SrasV1, Main, Exploration, bibRecord, 001F67

SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity

Identifieur interne : 001F67 ( Main/Exploration ); précédent : 001F66; suivant : 001F68

SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity

Auteurs : Wei-Yen Wei [Taïwan] ; Hui-Chun Li [Taïwan] ; Chiung-Yao Chen [Taïwan] ; Chee-Hing Yang [Taïwan] ; Shen-Kao Lee [Taïwan] ; Chia-Wen Wang [Taïwan] ; Hsin-Chieh Ma [Taïwan] ; Yue-Li Juang [Taïwan] ; Shih-Yen Lo [Taïwan]

Source :

Archives of virology [ 0304-8608 ] ; 2012.

RBID : Pascal:12-0177763

Descripteurs français

Pascal (Inist)
- Virus syndrome respiratoire aigu sévère, Nucléocapside, Non-specific serine/threonine protein kinase, Pyruvate kinase.

English descriptors

KwdEn :
- Non-specific serine/threonine protein kinase, Nucleocapsid, Pyruvate kinase, Severe acute respiratory syndrome virus.

Abstract

The pathogenesis of SARS-CoV remains largely unknown. To study the function of the SARS-CoV nucleocapsid protein, we have conducted a yeast two-hybrid screening experiment to identify cellular proteins that may interact with the SARS-CoV nucleocapsid protein. Pyruvate kinase (liver) was found to interact with SARS-CoV nucleocapsid protein in this experiment. The binding domains of these two proteins were also determined using the yeast two-hybrid system. The physical interaction between the SARS-CoV nucleocapsid and cellular pyruvate kinase (liver) proteins was further confirmed by GST pull-down assay, co-immunoprecipitation assay and confocal microscopy. Cellular pyruvate kinase activity in hepatoma cells was repressed by SARS-CoV nucleocapsid protein in either transiently transfected or stably transfected cells. PK deficiency in red blood cells is known to result in human hereditary non-spherocytic hemolytic anemia. It is reasonable to assume that an inhibition of PKL activity due to interaction with SARS-CoV N protein is likely to cause the death of the hepatocytes, which results in the elevation of serum alanine aminotransferase and liver dysfunction noted in most SARS patients. Thus, our results suggest that SARS-CoV could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease.

Affiliations:

Taïwan

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The pathogenesis of SARS-CoV remains largely unknown. To study the function of the SARS-CoV nucleocapsid protein, we have conducted a yeast two-hybrid screening experiment to identify cellular proteins that may interact with the SARS-CoV nucleocapsid protein. Pyruvate kinase (liver) was found to interact with SARS-CoV nucleocapsid protein in this experiment. The binding domains of these two proteins were also determined using the yeast two-hybrid system. The physical interaction between the SARS-CoV nucleocapsid and cellular pyruvate kinase (liver) proteins was further confirmed by GST pull-down assay, co-immunoprecipitation assay and confocal microscopy. Cellular pyruvate kinase activity in hepatoma cells was repressed by SARS-CoV nucleocapsid protein in either transiently transfected or stably transfected cells. PK deficiency in red blood cells is known to result in human hereditary non-spherocytic hemolytic anemia. It is reasonable to assume that an inhibition of PKL activity due to interaction with SARS-CoV N protein is likely to cause the death of the hepatocytes, which results in the elevation of serum alanine aminotransferase and liver dysfunction noted in most SARS patients. Thus, our results suggest that SARS-CoV could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease.</div>
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   |clé=     Pascal:12-0177763
   |texte=   SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity
}}

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SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity

SARS-CoV nucleocapsid protein interacts with cellular pyruvate kinase protein and inhibits its activity

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