scholarly journals Discovery of Novel Antiviral Agents Directed Against the Influenza A Virus Nucleoprotein

10.5772/33573 ◽  
2012 ◽  
Author(s):  
Yoko Aida ◽  
Yutaka Sasaki ◽  
Kyoji Hagiwar
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Antiviral Agents

scholarly journals Salidroside Protects Against Influenza A Virus-Induced Acute Lung Injury in Mice

Dose-Response ◽  
2021 ◽  
Vol 19 (2) ◽  
pp. 155932582110113
Author(s):  
Rufeng Lu ◽  
Yueguo Wu ◽  
Honggang Guo ◽  
Zhuoyi Zhang ◽  
Yuzhou He
Keyword(s):  
Acute Lung Injury ◽  
Lung Injury ◽  
Influenza A Virus ◽  
Influenza A ◽  
H1n1 Virus ◽  
Antiviral Agents ◽  
Toll Like Receptor ◽  
Virus Infections ◽  
Toll Like Receptor 4 ◽  
Inflammatory Cytokine Production

Influenza A virus infections can cause acute lung injury (ALI) in humans; thus, the identification of potent antiviral agents is urgently required. Herein, the effects of salidroside on influenza A virus-induced ALI were investigated in a murine model. BALB/c mice were intranasally inoculated with H1N1 virus and treated with salidroside. The results of this study show that salidroside treatment (30 and 60 mg/kg) significantly attenuated the H1N1 virus-induced histological alterations in the lung and inhibited inflammatory cytokine production. Salidroside also decreased the wet/dry ratio, viral titers, and Toll-like receptor 4 expression in the lungs. Therefore, salidroside may represent a potential therapeutic reagent for the treatment of influenza A virus-induced ALI.

GFP-expressing influenza a virus for evaluation of the efficacy of antiviral agents

2012 ◽  
Vol 50 (2) ◽  
pp. 359-362 ◽  
Author(s):  
Jin Il Kim ◽  
Sehee Park ◽  
Ilseob Lee ◽  
Sangmoo Lee ◽  
Saem Shin ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Antiviral Agents

Discovery of novel antiviral agents directed against the influenza A virus nucleoprotein using photo-cross-linked chemical arrays

2010 ◽  
Vol 394 (3) ◽  
pp. 721-727 ◽  
Author(s):  
Kyoji Hagiwara ◽  
Yasumitsu Kondoh ◽  
Atsushi Ueda ◽  
Kazunori Yamada ◽  
Hideo Goto ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Antiviral Agents

scholarly journals Repurposing Kinase Inhibitors as Antiviral Agents to Control Influenza A Virus Replication

2015 ◽  
Vol 13 (10) ◽  
pp. 638-649 ◽  
Author(s):  
Olivia Perwitasari ◽  
Xiuzhen Yan ◽  
Jason O'Donnell ◽  
Scott Johnson ◽  
Ralph A. Tripp
Keyword(s):  
Influenza A Virus ◽  
Virus Replication ◽  
Influenza A ◽  
Kinase Inhibitors ◽  
Antiviral Agents

scholarly journals Synthesis and Evaluation of Some Masked Phosphate Esters of the Anti-Herpesvirus Drug 882C (Netivudine) as Potential Antiviral Agents

1998 ◽  
Vol 9 (3) ◽  
pp. 233-243 ◽  
Author(s):  
C McGuigan ◽  
A Perry ◽  
CJ Yarnold ◽  
PW Sutton ◽  
D Lowe ◽  
...  
Keyword(s):  
Influenza A Virus ◽  
Virus Type ◽  
Influenza A ◽  
Relative Rate ◽  
Antiviral Agents ◽  
Phosphate Esters ◽  
Lead Target ◽  
Immunodeficiency Virus ◽  
Simplex Virus

A number of symmetric and asymmetric 5′-phosphate esters of the potent anti-varicellazoster virus (VZV) agent 1–(β-d-arabinofuranosyl)-5-prop-1-ynyluracil (882C; netivudine) were prepared as potential lipophilic, membrane-soluble prodrugs of the bioactive phosphate forms. The compounds were prepared by the base-catalysed coupling of various phosphorochloridates with the free nucleoside analogue. Compounds were fully characterized by a range of spectroscopic and analytical methods and were studied for their inhibition of several viruses in tissue culture. All of the phosphate esters were inactive against human cytomegalovirus, herpes simplex virus type 2, VZV, human immunodeficiency virus type 1 and influenza A virus (EC50 >100 μM) except the 5′-(4–nitrophenyl phenyl) phosphate, which inhibited influenza A virus. The relative rate of esterase-mediated hydrolysis of one of the lead target structures was measured in order to rationalize the poor antiviral action, and data were collected on possible metabolites in support of this analysis. Cell-specific esterases are implicated as key determinants of the antiviral potency of prodrugs of this type.

scholarly journals A novel family of peptides with potent activity against influenza A viruses

2012 ◽  
Vol 93 (5) ◽  
pp. 980-986 ◽  
Author(s):  
Marlynne Q. Nicol ◽  
Yvonne Ligertwood ◽  
Matthew N. Bacon ◽  
Bernadette M. Dutia ◽  
Anthony A. Nash
Keyword(s):  
Influenza Virus ◽  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Antiviral Agents ◽  
Influenza Virus Infection ◽  
Influenza A Viruses ◽  
Potent Inhibition ◽  
Human Immunodeficiency Virus Entry ◽  
Drug Resistant Strains

The emergence of drug-resistant strains of influenza virus has catalysed a search for new antiviral agents to supplement or replace existing drugs. Following the success of the human immunodeficiency virus entry blocker Enfuvirtide, there has been a resurgence of interest in peptide-based antivirals. In this paper, we report on the discovery of a novel family of peptides (FluPep, FP) that function as inhibitors of influenza A virus infection. The prototype peptide (FP1, also known as Tkip) interacts with haemagglutinin and inhibits the binding of the virus to cell membranes. Using a plaque-reduction assay, we have demonstrated that a variety of influenza A virus subtypes (including H1N1, H3N2 and H5N1) are inhibited by FluPep and its derivatives at nanomolar concentrations. By truncating FluPep we have identified a minimal sequence of 6 aa that binds to haemagglutinin and inhibits infection. Using a mouse model of intranasal influenza virus infection, we observed potent inhibition of virus infection when peptide is given at the time of virus administration. These data indicate that FluPep is a highly effective anti-influenza agent with the potential to translate to the clinic.

Antiviral effect of polyphenol-enriched extract of Rumex Acetosa L. against Influenza A virus

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
A Derksen ◽  
W Hafezi ◽  
A Hensel ◽  
J Kühn
Keyword(s):  
Influenza A Virus ◽  
Influenza A ◽  
Antiviral Effect ◽  
Rumex Acetosa
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