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Open AccessJournal ArticleDOI

Cellular DDX21 RNA Helicase Inhibits Influenza A Virus Replication but Is Counteracted by the Viral NS1 Protein

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TLDR
As sequential interaction of PB1 and NS1 with DDX21 leads to temporal regulation of viral gene expression, influenza A virus likely uses theDDX21-NS1 interaction not only to overcome restriction, but also to regulate the viral life cycle.
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This article is published in Cell Host & Microbe.The article was published on 2014-04-09 and is currently open access. It has received 99 citations till now. The article focuses on the topics: Viral structural protein & Viral entry.

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Journal ArticleDOI

Host and viral determinants of influenza A virus species specificity.

TL;DR: The host barriers that influenza A viruses of animals, especially birds, must overcome to initiate a pandemic in humans are examined and how, on crossing the species barrier, the virus mutates to establish new interactions with the human host is described.
Journal ArticleDOI

Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement.

TL;DR: The aim of this review is to present the current mechanistic understanding for how IAVs facilitate cell entry, replication, virion assembly, and intercellular movement, in an effort to highlight some of the unanswered questions regarding the coordination of the IAV infection process.
Book ChapterDOI

The NS1 protein: a multitasking virulence factor

TL;DR: The many roles that have been ascribed to the NS1 protein are overviewed, and insights into the sequence features and structural properties that make them possible are given, highlighting the need to understand how NS1 can actually perform all of these functions during viral infection.
Journal ArticleDOI

Influenza virus non-structural protein NS1: interferon antagonism and beyond.

TL;DR: A better understanding of NS1 could help in elaborating novel antiviral strategies, based on either live vaccines with altered NS1 or on small-compound inhibitors ofNS1.
Journal ArticleDOI

Tombusvirus-Host Interactions: Co-Opted Evolutionarily Conserved Host Factors Take Center Court

TL;DR: The viral replication process based on tombusviruses is described, highlighting common strategies with other plant and animal viruses, and advances in understanding of tombusvirus-host interactions are broadly applicable to many other viruses, which also usurp conserved host factors for various viral processes.
References
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Journal ArticleDOI

Strategies for mitigating an influenza pandemic

TL;DR: It is found that border restrictions and/or internal travel restrictions are unlikely to delay spread by more than 2–3 weeks unless more than 99% effective, and vaccine stockpiled in advance of a pandemic could significantly reduce attack rates even if of low efficacy.
Journal ArticleDOI

Influenza A Virus NS1 Targets the Ubiquitin Ligase TRIM25 to Evade Recognition by the Host Viral RNA Sensor RIG-I

TL;DR: This work reports that the influenza A virus nonstructural protein 1 (NS1) specifically inhibits TRIM25-mediated RIG-I CARD ubiquitination, thereby suppressing Rig-I signal transduction and revealing a mechanism by which influenza virus inhibits host IFN response.
Journal ArticleDOI

Avian flu: isolation of drug-resistant H5N1 virus.

TL;DR: The isolation of an H5N1 virus from a Vietnamese girl that is resistant to the drug oseltamivir, which is an inhibitor of the viral enzyme neuraminidase and is currently used for protection against and treatment of influenza is reported.
Journal ArticleDOI

Permissive Secondary Mutations Enable the Evolution of Influenza Oseltamivir Resistance

TL;DR: It is shown that H274Y decreases the amount of neuraminidase that reaches the cell surface and that this defect can be counteracted by secondary mutations that also restore viral fitness.
Journal ArticleDOI

Influenza Virus NS1 Protein Interacts with the Cellular 30 kDa Subunit of CPSF and Inhibits 3′ End Formation of Cellular Pre-mRNAs

TL;DR: It is demonstrated that the NS1 effector domain functionally interacts with the cellular 30 kDa subunit of CPSF, an essential component of the 3' end processing machinery of cellular pre-mRNAs.
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