Abstract
Viral cycle progression depends upon host-cell processes in infected cells, and this is true for bovine viral diarrhoea virus (BVDV), the causative agent of BVD that is a worldwide threat to the bovine industry. Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme for heme degradation. Recent studies have demonstrated that HO-1 has significant antiviral properties, inhibiting the replication of viruses such as ebola virus, human immunodeficiency virus, hepatitis C virus, and porcine reproductive and respiratory syndrome virus. However, the function of HO-1 in BVDV infection is unclear. In the present study, the relationship between HO-1 and BVDV was investigated. In vitro analysis of HO-1 expression in BVDV-infected MDBK cells demonstrated that a decrease in HO-1 as BVDV replication increased. Increasing HO-1 expression through adenoviral-mediated overexpression or induction with cobalt protoporphyrin (CoPP, a potent HO-1 inducer), pre- and postinfection, effectively inhibited BVDV replication. In contrast, HO-1 siRNA knockdown in BVDV-infected cells increased BVDV replication. Therefore, the data were consistent with HO-1 acting as an anti-viral factor and these findings suggested that induction of HO-1 may be a useful prevention and treatment strategy against BVDV infection.
Highlights
Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme of heme degradation and catabolizes free heme into biliverdin, carbon monoxide and iron[6]
The results showed that the expression of HO-1 was down-regulated in Madin-darby Bovine Kidney (MDBK) cells following bovine viral diarrhoea virus (BVDV) infection, and that adenoviral-mediated overexpression or induction of HO-1 using the potent HO-1 inducer cobalt protoporphyrin (CoPP) effectively inhibited BVDV replication, which was reversed by prior siRNA knockdown
BVDV infection affects the expression of HO-1, we examined the abundance of BVDV, two antioxidant response element (ARE)-driven genes, including HO-1 and NADPH quinone oxidoreductase 1 (NQO1), and HO-2 mRNA and protein in MDBK cells infected with or without BVDV at different times by Quantitative reverse transcriptase-PCR (qRT-PCR) and Western blot
Summary
Heme oxygenase-1 (HO-1) is a ubiquitously expressed inducible isoform of the first and rate-limiting enzyme of heme degradation and catabolizes free heme into biliverdin, carbon monoxide and iron[6]. Recent studies have demonstrated that HO-1 has significant antiviral properties[8,9]. The effect of HO-1 induction on BVDV infection is unknown. The results showed that the expression of HO-1 was down-regulated in MDBK cells following BVDV infection, and that adenoviral-mediated overexpression or induction of HO-1 using the potent HO-1 inducer cobalt protoporphyrin (CoPP) effectively inhibited BVDV replication, which was reversed by prior siRNA knockdown. These results suggested that induction of HO-1 may be a useful prevention and treatment strategy against BVDV infection
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