Microarray analysis reveals distinct signaling pathways transcriptionally activated by infection with bovine viral diarrhea virus in different cell types

Yamane, Daisuke; Zahoor, Muhammad Atif; Mohamed, Yassir Mahgoub; Azab, Walid; Kato, Kentaro; Tohya, Yukinobu; Akashi, Hiroomi

doi:10.1016/j.virusres.2009.02.015

Cited by 21 publications

(19 citation statements)

References 54 publications

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“…The data collectively suggested that NIBP inhibition allowed enhanced viral RNA replication. These data are in agreement with our other studies, where we have found that expression of NIBP is downregulated in BVDV-infected cells as revealed by microarray techniques (Yamane et al, 2009b). …”

supporting

confidence: 94%

“…It is known that NS5A is abundantly detected in BVDV-infected cells (Zahoor et al, 2009). Previously, we have reported that endogenous NIBP is downregulated in BVDV-infected cells (Yamane et al, 2009b). Although the molecular mechanisms underlying the pathogenesis of BVDV are poorly understood, we demonstrated that reduction of NIBP expression by siRNA enhanced virus RNA replication in both cp and ncp BVDV (Fig.…”

Section: Discussionmentioning

confidence: 55%

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Bovine viral diarrhea virus non-structural protein 5A interacts with NIK- and IKKβ-binding protein

Zahoor

Yamane

Mohamed

et al. 2010

Journal of General Virology

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Bovine viral diarrhea virus (BVDV) is a positive-sense, single-stranded RNA virus that causes an economically important livestock disease worldwide. Previous studies have suggested that nonstructural protein 5A (NS5A) from hepatitis C virus (HCV) and BVDV plays a similar role during virus infection. Extensive reports are available on HCV NS5A and its interactions with the host cellular proteins; however, the role of NS5A during BVDV infection remains largely unclear. To identify the cellular proteins that interact with the N terminus of NS5A and could be involved in its function, we conducted a yeast two-hybrid screening. As a result, we identified a cellular protein termed bovine NIK-and IKKb-binding protein (NIBP), which is involved in protein trafficking and nuclear factor kappa B (NF-kB) signalling in cells. The interaction of NS5A with NIBP was confirmed both in vitro and in vivo. Complementing our glutathione S-transferase pull-down and immunoprecipitation data are the confocal immunofluorescence results, which indicate that NS5A colocalized with NIBP on the endoplasmic reticulum in the cytoplasm of BVDV-infected cells. Moreover, the minimal residues of NIBP that interact with NS5A were mapped as aa 597-623. In addition, overexpression of NS5A inhibited NF-kB activation in HEK293 and LB9.K cells as determined by luciferase reporter-gene assay. We further showed that inhibition of endogenous NIBP by small interfering RNA molecules enhanced virus replication, indicating the importance of NIBP implications in BVDV pathogenesis. Being the first reported interaction between NIBP and a viral protein, this finding suggests a novel mechanism whereby viruses may subvert host-cell machinery for mediating trafficking as well as NF-kB signalling. INTRODUCTIONPestiviruses are important livestock pathogens that belong to the family Flaviviridae, which also includes the closely related genera Hepacivirus (Hepatitis C virus; HCV) and Flavivirus (Yellow fever virus and West Nile virus). The genus Pestivirus includes the species Bovine viral diarrhea virus 1 (BVDV-1), BVDV-2, Border disease virus and Classical swine fever virus. As a well-characterized prototype member of the genus Pestivirus within the family Flaviviridae, BVDV sometimes serves as a surrogate model for HCV life-cycle studies. BVDV is an enveloped virus containing a single, positive-sense RNA of approximately 12.3 kb. The genomic RNA consists of one long open reading frame (ORF), which is flanked by untranslated regions at both ends. The ORF encodes a single polyprotein of about 4000 aa, which is processed co-and posttranslationally by both viral and cellular proteases into at least 11 mature viral proteins (N pro , C, E rns , E1, E2, p7, NS2-3, NS4A, NS4B, NS5A and NS5B) (Lindenbach et al., 2007).BVDV non-structural protein 5A (NS5A) is a phosphoprotein of 56-58 kDa that plays an essential role in BVDV replication (Tellinghuisen et al., 2006) and shares many features with its counterpart HCV NS5A, e.g. both proteins are phosphorylated by the same or simila...

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supporting

confidence: 94%

Section: Discussionmentioning

confidence: 55%

Bovine viral diarrhea virus non-structural protein 5A interacts with NIK- and IKKβ-binding protein

Zahoor

Yamane

Mohamed

et al. 2010

Journal of General Virology

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“…A variety of other approaches were used to identify host factors important for pestivirus replication. Among them, yeast two-hybrid (Y2H) searches with individual viral proteins are the most frequently used (Doceul et al, 2008;Gladue, Baker-Bransetter, et al, 2014;Johns et al, 2010;Kang et al, 2012;Zahoor et al, 2010) followed by microarray techniques Yamane et al, 2009c). Other approaches relied on targeting possible interaction partners of viral proteins or RNA Fu, Shi, Shi, Meng, Bao, et al, 2014;He et al, 2012;Jordan, Nikolaeva, et al, 2002;Lin et al, 2014;Mohamed et al, 2014;Sheng et al, 2015;Wang et al, 2011;Yamane et al, 2009aYamane et al, , 2009b.…”

Section: Pestivirus-host Cell Interplaymentioning

confidence: 99%

The Molecular Biology of Pestiviruses

Tautz

Tews

Meyers

2015

Advances in Virus Research

200

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“…Moreover, gene chip analysis of RV‐infected adult and fetal fibroblasts showed that roughly 90% of the genes that were up‐ or downregulated were cell‐type specific [Adamo et al, 2008. Differences in the cellular response to bovine viral diarrhea virus infection were also observed in MDBK and BFM cells by microarray data analysis [Yamane et al, 2009.…”

Section: Discussionmentioning

confidence: 99%

Up the creek, with two paddles

Morrison¹

2010

Cathet Cardio Intervent

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Microarray analysis reveals distinct signaling pathways transcriptionally activated by infection with bovine viral diarrhea virus in different cell types

Cited by 21 publications

References 54 publications

Bovine viral diarrhea virus non-structural protein 5A interacts with NIK- and IKKβ-binding protein

Bovine viral diarrhea virus non-structural protein 5A interacts with NIK- and IKKβ-binding protein

The Molecular Biology of Pestiviruses

Up the creek, with two paddles

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