Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
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Abstract
Porcine reproductive and respiratory syndrome (PRRS) virus is an RNA virus that replicates in the cytoplasm, but the viral nucleocapsid (N) protein localizes specifically in the nucleus and nucleolus of virus-infected cells. Nuclear localization of N is non-essential for PRRSV replication in cultured cells but has been shown to modulate the pathogenesis of virus in pigs, suggesting that N plays an accessory role in the nucleus during infection. We identified by yeast two-hybrid screening the inhibitor of MyoD family-a (I-mfa) domain-containing protein (HIC) as a cellular partner for PRRS virus (PRRSV) N protein. This protein is a homolog of human HIC, a recently identified cellular transcription factor. The specific interaction of PRRSV N with HIC was confirmed in cells by mammalian two-hybrid assay and co-immunoprecipitation and in vitro by GST pull-down assay. HIC is a zinc-binding protein and confocal microscopy demonstrated co-localization of N with the HIC-p40 isomer in the nucleus and nucleolus, and in the cytoplasm with HIC-p32, which is the N-terminal truncation of HIC-p40. The porcine homolog of HIC is universally expressed in pig tissues including alveolar macrophages. The interaction of viral capsid with the cellular transcription factor implicates a possible regulation of host cell gene expression by the N protein during PRRSV infection.
©2009 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Review
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- Protein Structure and Function
- Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
- Role of catalytic and non-catalytic subsite residues in ribonuclease activity of human eosinophil-derived neurotoxin
- Cell Biology and Signaling
- Expression and localization of atypical PKC isoforms in liver parenchymal cells
- Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
- The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
- Proteolysis
- Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
- The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
Articles in the same Issue
- Review
- Glutathione dysregulation and the etiology and progression of human diseases
- Protein Structure and Function
- Interaction of the porcine reproductive and respiratory syndrome virus nucleocapsid protein with the inhibitor of MyoD family-a domain-containing protein
- Role of catalytic and non-catalytic subsite residues in ribonuclease activity of human eosinophil-derived neurotoxin
- Cell Biology and Signaling
- Expression and localization of atypical PKC isoforms in liver parenchymal cells
- Regulation of phosphoenolpyruvate carboxylase in PVYNTN-infected tobacco plants
- The influence of linoleic and linolenic acid on the activity and intracellular localisation of phospholipase D in COS-1 cells
- Proteolysis
- Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
- The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells
- Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
