Studies on co-infection of Peste des petits ruminants virus and orf virus In vitro

2021 ◽  
Vol 42 (1) ◽  
pp. 49-55
Author(s):  
P. Giridharan ◽  
Y. Krishnamohan Reddy
Keyword(s):  
Orf Virus ◽  
Peste Des Petits Ruminants

scholarly journals Correction to: In vitro and in vivo analyses of co‑infections with peste des petits ruminants and capripox vaccine strains

2021 ◽  
Vol 18 (1) ◽  
Author(s):  
Dajun Zhang ◽  
Bo Yang ◽  
Ting Zhang ◽  
Xijuan Shi ◽  
Chaochao Shen ◽  
...  
Keyword(s):  
Peste Des Petits Ruminants

An amendment to this paper has been published and can be accessed via the original article.

scholarly journals In vitro Antiviral Activity of Nigella sativa against Peste des Petits Ruminants (PPR) Virus

2018 ◽  
Vol 50 (6) ◽  
Author(s):  
Kiran Aqil ◽  
Muti-ur-Rehman Khan ◽  
Asim Aslam ◽  
Aqeel Javeed ◽  
Rizwan Qayyum ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Nigella Sativa ◽  
Peste Des Petits Ruminants ◽  
Ppr Virus

scholarly journals Effect of siRNA mediated suppression of signaling lymphocyte activation molecule on replication of peste des petits ruminants virus in vitro

2008 ◽  
Vol 136 (1-2) ◽  
pp. 118-123 ◽  
Author(s):  
Rahul Mohanchandra Pawar ◽  
G. Dhinakar Raj ◽  
T.M.A. Senthil Kumar ◽  
A. Raja ◽  
C. Balachandran
Keyword(s):  
Lymphocyte Activation ◽  
Peste Des Petits Ruminants

scholarly journals Orf virus encodes a functional dUTPase gene

2002 ◽  
Vol 83 (5) ◽  
pp. 1043-1048 ◽  
Author(s):  
R. Cottone ◽  
M. Büttner ◽  
C. J. McInnes ◽  
A. R. Wood ◽  
H.-J. Rziha
Keyword(s):  
Enzyme Activity ◽  
Fusion Protein ◽  
Enzymatic Activity ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Kinetic Studies ◽  
Orf Virus ◽  
Orfv Strain ◽  
Ph Range

The present study is the first report on the functional activity of a parapoxvirus-encoded dUTPase. The dUTPase gene of the attenuated orf virus (ORFV), strain D1701, was expressed as a bacterial thioredoxin fusion protein. In vitro assays showed that ORFV dUTPase was highly specific for dUTP as substrate. The enzyme was active over a broad pH range (pH 6·0–9·0), with maximal enzymatic activity at pH 7·0 in the presence of Mg2+ cations. Kinetic studies of the recombinant ORFV dUTPase revealed an apparent K m of 4·0 μM, which is more similar to that of the mammalian or African swine fever virus enzyme than to the K m of vaccinia virus dUTPase. Enzyme activity was also found with purified ORFV particles, indicating its virion association.

scholarly journals Antiviral Effectivity of Favipiravir Against Peste Des Petits Ruminants Virus Is Mediated by the JAK/STAT and PI3K/AKT Pathways

2021 ◽  
Vol 8 ◽  
Author(s):  
Weifeng Zhang ◽  
Hualong Deng ◽  
Yanfen Liu ◽  
Shaohong Chen ◽  
You Liu ◽  
...  
Keyword(s):  
Western Blotting ◽  
Effective Means ◽  
Small Ruminants ◽  
Antiviral Agent ◽  
Vero Cells ◽  
Host Cells ◽  
Peste Des Petits Ruminants ◽  
Expression Levels ◽  
Qrt Pcr

Peste des petits ruminants virus (PPRV), belonging to the genus Morbillivirus in the family Paramyxoviridae, causes severe infectious disease in small ruminants and has been rapidly spreading in many parts of Africa, the Middle East, and Asia. Although vaccination is considered to be an effective means of controlling PPR, the heat-sensitive nature of the vaccines against PPRV greatly limits their application in areas with a hot climate. In the present study, we investigated the anti-PPRV effects of favipiravir and sought to identify the underlying mechanisms in vitro using the Vero cell line. MTT assays, Western blotting, indirect immunofluorescence assays, virus plaque formation assays, and qRT-PCR were used to assess the effects of favipiravir on the life cycle of PPRV and the expression of RNA-dependent RNA polymerase (RdRp). Additionally, the expression levels of JAK1, STAT1, phosphorylated (p)-STAT1, PI3K, AKT, and p-AKT, as well as those of signaling molecules acting downstream of the JAK/STAT and PI3K/AKT signaling pathways, were determined by Western blotting and qRT-PCR. The results indicated that, in PPRV-infected, favipiravir-treated Vero cells, the attachment, invasion, replication, and release of PPRV were significantly inhibited, as was the expression of RdRp, when compared with that in untreated PPRV-infected cells. Furthermore, in favipiravir-treated cells, the expression of JAK1 and STAT1 was downregulated, whereas that of p-STAT1 was significantly upregulated. Similarly, the expression levels of PKR, IRF9, ISG54, and MxA proteins that are associated with innate antiviral activity in host cells were also markedly increased. Moreover, with favipiravir treatment, the expression of PI3K and p-AKT and the p-AKT/AKT ratio were significantly decreased, whereas the expression of AKT was noticeably upregulated. The expression of GSK3, NF-κB p65, p-NF-κB p65, and BAD was also increased with favipiravir treatment, while the expression of CREB, p-CREB, p-GSK3, and Bcl-2 was slightly decreased. In addition, all the p-GSK3/GSK3, p-CREB/CREB, p-NF-κB/NF-κB, and p-BAD/BAD ratios were significantly reduced in favipiravir-treated cells. These results implied that the antiviral effectivity of favipiravir against PPRV is mediated by the JAK/STAT and PI3K/AKT pathways and that favipiravir has potential for use as an effective antiviral agent against PPRV.

scholarly journals Regulation of PACT-Mediated Protein Kinase Activation by the OV20.0 Protein of Orf Virus

2015 ◽  
Vol 89 (22) ◽  
pp. 11619-11629 ◽  
Author(s):  
Yeu-Yang Tseng ◽  
Guan-Ru Liao ◽  
Ganes C. Sen ◽  
Fong-Yuan Lin ◽  
Wei-Li Hsu
Keyword(s):  
Protein Kinase ◽  
Rna Binding ◽  
Small Ruminants ◽  
Kinase Domain ◽  
Orf Virus ◽  
Infection Model ◽  
Content Type ◽  
Binding Domains ◽  
Mouse Infection Model

ABSTRACTDouble-stranded RNA (dsRNA)-activated protein kinase (PKR), a major component of the cellular antiviral system, is activated by the binding of either dsRNA or the cellular PKR activator, the PACT protein. The suppression of PKR activation is one of the main strategies that viruses employ to circumvent interferon signaling. Orf virus (ORFV), a parapoxvirus from thePoxviridaefamily, causes contagious pustular dermatitis in small ruminants. Previous studies have demonstrated that various OV20.0 isoforms, encoded by the OV20.0L gene, are able to inhibit PKR activation both by sequestering dsRNA and by physically interacting with PKRin vitro. Thus, this gene acts as a virulence factor of ORFV when tested using a mouse infection model. In the present study, the regions within OV20.0 that interact with dsRNA and with PKR have been mapped. Furthermore, this study demonstrates for the first time that OV20.0 is also able to interact with the dsRNA binding domain of PACT and that the presence of dsRNA strengthened the interaction of these two molecules. The presence of OV20.0 diminishes PKR phosphorylation when this is stimulated by PACT. Nevertheless, the association of OV20.0 with PKR, rather than with PACT, was found to be essential for reducing PACT-mediated PKR phosphorylation. These observations elucidate a new strategy whereby innate immunity can be evaded by ORFV.IMPORTANCEOur previous study indicated that ORFV's two OV20.0 isoforms act as a PKR antagonist via sequestering the PKR activator, dsRNA, and by interacting with PKR, leading to an inhibition of PKR activation (Y. Y. Tseng, F. Y. Lin, S. F. Cheng, D. Tscharke, S. Chulakasian, C. C. Chou, Y. F. Liu, W. S. Chang, M. L. Wong, and W. L. Hsu, J Virol89:4966–4979, 2015, doi:10.1128/JVI.03714-14). In the current study, the possible mechanisms by which OV20.0 protein counteracts PKR activation were studied in depth. OV20.0 is able to bind PKR and its two activators, dsRNA and PACT. In addition, OV20.0 binds directly to the RNA binding domains (RBDs) of PKR, and this interaction does not require dsRNA. Moreover, OV20.0 interacts with or occupies the RBD2 and the kinase domain of PKR, which then prevents PACT binding to PKR. Finally, OV20.0 associates with PACT via the RBDs, which may reduce the ability of PACT to induce PKR activation. The findings in this study provide new concepts in relation to how ORFV modulates PKR activation.

In vitro recognition of an orf virus early promoter in a vaccinia virus extract

1992 ◽  
Vol 123 (1-2) ◽  
pp. 223-228 ◽  
Author(s):  
J. C. Vos ◽  
A. A. Mercer ◽  
S. B. Fleming ◽  
A. J. Robinson
Keyword(s):  
Vaccinia Virus ◽  
Orf Virus ◽  
Early Promoter

Major mutation events in structural genes of peste des petits ruminants virus through serial passages in vitro

Virus Genes ◽  
2016 ◽  
Vol 52 (3) ◽  
pp. 422-427 ◽  
Author(s):  
Xiaodong Wu ◽  
Fuxiao Liu ◽  
Lin Li ◽  
Yanli Zou ◽  
Shan Liu ◽  
...  
Keyword(s):  
Peste Des Petits Ruminants ◽  
Structural Genes ◽  
Major Mutation

scholarly journals Inhibition of In Vitro Leukocyte Proliferation by Morbilliviruses

2002 ◽  
Vol 76 (7) ◽  
pp. 3579-3584 ◽  
Author(s):  
J. Heaney ◽  
T. Barrett ◽  
S. L. Cosby
Keyword(s):  
Immune Suppression ◽  
Measles Virus ◽  
Bacterial Infections ◽  
Peripheral Blood Lymphocytes ◽  
Peste Des Petits Ruminants ◽  
Proliferation Assay ◽  
In Vitro Proliferation ◽  
Lymphoblast Cell Line ◽  
Necessary And Sufficient

ABSTRACT Immune suppression associated with morbillivirus infections may influence the mortality rate by allowing secondary bacterial infections that are lethal to the host to flourish. Using an in vitro proliferation assay, we have shown that all members of the genus Morbillivirus inhibit the proliferation of a human B-lymphoblast cell line (BJAB). Proliferation of freshly isolated, stimulated bovine and caprine peripheral blood lymphocytes is also inhibited by UV-inactivated rinderpest (RPV) and peste-des-petits ruminants viruses. As for measles virus, coexpression of both the fusion and the hemagglutinin proteins of RPV is necessary and sufficient to induce immune suppression in vitro.

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