MAVS protein is attenuated by rotavirus nonstructural protein 1.

Rotavirus is the single, most important agent of infantile gastroenteritis in many animal species, including humans. In developing countries, rotavirus infection attributes approximately 500,000 deaths annually. Like other viruses it establishes an intimate and complex interaction with the host cell...

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Autores principales:	Satabdi Nandi, Shampa Chanda, Parikshit Bagchi, Mukti Kant Nayak, Rahul Bhowmick, Mamta Chawla-Sarkar
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2a20748201f845e2a53a0d26e1a03d9d
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spelling	oai:doaj.org-article:2a20748201f845e2a53a0d26e1a03d9d2021-11-18T08:27:26ZMAVS protein is attenuated by rotavirus nonstructural protein 1.1932-620310.1371/journal.pone.0092126https://doaj.org/article/2a20748201f845e2a53a0d26e1a03d9d2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24643253/?tool=EBIhttps://doaj.org/toc/1932-6203Rotavirus is the single, most important agent of infantile gastroenteritis in many animal species, including humans. In developing countries, rotavirus infection attributes approximately 500,000 deaths annually. Like other viruses it establishes an intimate and complex interaction with the host cell to counteract the antiviral responses elicited by the cell. Among various pattern recognition receptors (PAMPs) of the host, the cytosolic RNA helicases interact with viral RNA to activate the Mitochondrial Antiviral Signaling protein (MAVS), which regulates cellular interferon response. With an aim to identify the role of different PAMPs in rotavirus infected cell, MAVS was found to degrade in a time dependent and strain independent manner. Rotavirus non-structural protein 1 (NSP1) which is a known IFN antagonist, interacted with MAVS and degraded it in a strain independent manner, resulting in a complete loss of RNA sensing machinery in the infected cell. To best of our knowledge, this is the first report on NSP1 functionality where a signaling protein is targeted unanimously in all strains. In addition NSP1 inhibited the formation of detergent resistant MAVS aggregates, thereby averting the antiviral signaling cascade. The present study highlights the multifunctional role of rotavirus NSP1 and reinforces the fact that the virus orchestrates the cellular antiviral response to its own benefit by various back up strategies.Satabdi NandiShampa ChandaParikshit BagchiMukti Kant NayakRahul BhowmickMamta Chawla-SarkarPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 3, p e92126 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Satabdi Nandi Shampa Chanda Parikshit Bagchi Mukti Kant Nayak Rahul Bhowmick Mamta Chawla-Sarkar MAVS protein is attenuated by rotavirus nonstructural protein 1.
description	Rotavirus is the single, most important agent of infantile gastroenteritis in many animal species, including humans. In developing countries, rotavirus infection attributes approximately 500,000 deaths annually. Like other viruses it establishes an intimate and complex interaction with the host cell to counteract the antiviral responses elicited by the cell. Among various pattern recognition receptors (PAMPs) of the host, the cytosolic RNA helicases interact with viral RNA to activate the Mitochondrial Antiviral Signaling protein (MAVS), which regulates cellular interferon response. With an aim to identify the role of different PAMPs in rotavirus infected cell, MAVS was found to degrade in a time dependent and strain independent manner. Rotavirus non-structural protein 1 (NSP1) which is a known IFN antagonist, interacted with MAVS and degraded it in a strain independent manner, resulting in a complete loss of RNA sensing machinery in the infected cell. To best of our knowledge, this is the first report on NSP1 functionality where a signaling protein is targeted unanimously in all strains. In addition NSP1 inhibited the formation of detergent resistant MAVS aggregates, thereby averting the antiviral signaling cascade. The present study highlights the multifunctional role of rotavirus NSP1 and reinforces the fact that the virus orchestrates the cellular antiviral response to its own benefit by various back up strategies.
format	article
author	Satabdi Nandi Shampa Chanda Parikshit Bagchi Mukti Kant Nayak Rahul Bhowmick Mamta Chawla-Sarkar
author_facet	Satabdi Nandi Shampa Chanda Parikshit Bagchi Mukti Kant Nayak Rahul Bhowmick Mamta Chawla-Sarkar
author_sort	Satabdi Nandi
title	MAVS protein is attenuated by rotavirus nonstructural protein 1.
title_short	MAVS protein is attenuated by rotavirus nonstructural protein 1.
title_full	MAVS protein is attenuated by rotavirus nonstructural protein 1.
title_fullStr	MAVS protein is attenuated by rotavirus nonstructural protein 1.
title_full_unstemmed	MAVS protein is attenuated by rotavirus nonstructural protein 1.
title_sort	mavs protein is attenuated by rotavirus nonstructural protein 1.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/2a20748201f845e2a53a0d26e1a03d9d
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_version_	1718421730021605376

MAVS protein is attenuated by rotavirus nonstructural protein 1.

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