tetano
Editor, Senior Moderator
J Gen Virol. 2014 Jun 13. pii: vir.0.066282-0. doi: 10.1099/vir.0.066282-0. [Epub ahead of print]
Conformational plasticity of the influenza A virus NS1 protein.
Hale BG.
Author information
Abstract
During infection the influenza A virus NS1 protein interacts with a diverse range of viral and cellular factors to antagonize host antiviral defences and promote viral replication. Here, I review the structural basis for some of these functions, and discuss the emerging view that NS1 cannot simply be regarded as a 'static' protein with a single structure. Rather, the dynamic property of NS1 to adopt various quaternary conformations is critical for its multiple activities. Understanding NS1 plasticity, and the mechanisms governing this, will be essential for assessing both fundamental protein function and the consequences of strain-dependent polymorphisms in this important virulence factor.
Copyright ? 2014, the Society for General Microbiology.
KEYWORDS:
NS1; influenza; interferon; multimerization; virulence
PMID:
24928909
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24928909
Conformational plasticity of the influenza A virus NS1 protein.
Hale BG.
Author information
Abstract
During infection the influenza A virus NS1 protein interacts with a diverse range of viral and cellular factors to antagonize host antiviral defences and promote viral replication. Here, I review the structural basis for some of these functions, and discuss the emerging view that NS1 cannot simply be regarded as a 'static' protein with a single structure. Rather, the dynamic property of NS1 to adopt various quaternary conformations is critical for its multiple activities. Understanding NS1 plasticity, and the mechanisms governing this, will be essential for assessing both fundamental protein function and the consequences of strain-dependent polymorphisms in this important virulence factor.
Copyright ? 2014, the Society for General Microbiology.
KEYWORDS:
NS1; influenza; interferon; multimerization; virulence
PMID:
24928909
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24928909