Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.

The NS1 protein from avian influenza A viruses contains a PDZ binding motif (PBM) at its carboxyl terminus with the consensus sequence ESEV. The ESEV PBM confers binding to several cellular PDZ proteins, including Dlg1, MAGI-1 and Scribble. The interaction between NS1 and Scribble protects infected...

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Autores principales:	Manish Kumar, Hongbing Liu, Andrew P Rice
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/9387cd57eb6d4a76a6d6884f504fbcd6
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spelling	oai:doaj.org-article:9387cd57eb6d4a76a6d6884f504fbcd62021-11-18T07:11:41ZRegulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.1932-620310.1371/journal.pone.0041251https://doaj.org/article/9387cd57eb6d4a76a6d6884f504fbcd62012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22911767/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203The NS1 protein from avian influenza A viruses contains a PDZ binding motif (PBM) at its carboxyl terminus with the consensus sequence ESEV. The ESEV PBM confers binding to several cellular PDZ proteins, including Dlg1, MAGI-1 and Scribble. The interaction between NS1 and Scribble protects infected cells from apoptosis, while the interaction between NS1 and both Dlg1 and Scribble disrupts tight junctions. In this study, we examined the MAGI-1 protein. We made the unexpected observation that siRNA depletion of MAGI-1 activates IRF3 and induces the IFN-β promoter. We found that the ESEV NS1 protein sequesters MAGI-1 away from the plasma membrane in infected cells. Using plasmid vectors to express NS1 proteins, we observed that the ESEV PBM elicits an IFN-β induction signal as indicated by activation of IRF3 and a relative deficiency in NS1 inhibition of induction of the IFN-β promoter by dsRNA or RIG-I. Taken together, our data suggest that disruption of MAGI-1 by the ESEV PBM activates an IFN-β induction signal. During viral infection, however, induction of the IFN-β gene does not occur presumably because other anti-IFN functions dominate over the IFN-activation activity of the ESEV PBM. We postulate that the ESEV PBM's broad binding activity for PDZ proteins may allow NS1 to bind to some PDZ proteins such as MAGI-1 that confer no benefit or may even be detrimental to viral replication. However, the advantage of binding to key PDZ proteins such as Dlg1 and Scribble may dominate and therefore provide an overall benefit for the virus to encode the ESEV PBM.Manish KumarHongbing LiuAndrew P RicePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 7, p e41251 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Manish Kumar Hongbing Liu Andrew P Rice Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.
description	The NS1 protein from avian influenza A viruses contains a PDZ binding motif (PBM) at its carboxyl terminus with the consensus sequence ESEV. The ESEV PBM confers binding to several cellular PDZ proteins, including Dlg1, MAGI-1 and Scribble. The interaction between NS1 and Scribble protects infected cells from apoptosis, while the interaction between NS1 and both Dlg1 and Scribble disrupts tight junctions. In this study, we examined the MAGI-1 protein. We made the unexpected observation that siRNA depletion of MAGI-1 activates IRF3 and induces the IFN-β promoter. We found that the ESEV NS1 protein sequesters MAGI-1 away from the plasma membrane in infected cells. Using plasmid vectors to express NS1 proteins, we observed that the ESEV PBM elicits an IFN-β induction signal as indicated by activation of IRF3 and a relative deficiency in NS1 inhibition of induction of the IFN-β promoter by dsRNA or RIG-I. Taken together, our data suggest that disruption of MAGI-1 by the ESEV PBM activates an IFN-β induction signal. During viral infection, however, induction of the IFN-β gene does not occur presumably because other anti-IFN functions dominate over the IFN-activation activity of the ESEV PBM. We postulate that the ESEV PBM's broad binding activity for PDZ proteins may allow NS1 to bind to some PDZ proteins such as MAGI-1 that confer no benefit or may even be detrimental to viral replication. However, the advantage of binding to key PDZ proteins such as Dlg1 and Scribble may dominate and therefore provide an overall benefit for the virus to encode the ESEV PBM.
format	article
author	Manish Kumar Hongbing Liu Andrew P Rice
author_facet	Manish Kumar Hongbing Liu Andrew P Rice
author_sort	Manish Kumar
title	Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.
title_short	Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.
title_full	Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.
title_fullStr	Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.
title_full_unstemmed	Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.
title_sort	regulation of interferon-β by magi-1 and its interaction with influenza a virus ns1 protein with esev pbm.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/9387cd57eb6d4a76a6d6884f504fbcd6
work_keys_str_mv	AT manishkumar regulationofinterferonbbymagi1anditsinteractionwithinfluenzaavirusns1proteinwithesevpbm AT hongbingliu regulationofinterferonbbymagi1anditsinteractionwithinfluenzaavirusns1proteinwithesevpbm AT andrewprice regulationofinterferonbbymagi1anditsinteractionwithinfluenzaavirusns1proteinwithesevpbm
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Regulation of interferon-β by MAGI-1 and its interaction with influenza A virus NS1 protein with ESEV PBM.

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