Induction and suppression of type I interferon responses by mink enteritis virus in CRFK cells

Zhang, Xiaomei; Wang, Jigui; Mao, Yuxin; Xi, Ji; Yu, Yongle; Liu, Weiquan

doi:10.1016/j.vetmic.2016.12.002

Cited by 13 publications

(5 citation statements)

References 25 publications

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“…There are also limited studies on the NS1 protein, based only on evaluations of its functions [66,67,68] and on the potential location of its functional domains [10,22,23]. Changes in specific residues of NS1 CPV sequence [27] or affecting functional domains in others Carnivore protoparvovirus 1 such as mink enteritis parvovirus [69] were hypothesized as potentially affecting the functions of this protein. According to a previous study [22], several described changes lay in the encoding sequence of ORI binding, helicase, and transactivation functional domains (Figure 2), despite only helicase domains being analyzed in great detail [23].…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization and Evolutionary Analyses of Carnivore Protoparvovirus 1 NS1 Gene

Mira

Canuti

Purpari

et al. 2019

Viruses

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Carnivore protoparvovirus 1 is the etiological agent of a severe disease of terrestrial carnivores. This unique specie encompasses canine parvovirus type 2 (CPV-2) and feline panleukopenia virus (FPLV). Studies widely analyzed the main capsid protein (VP2), but limited information is available on the nonstructural genes (NS1/NS2). This paper analyzed the NS1 gene sequence of FPLV and CPV strains collected in Italy in 2009–2017, along with worldwide related sequences. Differently from VP2, only one NS1 amino-acid residue (248) clearly and constantly distinguished FPLV from CPV-2, while five possible convergent amino-acid changes were observed that may affect the functional domains of the NS1. Some synonymous mutation in NS1 were non-synonymous in NS2 and vice versa. No evidence for recombination between the two lineages was found, and the predominance of negative selection pressure on NS1 proteins was observed, with low and no overlap between the two lineages in negatively and positively selected codons, respectively. More sites were under selection in the CPV-2 lineage. NS1 phylogenetic analysis showed divergent evolution between FPLV and CPV, and strains were clustered mostly by country and year of detection. We highlight the importance of obtaining the NS1/NS2 coding sequence in molecular epidemiology investigations.

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Section: Discussionmentioning

confidence: 99%

Molecular Characterization and Evolutionary Analyses of Carnivore Protoparvovirus 1 NS1 Gene

Mira

Canuti

Purpari

et al. 2019

Viruses

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“…However, previous studies had shown that parvovirus infection can block the IFN-I pathway [13]. After infection, IFN-I fails to inhibit parvovirus replication [12], and we search for a novel antiviral factor, CaIRF1. Interestingly, CaIRF1 can inhibit the production of VSV and CPV-2 in MDCK cells and shows an adequate antiviral effect on MDCK cells.…”

Section: Discussionmentioning

confidence: 97%

“…3D). Third, according to previous studies, IFNβ exerts a small antiviral effect on parvovirus replication [12,13]. However, few studies have reported the mechanism by which this virus regulates CaIRF1 or whether CaIRF1 inhibits CPV-2 replication.…”

Section: Vsv and Cpv-2 Yields Were Low In Mdck-cairf1 Cellsmentioning

confidence: 98%

Molecular characterization and antiviral effects of canine interferon regulatory factor 1 (CaIRF1)

Hao

Chen

et al. 2022

BMC Vet Res

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Background Interferon regulatory factor 1 (IRF1) is an important transcription factor that activates the type I interferon (IFN-I) response and plays a vital role in the antiviral immune response. Although IRF1 has been identified in several mammals, little information related to its function in canines has been described. Results In this study, canine IRF1 (CaIRF1) was cloned. After a series of bioinformatics analyses, we found that the CaIRF1 protein structure was similar to that of other animal IRF1 proteins, including a conserved DNA-binding domain (DBD), an IRF-association domain 2 (IAD2) domain and two nuclear localization signals (NLSs). An indirect immunofluorescence assay (IFA) revealed that CaIRF1 was mainly distributed in the nucleus. Overexpression of CaIRF1 in Madin-Darby canine kidney cells (MDCK) induced high levels of interferon β (IFNβ) and IFN-stimulated response element (ISRE) promoter activation and induced interferon-stimulated gene (ISG) expression. Subsequently, we assayed the antiviral activity of CaIRF1 against vesicular stomatitis virus (VSV) and canine parvovirus type-2 (CPV-2) in MDCK cells. Overexpression of CaIRF1 effectively inhibited the viral yields of VSV and CPV-2, while knocking down of CaIRF1 expression mildly increased viral gene copies. Conclusions CaIRF1 is involved in the cellular IFN-I signaling pathway and plays an important role in the antiviral response.

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“…NS1 is a multifunctional protein, which is necessary for effective viral replication and production of infective virion [ 3 , 4 ]. It is related to cell apoptosis induction [ 5 , 6 ], cell cycle arrest and the suppression of type I interferon responses [ 7 , 8 ]. Mature NS2 mRNA is completely located in NS1 mRNA, which is formed by NS1 mRNA after alternative splicing.…”

Section: Introductionmentioning

confidence: 99%

SYNCRIP facilitates porcine parvovirus viral DNA replication through the alternative splicing of NS1 mRNA to promote NS2 mRNA formation

Chen

Miao

Chen

et al. 2021

Vet Res

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Porcine Parvovirus (PPV), a pathogen causing porcine reproductive disorders, encodes two capsid proteins (VP1 and VP2) and three nonstructural proteins (NS1, NS2 and SAT) in infected cells. The PPV NS2 mRNA is from NS1 mRNA after alternative splicing, yet the corresponding mechanism is unclear. In this study, we identified a PPV NS1 mRNA binding protein SYNCRIP, which belongs to the hnRNP family and has been identified to be involved in host pre-mRNA splicing by RNA-pulldown and mass spectrometry approaches. SYNCRIP was found to be significantly up-regulated by PPV infection in vivo and in vitro. We confirmed that it directly interacts with PPV NS1 mRNA and is co-localized at the cytoplasm in PPV-infected cells. Overexpression of SYNCRIP significantly reduced the NS1 mRNA and protein levels, whereas deletion of SYNCRIP significantly reduced NS2 mRNA and protein levels and the ratio of NS2 to NS1, and further impaired replication of the PPV. Furthermore, we found that SYNCRIP was able to bind the 3′-terminal site of NS1 mRNA to promote the cleavage of NS1 mRNA into NS2 mRNA. Taken together, the results presented here demonstrate that SYNCRIP is a critical molecule in the alternative splicing process of PPV mRNA, while revealing a novel function for this protein and providing a potential target of antiviral intervention for the control of porcine parvovirus disease.

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Induction and suppression of type I interferon responses by mink enteritis virus in CRFK cells

Cited by 13 publications

References 25 publications

Molecular Characterization and Evolutionary Analyses of Carnivore Protoparvovirus 1 NS1 Gene

Molecular Characterization and Evolutionary Analyses of Carnivore Protoparvovirus 1 NS1 Gene

Molecular characterization and antiviral effects of canine interferon regulatory factor 1 (CaIRF1)

SYNCRIP facilitates porcine parvovirus viral DNA replication through the alternative splicing of NS1 mRNA to promote NS2 mRNA formation

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