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...
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Veröffentlicht in: | Theranostics 2019-01, Vol.9 (23), p.6920-6935 |
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creator | 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 |
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.
We evaluated the antiviral activities of our IONzymes using a hemagglutination assay, together with a 50% tissue culture infectious doses (TCID
) 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.
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.
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. |
doi_str_mv | 10.7150/thno.35826 |
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We evaluated the antiviral activities of our IONzymes using a hemagglutination assay, together with a 50% tissue culture infectious doses (TCID
) 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.
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.
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.</description><identifier>ISSN: 1838-7640</identifier><identifier>EISSN: 1838-7640</identifier><identifier>DOI: 10.7150/thno.35826</identifier><identifier>PMID: 31660077</identifier><language>eng</language><publisher>Australia: Ivyspring International Publisher Pty Ltd</publisher><subject>Avian flu ; Enzymes ; Hydrogen peroxide ; Lipid peroxidation ; Lipids ; Morphology ; Nanomaterials ; Nanoparticles ; Proteins ; Research Paper ; Viruses</subject><ispartof>Theranostics, 2019-01, Vol.9 (23), p.6920-6935</ispartof><rights>The author(s).</rights><rights>2019. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>The author(s) 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-d6bb8b6832cd6058a9c1ccd0c13ccbff314f8821e7eee5d1ad90a623675b3ff3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815955/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6815955/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31660077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Qin, Tao</creatorcontrib><creatorcontrib>Ma, Ruonan</creatorcontrib><creatorcontrib>Yin, Yinyan</creatorcontrib><creatorcontrib>Miao, Xinyu</creatorcontrib><creatorcontrib>Chen, Sujuan</creatorcontrib><creatorcontrib>Fan, Kelong</creatorcontrib><creatorcontrib>Xi, Juqun</creatorcontrib><creatorcontrib>Liu, Qi</creatorcontrib><creatorcontrib>Gu, Yunhao</creatorcontrib><creatorcontrib>Yin, Yuncong</creatorcontrib><creatorcontrib>Hu, Jiao</creatorcontrib><creatorcontrib>Liu, Xiufan</creatorcontrib><creatorcontrib>Peng, Daxin</creatorcontrib><creatorcontrib>Gao, Lizeng</creatorcontrib><title>Catalytic inactivation of influenza virus by iron oxide nanozyme</title><title>Theranostics</title><addtitle>Theranostics</addtitle><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.
We evaluated the antiviral activities of our IONzymes using a hemagglutination assay, together with a 50% tissue culture infectious doses (TCID
) 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.
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.
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.</description><subject>Avian flu</subject><subject>Enzymes</subject><subject>Hydrogen peroxide</subject><subject>Lipid peroxidation</subject><subject>Lipids</subject><subject>Morphology</subject><subject>Nanomaterials</subject><subject>Nanoparticles</subject><subject>Proteins</subject><subject>Research Paper</subject><subject>Viruses</subject><issn>1838-7640</issn><issn>1838-7640</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNpdkV9LwzAUxYMobsy9-AGk4IsInUnTpOmLKMN_MPBl7yFNU5fRJTNph92nN3VzTO9Lbjg_DvfeA8AlgpMMEXjXLIydYMISegKGiGEWZzSFp0f9AIy9X8JQKUxylJ-DAUaUQphlQ_AwFY2ou0bLSBshG70RjbYmslX4V3WrzFZEG-1aHxVdpF0vfelSRUYYu-1W6gKcVaL2arx_R2D-_DSfvsaz95e36eMslimkTVzSomAFZTiRJYWEiVwiKUsoEZayqCqM0oqxBKlMKUVKJMocCppgmpECB3kE7ne267ZYqVIq0zhR87XTK-E6boXmfxWjF_zDbjhliOSEBIObvYGzn63yDV9pL1VdC6Ns63mCUbgORDkM6PU_dGlbZ8J2PCF5uDRkSU_d7ijprPdOVYdhEOR9NLyPhv9EE-Cr4_EP6G8Q-Bv7_ItY</recordid><startdate>20190101</startdate><enddate>20190101</enddate><creator>Qin, Tao</creator><creator>Ma, Ruonan</creator><creator>Yin, Yinyan</creator><creator>Miao, Xinyu</creator><creator>Chen, Sujuan</creator><creator>Fan, Kelong</creator><creator>Xi, Juqun</creator><creator>Liu, Qi</creator><creator>Gu, Yunhao</creator><creator>Yin, Yuncong</creator><creator>Hu, Jiao</creator><creator>Liu, Xiufan</creator><creator>Peng, Daxin</creator><creator>Gao, Lizeng</creator><general>Ivyspring International Publisher Pty Ltd</general><general>Ivyspring International Publisher</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20190101</creationdate><title>Catalytic inactivation of influenza virus by iron oxide nanozyme</title><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></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-d6bb8b6832cd6058a9c1ccd0c13ccbff314f8821e7eee5d1ad90a623675b3ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Avian flu</topic><topic>Enzymes</topic><topic>Hydrogen peroxide</topic><topic>Lipid peroxidation</topic><topic>Lipids</topic><topic>Morphology</topic><topic>Nanomaterials</topic><topic>Nanoparticles</topic><topic>Proteins</topic><topic>Research Paper</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Qin, Tao</creatorcontrib><creatorcontrib>Ma, Ruonan</creatorcontrib><creatorcontrib>Yin, Yinyan</creatorcontrib><creatorcontrib>Miao, Xinyu</creatorcontrib><creatorcontrib>Chen, Sujuan</creatorcontrib><creatorcontrib>Fan, Kelong</creatorcontrib><creatorcontrib>Xi, Juqun</creatorcontrib><creatorcontrib>Liu, Qi</creatorcontrib><creatorcontrib>Gu, Yunhao</creatorcontrib><creatorcontrib>Yin, Yuncong</creatorcontrib><creatorcontrib>Hu, Jiao</creatorcontrib><creatorcontrib>Liu, Xiufan</creatorcontrib><creatorcontrib>Peng, Daxin</creatorcontrib><creatorcontrib>Gao, Lizeng</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Theranostics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Qin, Tao</au><au>Ma, Ruonan</au><au>Yin, Yinyan</au><au>Miao, Xinyu</au><au>Chen, Sujuan</au><au>Fan, Kelong</au><au>Xi, Juqun</au><au>Liu, Qi</au><au>Gu, Yunhao</au><au>Yin, Yuncong</au><au>Hu, Jiao</au><au>Liu, Xiufan</au><au>Peng, Daxin</au><au>Gao, Lizeng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Catalytic inactivation of influenza virus by iron oxide nanozyme</atitle><jtitle>Theranostics</jtitle><addtitle>Theranostics</addtitle><date>2019-01-01</date><risdate>2019</risdate><volume>9</volume><issue>23</issue><spage>6920</spage><epage>6935</epage><pages>6920-6935</pages><issn>1838-7640</issn><eissn>1838-7640</eissn><abstract>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.
We evaluated the antiviral activities of our IONzymes using a hemagglutination assay, together with a 50% tissue culture infectious doses (TCID
) 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.
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.
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.</abstract><cop>Australia</cop><pub>Ivyspring International Publisher Pty Ltd</pub><pmid>31660077</pmid><doi>10.7150/thno.35826</doi><tpages>16</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Avian flu Enzymes Hydrogen peroxide Lipid peroxidation Lipids Morphology Nanomaterials Nanoparticles Proteins Research Paper Viruses |
title | Catalytic inactivation of influenza virus by iron oxide nanozyme |
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