Alteration of copper-zinc superoxide dismutase 1 expression by influenza A virus is correlated with virus replication.
Identifieur interne : 000F59 ( Main/Exploration ); précédent : 000F58; suivant : 000F60Alteration of copper-zinc superoxide dismutase 1 expression by influenza A virus is correlated with virus replication.
Auteurs : Chul-Woong Pyo [Corée du Sud] ; Nary Shin [Corée du Sud] ; Kwang Il Jung [Corée du Sud] ; Joon Hwan Choi [Corée du Sud] ; Sang-Yun Choi [Corée du Sud]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2014.
Descripteurs français
- KwdFr :
- Humains, Lignée cellulaire, Poumon (cytologie), Poumon (enzymologie), Poumon (virologie), Régulation de l'expression des gènes viraux (physiologie), Réplication virale (physiologie), Statistiques comme sujet, Superoxide dismutase (métabolisme), Superoxide dismutase-1, Virus de la grippe A (physiologie).
- MESH :
- cytologie : Poumon.
- enzymologie : Poumon.
- métabolisme : Superoxide dismutase.
- physiologie : Régulation de l'expression des gènes viraux, Réplication virale, Virus de la grippe A.
- virologie : Poumon.
- Humains, Lignée cellulaire, Statistiques comme sujet, Superoxide dismutase-1.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Superoxide Dismutase.
- cytology : Lung.
- enzymology : Lung.
- physiology : Gene Expression Regulation, Viral, Influenza A virus, Virus Replication.
- virology : Lung.
- Cell Line, Humans, Statistics as Topic, Superoxide Dismutase-1.
Abstract
Viruses have evolved mechanisms designated to potentiate virus replication by modulating the physiological condition of host cells. The generation of reactive oxygen species (ROS) during infection with influenza virus A (IAV) is a well-established mechanism in animals, but little is known about the generation of ROS in in vitro cell culture models and about its role in virus replication. We show here that IAV H1N1 infected human alveolar cells increased superoxide anion level mainly by suppressing the copper-zinc superoxide dismutase 1 (SOD1) gene, and that the SOD1-controlled generation of ROS was tightly correlated with virus replication. The transcription factor Sp1, which is a major element of the proximal region of the sod1 promoter, was slightly downregulated at the transcriptional level during IAV infection, and subsequently modulated by post-translational control. A gradual reduction of whole Sp1 was largely responsible for the repression of sod1 transcription with increasing time post-infection, and their rescue by the proteasome inhibitor, MG132, proved the involvement of proteasomal degradation in Sp1 regulation during IAV infection. Furthermore, we observed that expression of viral polymerase PB1 was inversely proportional to SOD1 level. The antioxidant N-acetyl-cysteine (NAC) neutralized IAV-mediated oxidative stress, and either NAC treatment or sod1 transfection considerably diminished viral polymerase activity. These data indicate that IAV-induced SOD1 repression, which may cause impaired redox balance in host cells, can be attributed, at least in part, to enhance viral replication.
DOI: 10.1016/j.bbrc.2014.06.037
PubMed: 24946209
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Viruses have evolved mechanisms designated to potentiate virus replication by modulating the physiological condition of host cells. The generation of reactive oxygen species (ROS) during infection with influenza virus A (IAV) is a well-established mechanism in animals, but little is known about the generation of ROS in in vitro cell culture models and about its role in virus replication. We show here that IAV H1N1 infected human alveolar cells increased superoxide anion level mainly by suppressing the copper-zinc superoxide dismutase 1 (SOD1) gene, and that the SOD1-controlled generation of ROS was tightly correlated with virus replication. The transcription factor Sp1, which is a major element of the proximal region of the sod1 promoter, was slightly downregulated at the transcriptional level during IAV infection, and subsequently modulated by post-translational control. A gradual reduction of whole Sp1 was largely responsible for the repression of sod1 transcription with increasing time post-infection, and their rescue by the proteasome inhibitor, MG132, proved the involvement of proteasomal degradation in Sp1 regulation during IAV infection. Furthermore, we observed that expression of viral polymerase PB1 was inversely proportional to SOD1 level. The antioxidant N-acetyl-cysteine (NAC) neutralized IAV-mediated oxidative stress, and either NAC treatment or sod1 transfection considerably diminished viral polymerase activity. These data indicate that IAV-induced SOD1 repression, which may cause impaired redox balance in host cells, can be attributed, at least in part, to enhance viral replication. </div>
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