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Comparison of the antiviral effect of solid-state copper and silver compounds

Antiviral activities of insoluble solid-state and soluble ionic copper and silver compounds were evaluated against influenza A virus (A/PR8/H1N1) possessing a viral envelope and bacteriophage Qβ lacking an envelope. The viral solutions were exposed on glass samples uniformly loaded with copper and s...

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Detalles Bibliográficos
Autores principales: Minoshima, Masafumi, Lu, Yue, Kimura, Takuto, Nakano, Ryuichi, Ishiguro, Hitoshi, Kubota, Yoshinobu, Hashimoto, Kazuhito, Sunada, Kayano
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7116991/
https://www.ncbi.nlm.nih.gov/pubmed/27015373
http://dx.doi.org/10.1016/j.jhazmat.2016.03.023
Descripción
Sumario:Antiviral activities of insoluble solid-state and soluble ionic copper and silver compounds were evaluated against influenza A virus (A/PR8/H1N1) possessing a viral envelope and bacteriophage Qβ lacking an envelope. The viral solutions were exposed on glass samples uniformly loaded with copper and silver compounds. Exposure to solid-state cuprous oxide (Cu(2)O) efficiently inactivated both influenza A virus and bacteriophage Qβ, whereas solid-state cupric oxide (CuO) and silver sulfide (Ag(2)S) showed little antiviral activity. Copper ions from copper chloride (CuCl(2)) had little effect on the activity of bacteriophage Qβ in spite of the fact that copper ions strongly inactivate influenza A in previous studies. Silver ions from silver nitrate (AgNO(3)) and silver(I) oxide (Ag(2)O) in solution showed strong inactivation of influenza A and weak inactivation of bacteriophage Qβ. We also investigated the influence of the compounds on the function of two influenza viral proteins, hemagglutinin and neuraminidase. Silver ions from AgNO(3) and Ag(2)O remarkably decreased enzymatic activity of neuraminidase through the breakage of disulfide (S—S) bonds, corresponding to the selective inactivation of influenza A virus. By contrast, exposure to Cu(2)O markedly reduced the activity of hemagglutinin rather than neuraminidase. These findings suggest that solid-state Cu(2)O disrupts host cell recognition by denaturing protein structures on viral surfaces, leading to the inactivation of viruses regardless of the presence of a viral envelope.