously reported siRNAs, M331 and M950, which target the matrix 1 and 2 genes. Treatment with M331-, M776-, M832-, and M950-siRNAs attenuated influenza titer. M776-siRNA treated cells had 29.8% less infect...
Source: Virology - July 26, 2016 Category: Virology Authors: McMillen CM, Beezhold DH, Blachere FM, Othumpangat S, Kashon ML, Noti JD Tags: Virology Source Type: research

Equine schlafen 11 restricts the production of equine infectious anemia virus via a codon usage-dependent mechanism.
Abstract Human schlafen11 is a novel restriction factor for HIV-1 based on bias regarding relative synonymous codon usage (RSCU). Here, we report the cloning of equine schlafen11 (eSLFN11) and the characteristics of its role in restricting the production of equine infectious anemia virus (EIAV), a retrovirus similar to HIV-1. Overexpression of eSLFN11 inhibited EIAV replication, whereas knockdown of endogenous eSLFN11 by siRNA enhanced the release of EIAV from its principal target cell. Notably, although eSLFN11 significantly suppressed expression of viral Gag protein and EIAV release into the culture medium, the ...
Source: Virology - May 16, 2016 Category: Virology Authors: Lin YZ, Sun LK, Zhu DT, Hu Z, Wang XF, Du C, Wang YH, Wang XJ, Zhou JH Tags: Virology Source Type: research

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