Copper Nanoparticle–Graphene Composite-Based Transparent Surface Coating with Antiviral Activity against Influenza Virus

Author(s):  
Indrani Das Jana ◽  
Partha Kumbhakar ◽  
Saptarshi Banerjee ◽  
Chinmayee Chowde Gowda ◽  
Nandita Kedia ◽  
...  
Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3678
Author(s):  
Olga V. Andreeva ◽  
Bulat F. Garifullin ◽  
Vladimir V. Zarubaev ◽  
Alexander V. Slita ◽  
Iana L. Yesaulkova ◽  
...  

A series of 1,2,3-triazolyl nucleoside analogues in which 1,2,3-triazol-4-yl-β-d-ribofuranosyl fragments are attached via polymethylene linkers to both nitrogen atoms of the heterocycle moiety (uracil, 6-methyluracil, thymine, quinazoline-2,4-dione, alloxazine) or to the C-5 and N-3 atoms of the 6-methyluracil moiety was synthesized. All compounds synthesized were evaluated for antiviral activity against influenza virus A/PR/8/34/(H1N1) and coxsackievirus B3. Antiviral assays revealed three compounds, 2i, 5i, 11c, which showed moderate activity against influenza virus A H1N1 with IC50 values of 57.5 µM, 24.3 µM, and 29.2 µM, respectively. In the first two nucleoside analogues, 1,2,3-triazol-4-yl-β-d-ribofuranosyl fragments are attached via butylene linkers to N-1 and N-3 atoms of the heterocycle moiety (6-methyluracil and alloxazine, respectively). In nucleoside analogue 11c, two 1,2,3-triazol-4-yl-2′,3′,5′-tri-O-acetyl-β-d-ribofuranose fragments are attached via propylene linkers to the C-5 and N-3 atoms of the 6-methyluracil moiety. Almost all synthesized 1,2,3-triazolyl nucleoside analogues showed no antiviral activity against the coxsackie B3 virus. Two exceptions are 1,2,3-triazolyl nucleoside analogs 2f and 5f, in which 1,2,3-triazol-4-yl-2′,3′,5′-tri-O-acetyl-β-d-ribofuranose fragments are attached to the C-5 and N-3 atoms of the heterocycle moiety (6-methyluracil and alloxazine respectively). These compounds exhibited high antiviral potency against the coxsackie B3 virus with IC50 values of 12.4 and 11.3 µM, respectively, although both were inactive against influenza virus A H1N1. According to theoretical calculations, the antiviral activity of the 1,2,3-triazolyl nucleoside analogues 2i, 5i, and 11c against the H1N1 (A/PR/8/34) influenza virus can be explained by their influence on the functioning of the polymerase acidic protein (PA) of RNA-dependent RNA polymerase (RdRp). As to the antiviral activity of nucleoside analogs 2f and 5f against coxsackievirus B3, it can be explained by their interaction with the coat proteins VP1 and VP2.


2016 ◽  
Vol 90 (9) ◽  
pp. 4637-4646 ◽  
Author(s):  
Kanyarat Ruangrung ◽  
Ornpreya Suptawiwat ◽  
Kittipong Maneechotesuwan ◽  
Chompunuch Boonarkart ◽  
Warunya Chakritbudsabong ◽  
...  

ABSTRACTHuman bronchoalveolar fluid is known to have anti-influenza activity. It is believed to be a frontline innate defense against the virus. Several antiviral factors, including surfactant protein D, are believed to contribute to the activity. The 2009 pandemic H1N1 influenza virus was previously shown to be less sensitive to surfactant protein D. Nevertheless, whether different influenza virus strains have different sensitivities to the overall anti-influenza activity of human bronchoalveolar fluid was not known. We compared the sensitivities of 2009 pandemic H1N1, seasonal H1N1, and seasonal H3N2 influenza virus strains to inhibition by human bronchoalveolar lavage (BAL) fluid. The pandemic and seasonal H1N1 strains showed lower sensitivity to human BAL fluid than the H3N2 strains. The BAL fluid anti-influenza activity could be enhanced by oseltamivir, indicating that the viral neuraminidase (NA) activity could provide resistance to the antiviral defense. In accordance with this finding, the BAL fluid anti-influenza activity was found to be sensitive to sialidase. The oseltamivir resistance mutation H275Y rendered the pandemic H1N1 virus but not the seasonal H1N1 virus more sensitive to BAL fluid. Since only the seasonal H1N1 but not the pandemic H1N1 had compensatory mutations that allowed oseltamivir-resistant strains to maintain NA enzymatic activity and transmission fitness, the resistance to BAL fluid of the drug-resistant seasonal H1N1 virus might play a role in viral fitness.IMPORTANCEHuman airway secretion contains anti-influenza activity. Different influenza strains may vary in their susceptibilities to this antiviral activity. Here we show that the 2009 pandemic and seasonal H1N1 influenza viruses were less sensitive to human bronchoalveolar lavage (BAL) fluid than H3N2 seasonal influenza virus. The resistance to the pulmonary innate antiviral activity of the pandemic virus was determined by its neuraminidase (NA) gene, and it was shown that the NA inhibitor resistance mutation H275Y abolished this resistance of the pandemic H1N1 but not the seasonal H1N1 virus, which had compensatory mutations that maintained the fitness of drug-resistant strains. Therefore, the innate respiratory tract defense may be a barrier against NA inhibitor-resistant mutants, and evasion of this defense may play a role in the emergence and spread of drug-resistant strains.


2021 ◽  
Vol 17 (1) ◽  
pp. 1-14
Author(s):  
Thongchai Taechowisa ◽  
Tipparat Samsawat ◽  
Chanjira Jaramornbu ◽  
Weerachai Phutdhawon ◽  
Waya S. Phutdhawong Phutdhawon

2012 ◽  
Vol 55 ◽  
pp. 117-124 ◽  
Author(s):  
Lan-hu Hao ◽  
Yan-ping Li ◽  
Wei-ying He ◽  
Hui-qiang Wang ◽  
Guang-zhi Shan ◽  
...  

2021 ◽  
Author(s):  
Christian Marco Hadi Nugroho ◽  
Ryan Septa Kurnia ◽  
Simson Tarigan ◽  
Otto Sahat Martua Silaen ◽  
Silvia Tri Widyaningtyas ◽  
...  

Abstract Study on sialidases as antiviral agents has been widely performed, but many types of sialidase had not been tested for their antiviral activity. One of such sialidase is the NanB sialidase of Pasteurella multocida, which has never been isolated for further study. In this study, the activity of NanB sialidase was investigated in silico by docking the NanB sialidase of Pasteurella multocida to the Neu5Acα(2-6)Gal ligand. Additionally, some local isolates of Pasteurella multocida, which had the NanB gene were screened, and the proteins were isolated for further testing regarding their activity in hydrolyzing Neu5Acα(2-6)Gal. In silico studies showed that the NanB sialidase possesses an exceptional affinity towards forming a protein-ligand complex with Neu5Acα(2-6)Gal. This was further confirmed by showing that a dose of 0.258 U/ml (100%) NanB sialidase of Pasteurella multocida B018 can hydrolyze up to 44.28% of Neu5Acα(2-6)Gal in chicken red blood cells and 81.95% in rabbit red blood cells. This study suggested that the NanB sialidase of Pasteurella multocida B018 has a potent antiviral activity that can inhibit avian influenza virus infection.


2020 ◽  
Vol 30 (2) ◽  
pp. 172-177 ◽  
Author(s):  
Minjee Kim ◽  
Dinh-Van Nguyen ◽  
Yoonki Heo ◽  
Ki Hoon Park ◽  
Hyun-Dong Paik ◽  
...  

2018 ◽  
Vol 46 (08) ◽  
pp. 1663-1700 ◽  
Author(s):  
Ju-Young Lee ◽  
Michael Edward C. Abundo ◽  
Chang-Won Lee

The rapidly changing influenza virus has remained a consistent threat to the well-being of a variety of species on the planet. Influenza virus’ high mutation rate has allowed the virus to rapidly and continuously evolve, as well as generate new strains that are resistant to the current commercially available antivirals. Thus, the increased resistance has compelled the scientific community to explore alternative compounds that have antiviral effects against influenza virus. In this paper, the authors systematically review numerous herbal extracts that were shown to have antiviral effects against the virus. Specifically, the herbal antiviral targets mainly include hemagglutinin, neuraminidase and matrix 2 proteins. In some instances, herbal extracts inhibited the replication of oseltamivir-resistant strains and certain pentacyclic triterpenes exhibited higher antiviral activity than oseltamivir. This paper also explores the possibility of targeting various host-cell signaling pathways that are utilized by the virus during its replication process. Infected cell pathways are hijacked by intracellular signaling cascades such as NF-kB signaling, PI3K/Akt pathway, MAPK pathway and PKC/PKR signaling cascades. Herbal antivirals have been shown to target these pathways by suppressing nuclear export of influenza vRNP and thus inhibiting the phosphorylation signaling cascade. In conclusion, copious amounts of herbal antivirals have been shown to inhibit influenza virus, however further studies are needed for these new compounds to be up to modern pharmacological standards.


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