Cargando…
Catalytic inactivation of influenza virus by iron oxide nanozyme
Influenza poses a severe threat to human health in the world. However, developing a universal anti-viral strategy has remained challenging due to the presence of diverse subtypes as well as its high mutation rate, resulting in antigenic shift and drift. Here we developed an antiviral strategy using...
Autores principales: | , , , , , , , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Ivyspring International Publisher
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815955/ https://www.ncbi.nlm.nih.gov/pubmed/31660077 http://dx.doi.org/10.7150/thno.35826 |
_version_ | 1783463292797190144 |
---|---|
author | Qin, Tao Ma, Ruonan Yin, Yinyan Miao, Xinyu Chen, Sujuan Fan, Kelong Xi, Juqun Liu, Qi Gu, Yunhao Yin, Yuncong Hu, Jiao Liu, Xiufan Peng, Daxin Gao, Lizeng |
author_facet | Qin, Tao Ma, Ruonan Yin, Yinyan Miao, Xinyu Chen, Sujuan Fan, Kelong Xi, Juqun Liu, Qi Gu, Yunhao Yin, Yuncong Hu, Jiao Liu, Xiufan Peng, Daxin Gao, Lizeng |
author_sort | Qin, Tao |
collection | PubMed |
description | Influenza poses a severe threat to human health in the world. However, developing a universal anti-viral strategy has remained challenging due to the presence of diverse subtypes as well as its high mutation rate, resulting in antigenic shift and drift. Here we developed an antiviral strategy using iron oxide nanozymes (IONzymes) to target the lipid envelope of the influenza virus. Methods: We evaluated the antiviral activities of our IONzymes using a hemagglutination assay, together with a 50% tissue culture infectious doses (TCID(50)) method. Lipid peroxidation of the viral envelope was analyzed using a maleic dialdehyde (MDA) assay and transmission electron microscopy (TEM). The neighboring viral proteins were detected by western blotting. Results: We show that IONzymes induce envelope lipid peroxidation and destroy the integrity of neighboring proteins, including hemagglutinin, neuraminidase, and matrix protein 1, causing the inactivation of influenza A viruses (IAVs). Furthermore, we show that our IONzymes possess a broad-spectrum antiviral activity on 12 subtypes of IAVs (H1~H12). Lastly, we demonstrate that applying IONzymes to a facemask improves the ability of virus protection against 3 important subtypes that pose a threat to human, including H1N1, H5N1, and H7N9 subtype. Conclusion: Together, our results clearly demonstrate that IONzymes can catalyze lipid peroxidation of the viral lipid envelope to inactivate enveloped viruses and provide protection from viral transmission and infection. |
format | Online Article Text |
id | pubmed-6815955 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Ivyspring International Publisher |
record_format | MEDLINE/PubMed |
spelling | pubmed-68159552019-10-28 Catalytic inactivation of influenza virus by iron oxide nanozyme Qin, Tao Ma, Ruonan Yin, Yinyan Miao, Xinyu Chen, Sujuan Fan, Kelong Xi, Juqun Liu, Qi Gu, Yunhao Yin, Yuncong Hu, Jiao Liu, Xiufan Peng, Daxin Gao, Lizeng Theranostics Research Paper Influenza poses a severe threat to human health in the world. However, developing a universal anti-viral strategy has remained challenging due to the presence of diverse subtypes as well as its high mutation rate, resulting in antigenic shift and drift. Here we developed an antiviral strategy using iron oxide nanozymes (IONzymes) to target the lipid envelope of the influenza virus. Methods: We evaluated the antiviral activities of our IONzymes using a hemagglutination assay, together with a 50% tissue culture infectious doses (TCID(50)) method. Lipid peroxidation of the viral envelope was analyzed using a maleic dialdehyde (MDA) assay and transmission electron microscopy (TEM). The neighboring viral proteins were detected by western blotting. Results: We show that IONzymes induce envelope lipid peroxidation and destroy the integrity of neighboring proteins, including hemagglutinin, neuraminidase, and matrix protein 1, causing the inactivation of influenza A viruses (IAVs). Furthermore, we show that our IONzymes possess a broad-spectrum antiviral activity on 12 subtypes of IAVs (H1~H12). Lastly, we demonstrate that applying IONzymes to a facemask improves the ability of virus protection against 3 important subtypes that pose a threat to human, including H1N1, H5N1, and H7N9 subtype. Conclusion: Together, our results clearly demonstrate that IONzymes can catalyze lipid peroxidation of the viral lipid envelope to inactivate enveloped viruses and provide protection from viral transmission and infection. Ivyspring International Publisher 2019-09-21 /pmc/articles/PMC6815955/ /pubmed/31660077 http://dx.doi.org/10.7150/thno.35826 Text en © The author(s) This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/). See http://ivyspring.com/terms for full terms and conditions. |
spellingShingle | Research Paper Qin, Tao Ma, Ruonan Yin, Yinyan Miao, Xinyu Chen, Sujuan Fan, Kelong Xi, Juqun Liu, Qi Gu, Yunhao Yin, Yuncong Hu, Jiao Liu, Xiufan Peng, Daxin Gao, Lizeng Catalytic inactivation of influenza virus by iron oxide nanozyme |
title | Catalytic inactivation of influenza virus by iron oxide nanozyme |
title_full | Catalytic inactivation of influenza virus by iron oxide nanozyme |
title_fullStr | Catalytic inactivation of influenza virus by iron oxide nanozyme |
title_full_unstemmed | Catalytic inactivation of influenza virus by iron oxide nanozyme |
title_short | Catalytic inactivation of influenza virus by iron oxide nanozyme |
title_sort | catalytic inactivation of influenza virus by iron oxide nanozyme |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815955/ https://www.ncbi.nlm.nih.gov/pubmed/31660077 http://dx.doi.org/10.7150/thno.35826 |
work_keys_str_mv | AT qintao catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT maruonan catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT yinyinyan catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT miaoxinyu catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT chensujuan catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT fankelong catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT xijuqun catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT liuqi catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT guyunhao catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT yinyuncong catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT hujiao catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT liuxiufan catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT pengdaxin catalyticinactivationofinfluenzavirusbyironoxidenanozyme AT gaolizeng catalyticinactivationofinfluenzavirusbyironoxidenanozyme |