scholarly journals Effects of microvirin monomers and oligomers on hepatitis C virus

2017 ◽  
Vol 37 (3) ◽  
Author(s):  
Yuan-Qin Min ◽  
Xu-Chu Duan ◽  
Yi-Dan Zhou ◽  
Anna Kulinich ◽  
Wang Meng ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Specificity ◽  
Antiviral Effect ◽  
Carbohydrate Binding ◽  
Viral Inhibition ◽  
Linker Sequence ◽  
Carbohydrate Binding Protein ◽  
High Mannose ◽  
Tetrameric Form

Microvirin (MVN) is a carbohydrate-binding protein which shows high specificity for high-mannose type N-glycan structures. In the present study, we tried to identify whether MVN could bind to high-mannose containing hepatitis C virus (HCV) envelope glycoproteins, which are heavily decorated high-mannose glycans. In addition, recombinantly expressed MVN oligomers in di-, tri- and tetrameric form were evaluated for their viral inhibition. MVN oligomers bound more efficiently to HCV virions, and displayed in comparison with the MVN monomer a higher neutralization potency against HCV infection. The antiviral effect was furthermore affected by the peptide linker sequence connecting the MVN monomers. The results indicate that MVN oligomers such as trimers and tetramers may be used as future neutralization agents against HCV infections.

Antiviral effect of ribonuclease conjugated oligodeoxynucleotides targeting the IRES RNA of the hepatitis C virus

2009 ◽  
Vol 19 (13) ◽  
pp. 3581-3585 ◽  
Author(s):  
Carly Gamble ◽  
Maud Trotard ◽  
Jacques Le Seyec ◽  
Valérie Abreu-Guerniou ◽  
Nicolas Gernigon ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Antiviral Effect

Antiviral effect of human recombinant interleukin-12 in patients infected with hepatitis C virus

2000 ◽  
Vol 60 (3) ◽  
pp. 264-268 ◽  
Author(s):  
Jung-Hun Lee ◽  
Gerlinde Teuber ◽  
Michael von Wagner ◽  
Willi Kurt Roth ◽  
Stefan Zeuzem
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Antiviral Effect ◽  
Interleukin 12

scholarly journals Inhibition of Hepatitis C Virus by the Cyanobacterial ProteinMicrocystis viridisLectin: Mechanistic Differences between the High-Mannose Specific Lectins MVL, CV-N, and GNA

2013 ◽  
Vol 10 (12) ◽  
pp. 4590-4602 ◽  
Author(s):  
Alla Kachko ◽  
Sandra Loesgen ◽  
Syed Shahzad-ul-Hussan ◽  
Wendy Tan ◽  
Iryna Zubkova ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
High Mannose

scholarly journals ISG12a Restricts Hepatitis C Virus Infection through the Ubiquitination-Dependent Degradation Pathway

2016 ◽  
Vol 90 (15) ◽  
pp. 6832-6845 ◽  
Author(s):  
Binbin Xue ◽  
Darong Yang ◽  
Jingjing Wang ◽  
Yan Xu ◽  
Xiaohong Wang ◽  
...  
Keyword(s):  
Innate Immunity ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Viral Infection ◽  
Viral Protein ◽  
E3 Ligase ◽  
Antiviral Effect ◽  
Degradation Pathway ◽  
Viral Spread ◽  
Ubiquitin E3 Ligase

ABSTRACTInterferons (IFNs) restrict various kinds of viral infection via induction of hundreds of IFN-stimulated genes (ISGs), while the functions of the majority of ISGs are broadly unclear. Here, we show that a high-IFN-inducible gene, ISG12a (also known as IFI27), exhibits a nonapoptotic antiviral effect on hepatitis C virus (HCV) infection. Viral NS5A protein is targeted specifically by ISG12a, which mediates NS5A degradation via a ubiquitination-dependent proteasomal pathway. K374R mutation in NS5A domain III abrogates ISG12a-induced ubiquitination and degradation of NS5A. S-phase kinase-associated protein 2 (SKP2) is identified as an ubiquitin E3 ligase for NS5A. ISG12a functions as a crucial adaptor that promotes SKP2 to interact with and degrade viral protein. Moreover, the antiviral effect of ISG12a is dependent on the E3 ligase activity of SKP2. These findings uncover an intriguing mechanism by which ISG12a restricts viral infection and provide clues for understanding the actions of innate immunity.IMPORTANCEUpon virus invasion, IFNs induce numerous ISGs to control viral spread, while the functions of the majority of ISGs are broadly unclear. The present study shows a novel antiviral mechanism of ISGs and elucidated that ISG12a recruits an E3 ligase, SKP2, for ubiquitination and degradation of viral protein and restricts viral infection. These findings provide important insights into exploring the working principles of innate immunity.

P420 GALLIC ACID HAS ANTIVIRAL EFFECT AGAINST HEPATITIS C VIRUS (HCV), WHICH IS MEDIATED BY ITS ANTIOXIDANT ACTIVITY

2014 ◽  
Vol 60 (1) ◽  
pp. S208 ◽  
Author(s):  
M. Govea Salas ◽  
A.M. Rivas Estilla ◽  
J.A. Morlett Chávez ◽  
S.A. Lozano Sepúlveda ◽  
R. Rodríguez Herrera ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Gallic Acid ◽  
Antiviral Effect

scholarly journals Required concentration index quantifies effective drug combinations against hepatitis C virus infection

2020 ◽  
Author(s):  
Yusuke Kakizoe ◽  
Yoshiki Koizumi ◽  
Yukino Ikoma ◽  
Hirofumi Ohashi ◽  
Takaji Wakita ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Drug Development ◽  
Concentration Index ◽  
Rational Design ◽  
Antiviral Effect ◽  
Drug Combinations ◽  
Hcv Genotype ◽  
Clinical Drug Development ◽  
Clinical Drug

Abstract Successful clinical drug development requires rational design of combination treatments based on preclinical data. Anti-HCV drugs exhibit significant diversity in antiviral effect. Dose-response assessments can be used to determine parameters profiling the diverse antiviral effect during combination treatment. In the current study, a combined experimental and mathematical approaches were used to compare and score different combinations of anti-hepatitis C virus (HCV) treatments. A “required concentration index” was generated and used to rank the antiviral profile of possible double- and triple-drug combinations against HCV genotype 1 and 2. Rankings varied based on target HCV genotype. Interestingly, multidrug (double and triple) treatment not only augmented antiviral activity, but also reduced genotype-specific efficacy, suggesting another advantage of multidrug treatment. The current study provides a quantitative method for profiling drug combinations against viral genotypes, to better inform clinical drug development.

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