Influenza NS1 interacts with p53 and alters its binding to p53-responsive genes, in a promoter-dependent manner

Olivier Terrier; Audrey Diederichs; Julia Dubois; Gaëlle Cartet; Bruno Lina; Jean-Christophe Bourdon; Manuel Rosa-Calatrava

doi:10.1016/j.febslet.2013.08.006

Influenza NS1 interacts with p53 and alters its binding to p53-responsive genes, in a promoter-dependent manner

Olivier Terrier
, Audrey Diederichs
, Julia Dubois
, Gaëlle Cartet
, Bruno Lina
, Jean-Christophe Bourdon
, Manuel Rosa-Calatrava

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

The interplay between influenza A viruses (IAV) and p53 has only been reported in a limited number of studies, mainly focusing on the antiviral role of p53. We investigated the impact of IAV infection on p53 stability and transcriptional activity. Our results indicate that IAV-induced stabilization of p53 only partially correlates with modulation of p53 transcriptional activity measured during infection. Moreover, we show that the viral non-structural protein 1 (NS1) is able to inhibit p53 transcriptional activity, in a promoter-dependent manner. Based on these data, we propose that NS1 may contribute to p53-mediated cell fate decision during IAV infection.

Original language	English
Pages (from-to)	2965-2971
Number of pages	7
Journal	FEBS Letters
Volume	587
Issue number	18
DOIs	https://doi.org/10.1016/j.febslet.2013.08.006
Publication status	Published - 13 Aug 2013

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10.1016/j.febslet.2013.08.006

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title = "Influenza NS1 interacts with p53 and alters its binding to p53-responsive genes, in a promoter-dependent manner",

abstract = "The interplay between influenza A viruses (IAV) and p53 has only been reported in a limited number of studies, mainly focusing on the antiviral role of p53. We investigated the impact of IAV infection on p53 stability and transcriptional activity. Our results indicate that IAV-induced stabilization of p53 only partially correlates with modulation of p53 transcriptional activity measured during infection. Moreover, we show that the viral non-structural protein 1 (NS1) is able to inhibit p53 transcriptional activity, in a promoter-dependent manner. Based on these data, we propose that NS1 may contribute to p53-mediated cell fate decision during IAV infection.",

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T1 - Influenza NS1 interacts with p53 and alters its binding to p53-responsive genes, in a promoter-dependent manner

AU - Terrier, Olivier

AU - Diederichs, Audrey

AU - Dubois, Julia

AU - Cartet, Gaëlle

AU - Lina, Bruno

AU - Bourdon, Jean-Christophe

AU - Rosa-Calatrava, Manuel

PY - 2013/8/13

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N2 - The interplay between influenza A viruses (IAV) and p53 has only been reported in a limited number of studies, mainly focusing on the antiviral role of p53. We investigated the impact of IAV infection on p53 stability and transcriptional activity. Our results indicate that IAV-induced stabilization of p53 only partially correlates with modulation of p53 transcriptional activity measured during infection. Moreover, we show that the viral non-structural protein 1 (NS1) is able to inhibit p53 transcriptional activity, in a promoter-dependent manner. Based on these data, we propose that NS1 may contribute to p53-mediated cell fate decision during IAV infection.

AB - The interplay between influenza A viruses (IAV) and p53 has only been reported in a limited number of studies, mainly focusing on the antiviral role of p53. We investigated the impact of IAV infection on p53 stability and transcriptional activity. Our results indicate that IAV-induced stabilization of p53 only partially correlates with modulation of p53 transcriptional activity measured during infection. Moreover, we show that the viral non-structural protein 1 (NS1) is able to inhibit p53 transcriptional activity, in a promoter-dependent manner. Based on these data, we propose that NS1 may contribute to p53-mediated cell fate decision during IAV infection.

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DO - 10.1016/j.febslet.2013.08.006

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EP - 2971

JO - FEBS Letters

JF - FEBS Letters

IS - 18

ER -

Influenza NS1 interacts with p53 and alters its binding to p53-responsive genes, in a promoter-dependent manner

Abstract

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