Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling

Chinnakannan, Senthil; Holzer, Barbara; Bernardo, Beatriz Sanz; Nanda, Sambit K.; Baron, Michael D.

doi:10.1099/vir.0.056739-0

Cited by 17 publications

(14 citation statements)

References 30 publications

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“…We tested if the expression in trans of the PPRV V protein was also able to block the MDA-5-mediated activation of the IFN-β promoter, comparing it to the V protein of PIV5 (the paramyxovirus that has been the model to study the role of the V protein) and the V protein of another morbillivirus, RPV, which has previously been shown to affect host IFN signalling [58–60]. We transfected VHS cells with the reporter plasmids and plasmids encoding the selected V proteins and induced the activation of the MDA-5 signalling cascade by transfection of poly(I:C).…”

Section: Resultsmentioning

confidence: 99%

Control of the induction of type I interferon by Peste des petits ruminants virus

2017

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Peste des petits ruminants virus (PPRV) is a morbillivirus that produces clinical disease in goats and sheep. We have studied the induction of interferon-β (IFN-β) following infection of cultured cells with wild-type and vaccine strains of PPRV, and the effects of such infection with PPRV on the induction of IFN-β through both MDA-5 and RIG-I mediated pathways. Using both reporter assays and direct measurement of IFN-β mRNA, we have found that PPRV infection induces IFN-β only weakly and transiently, and the virus can actively block the induction of IFN-β. We have also generated mutant PPRV that lack expression of either of the viral accessory proteins (V&C) to characterize the role of these proteins in IFN-β induction during virus infection. Both PPRV_ΔV and PPRV_ΔC were defective in growth in cell culture, although in different ways. While the PPRV V protein bound to MDA-5 and, to a lesser extent, RIG-I, and over-expression of the V protein inhibited both IFN-β induction pathways, PPRV lacking V protein expression can still block IFN-β induction. In contrast, PPRV C bound to neither MDA-5 nor RIG-I, but PPRV lacking C protein expression lost the ability to block both MDA-5 and RIG-I mediated activation of IFN-β. These results shed new light on the inhibition of the induction of IFN-β by PPRV.

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Section: Resultsmentioning

confidence: 99%

Control of the induction of type I interferon by Peste des petits ruminants virus

2017

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“…Moreover, a zinc finger domain and specific residues in the carboxy-terminal domain of the MeV V protein were shown to interact with STAT2 [26]. In RPV, the amino-terminal domain of the V protein binds to STAT1, whereas the carboxy-terminal domain interacts with the IFN receptor-associated kinases JAK1 and TYK2 [7]. Both RPV amino-and carboxy-V domains were required to block the IFN-induced antiviral state [7].…”

Section: Discussionmentioning

confidence: 99%

Retraction: Peste des petits ruminants virus V protein inhibits cellular antiviral response by blocking the secretion of endogenous and exogenous interferons

Shi

Zhang

et al. 2020

J. Vet. Med. Sci.

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“…Six amino acid changes were found in the reading frame of the V protein and two amino acid changes were found in the reading frame of the C protein. The V and C proteins both play important roles in the inhibition of interferons (Nanda & Baron 2006;Chinnakannan et al, 2014) and influence the antiviral host response. Additionally, the C protein is believed to affect the transcription of mRNA of the viral genes (Baron & Barrett 2000) and this could explain why the percentage of changes is lower than the V protein.…”

Section: New Insights To Pdv Virus Evolutionmentioning

confidence: 99%

Phylogenomic insights to the origin and spread of phocine distemper virus in European harbour seals in 1988 and 2002

Stokholm

Härkönen²,

Hårding³

et al. 2019

Dis. Aquat. Org.

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The 1988 and 2002 Phocine Distemper Virus (PDV) outbreaks in European harbour seals (Phoca vitulina) are among the largest mass mortality events recorded in marine mammals. Despite its large impact on harbour seal population numbers, and three decades of studies, many questions regarding the spread and temporal origin of PDV remain unanswered. Here, we sequenced and analysed 7,123 base pairs of the PDV genome, including the coding and non-coding regions of the entire P, M, F and H genes in tissues from 44 harbour seals to shed new light on the origin and spread of PDV in 1988 and 2002. The phylogenetic analyses trace the origin of the PDV strain causing the 1988 outbreak to between May 1987 and April 1988, while the origin of the strain causing the 2002 outbreak can be traced back to between June 2001 and May 2002. The analyses further point to several independent introductions of PDV in 1988, possibly linked to a southward mass immigration of harp seals in the winter and spring of 1987-1988. The vector for the 2002 outbreak is unknown, but the epidemiological analyses suggest that the subsequent spread of PDV from the epicentre in Kattegat, Denmark, to haul-out sites in the North Sea through several independent introductions.

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Different functions of the common P/V/W and V-specific domains of rinderpest virus V protein in blocking IFN signalling

Cited by 17 publications

References 30 publications

Control of the induction of type I interferon by Peste des petits ruminants virus

Control of the induction of type I interferon by Peste des petits ruminants virus

Retraction: Peste des petits ruminants virus V protein inhibits cellular antiviral response by blocking the secretion of endogenous and exogenous interferons

Phylogenomic insights to the origin and spread of phocine distemper virus in European harbour seals in 1988 and 2002

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