scholarly journals OL-046 Comparative study of rapid test with standard method RT-PCR for detection of influenza A virus infection in suspected cases admitted at Khonkaen Hospital, Thailand during 2005–2007

2009 ◽  
Vol 13 ◽  
pp. S44
Author(s):  
Pairoj Wechagama ◽  
Wisansanee Thaewpia ◽  
Rinjong Promsorn ◽  
Sompong Jinathongthai
Keyword(s):  
Virus Infection ◽  
Comparative Study ◽  
Influenza A Virus ◽  
Standard Method ◽  
Influenza A ◽  
Rapid Test ◽  
Rt Pcr ◽  
Influenza A Virus Infection

scholarly journals Nitrostative stress status during seasonal and pdmH1N1 infection in Iraq

2011 ◽  
Vol 5 (12) ◽  
pp. 863-867 ◽  
Author(s):  
Marwan S. M. Al-Nimer ◽  
Majid M Mahmood ◽  
Saba Saadoon Khazaal
Keyword(s):  
Nitric Oxide ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Healthy Subjects ◽  
Influenza A ◽  
Seasonal Influenza ◽  
Nitrosative Stress ◽  
Rt Pcr ◽  
One Step ◽  
Influenza A Virus Infection

Introduction: Influenza A virus infection is associated with oxidative and nitrosative stress. This study aimed to assess nitrosative stress in pandemic H1N1 (pdmH1N1) and seasonal influenza A infected patients. Methodology: The study included the following subjects:  20 patients infected with seasonal (negative one-step probe RT-PCR) influenza and 12 patients infected with pdmH1N1 (positive, one-step probe RT-PCR) influenza during the 2009 pandemic in Iraq. Twenty healthy subjects served as controls. Serum nitric oxide using Greiss reagent and peroxynitrite were used to assess nitrosative stress status. Results: Serum nitric oxide and peroxynitrite are significantly increased in patients infected with seasonal and pdmH1N1 influenza compared with the levels in healthy subjects. Infected patients with seasonal influenza showed significantly higher numbers of serum nitrogen species than corresponding pdmH1N1 infected patients. The turnover process reflected by the peroxynitrite/nitric oxide ratio was 0.177, 0.313 and 0.214 in healthy subjects, seasonal and pdmH1N1infected patients respectively. Conclusions: Influenza A virus infection is associated with significant nitrosative stress activity which is more pronounced in seasonal than in pdmH1N1 infected patients. The determination of serum nitric oxide and peroxynitrite may serve as biochemical markers.  

scholarly journals Induction of cyclophilin A by influenza A virus infection facilitates group A Streptococcus coinfection

Cell Reports ◽  
2021 ◽  
Vol 35 (7) ◽  
pp. 109159
Author(s):  
Xiaoyuan Bai ◽  
Wenxian Yang ◽  
Xiaohan Luan ◽  
Huizi Li ◽  
Heqiao Li ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Group A Streptococcus ◽  
Cyclophilin A ◽  
Group A ◽  
Influenza A Virus Infection

scholarly journals Dicer is involved in protection against influenza A virus infection

2007 ◽  
Vol 88 (10) ◽  
pp. 2627-2635 ◽  
Author(s):  
Alexey A. Matskevich ◽  
Karin Moelling
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Mammalian Cells ◽  
Influenza A ◽  
Virus Production ◽  
Vero Cells ◽  
Antiviral Response ◽  
Protein Levels ◽  
Infected Cells ◽  
Influenza A Virus Infection

In mammals the interferon (IFN) system is a central innate antiviral defence mechanism, while the involvement of RNA interference (RNAi) in antiviral response against RNA viruses is uncertain. Here, we tested whether RNAi is involved in the antiviral response in mammalian cells. To investigate the role of RNAi in influenza A virus-infected cells in the absence of IFN, we used Vero cells that lack IFN-α and IFN-β genes. Our results demonstrate that knockdown of a key RNAi component, Dicer, led to a modest increase of virus production and accelerated apoptosis of influenza A virus-infected cells. These effects were much weaker in the presence of IFN. The results also show that in both Vero cells and the IFN-producing alveolar epithelial A549 cell line influenza A virus targets Dicer at mRNA and protein levels. Thus, RNAi is involved in antiviral response, and Dicer is important for protection against influenza A virus infection.

scholarly journals A Functional Variation in CD55 Increases the Severity of 2009 Pandemic H1N1 Influenza A Virus Infection

2012 ◽  
Vol 206 (4) ◽  
pp. 495-503 ◽  
Author(s):  
Jie Zhou ◽  
Kelvin Kai-Wang To ◽  
Hui Dong ◽  
Zhong-Shan Cheng ◽  
Candy Choi-Yi Lau ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Influenza ◽  
Pandemic H1n1 ◽  
Functional Variation ◽  
Pandemic H1n1 Influenza ◽  
Influenza A Virus Infection

scholarly journals Dendritic cells and influenza A virus infection

Virulence ◽  
2012 ◽  
Vol 3 (7) ◽  
pp. 603-608 ◽  
Author(s):  
Jason Waithman ◽  
Justine D. Mintern
Keyword(s):  
Dendritic Cells ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Influenza A Virus Infection

Role of the chaperone protein 14-3-3ε in the regulation of influenza A virus-activated beta interferon

2021 ◽  
Author(s):  
Ee-Hong Tam ◽  
Yen-Chin Liu ◽  
Chian-Huey Woung ◽  
Helene Minyi Liu ◽  
Guan-Hong Wu ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Critical Role ◽  
Type I ◽  
Type I Ifn ◽  
Ns1 Protein ◽  
Chaperone Protein ◽  
Influenza A Virus Infection

The NS1 protein of the influenza A virus plays a critical role in regulating several biological processes in cells, including the type I interferon (IFN) response. We previously profiled the cellular factors that interact with the NS1 protein of influenza A virus and found that the NS1 protein interacts with proteins involved in RNA splicing/processing, cell cycle regulation, and protein targeting processes, including 14-3-3ε. Since 14-3-3ε plays an important role in RIG-I translocation to MAVS to activate type I IFN expression, the interaction of the NS1 and 14-3-3ε proteins may prevent the RIG-I-mediated IFN response. In this study, we confirmed that the 14-3-3ε protein interacts with the N-terminal domain of the NS1 protein and that the NS1 protein inhibits RIG-I-mediated IFN-β promoter activation in 14-3-3ε-overexpressing cells. In addition, our results showed that knocking down 14-3-3ε can reduce IFN-β expression elicited by influenza A virus and enhance viral replication. Furthermore, we found that threonine in the 49 th amino acid position of the NS1 protein plays a role in the interaction with 14-3-3ε. Influenza A virus expressing C-terminus-truncated NS1 with T49A mutation dramatically increases IFN-β mRNA in infected cells and causes slower replication than that of virus without the T-to-A mutation. Collectively, this study demonstrates that 14-3-3ε is involved in influenza A virus-initiated IFN-β expression and that the interaction of the NS1 protein and 14-3-3ε may be one of the mechanisms for inhibiting type I IFN activation during influenza A virus infection. IMPORTANCE Influenza A virus is an important human pathogen causing severe respiratory disease. The virus has evolved several strategies to dysregulate the innate immune response and facilitate its replication. We demonstrate that the NS1 protein of influenza A virus interacts with the cellular chaperone protein 14-3-3ε, which plays a critical role in RIG-I translocation that induces type I IFN expression, and that NS1 protein prevents RIG-I translocation to mitochondrial membrane. The interaction site for 14-3-3ε is the RNA-binding domain (RBD) of the NS1 protein. Therefore, this research elucidates a novel mechanism by which the NS1 RBD mediates IFN-β suppression to facilitate influenza A viral replication. Additionally, the findings reveal the antiviral role of 14-3-3ε during influenza A virus infection.

Sign in / Sign up

Export Citation Format

Share Document