In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus
Tyrosinases from a commercial <i>Agaricus bisporus</i> protein extract and directly isolated from white mushrooms were purified in order to obtaining the well-known tyrosinase from <i>A. bisporus</i> (<i>TyrAB</i>) of 45 kDa and a newly discovered 50 kDa tyrosinas...
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MDPI AG
2021-08-01
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| Series: | Pharmaceuticals |
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| Online Access: | https://www.mdpi.com/1424-8247/14/8/759 |
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| author | David Lopez-Tejedor Rafael Claveria-Gimeno Adrian Velazquez-Campoy Olga Abian Jose M. Palomo |
| author_facet | David Lopez-Tejedor Rafael Claveria-Gimeno Adrian Velazquez-Campoy Olga Abian Jose M. Palomo |
| author_sort | David Lopez-Tejedor |
| collection | DOAJ |
| description | Tyrosinases from a commercial <i>Agaricus bisporus</i> protein extract and directly isolated from white mushrooms were purified in order to obtaining the well-known tyrosinase from <i>A. bisporus</i> (<i>TyrAB</i>) of 45 kDa and a newly discovered 50 kDa tyrosinase isoform (<i>Tyr50 kDa</i>), and tested showing high antiviral activity against the hepatitis C virus for the first time. Cell toxicity and antiviral activity of tyrosinases were determined in cultured Huh 5-2 liver tumor cells transfected with a replicon system (a plasmid that includes all non-structural hepatitis C virus proteins and replicates autonomously). <i>TyrAB</i> was able to inhibit the replication of the hepatitis C virus without inducing toxicity in liver cells. In addition, the post-translational isoform <i>Tyr50 kDa</i> showed higher antiviral capacity than the former (up to 10 times greater), also exhibiting 10 times higher activity than the commercial drug Ribavirin<sup>®</sup>. This antiviral activity was directly proportional to the enzymatic activity of tyrosinases, as no antiviral capacity was observed in the inactive form of the enzymes. The tyrosinases approach could represent a new antiviral inhibition mechanism, through a plausible catalytic mechanism of selective hydroxylation of the key role of tyrosine residues in viral proteases. |
| first_indexed | 2024-03-10T08:29:29Z |
| format | Article |
| id | doaj.art-a4b07f831df94cb3821f06913638018c |
| institution | Directory Open Access Journal |
| issn | 1424-8247 |
| language | English |
| last_indexed | 2024-03-10T08:29:29Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Pharmaceuticals |
| spelling | doaj.art-a4b07f831df94cb3821f06913638018c2023-11-22T09:11:23ZengMDPI AGPharmaceuticals1424-82472021-08-0114875910.3390/ph14080759In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C VirusDavid Lopez-Tejedor0Rafael Claveria-Gimeno1Adrian Velazquez-Campoy2Olga Abian3Jose M. Palomo4Department of Biocatalysis, Institute of Catalysis (CSIC), c/Marie Curie 2, Cantoblanco Campus UAM, 28049 Madrid, SpainInstitute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, 50018 Zaragoza, SpainFundación Instituto de Investigación Sanitaria de Aragón (IIS Aragón), 50009 Zaragoza, SpainInstitute of Biocomputation and Physics of Complex Systems (BIFI), Joint Unit IQFR-CSIC-BIFI, Universidad de Zaragoza, 50018 Zaragoza, SpainDepartment of Biocatalysis, Institute of Catalysis (CSIC), c/Marie Curie 2, Cantoblanco Campus UAM, 28049 Madrid, SpainTyrosinases from a commercial <i>Agaricus bisporus</i> protein extract and directly isolated from white mushrooms were purified in order to obtaining the well-known tyrosinase from <i>A. bisporus</i> (<i>TyrAB</i>) of 45 kDa and a newly discovered 50 kDa tyrosinase isoform (<i>Tyr50 kDa</i>), and tested showing high antiviral activity against the hepatitis C virus for the first time. Cell toxicity and antiviral activity of tyrosinases were determined in cultured Huh 5-2 liver tumor cells transfected with a replicon system (a plasmid that includes all non-structural hepatitis C virus proteins and replicates autonomously). <i>TyrAB</i> was able to inhibit the replication of the hepatitis C virus without inducing toxicity in liver cells. In addition, the post-translational isoform <i>Tyr50 kDa</i> showed higher antiviral capacity than the former (up to 10 times greater), also exhibiting 10 times higher activity than the commercial drug Ribavirin<sup>®</sup>. This antiviral activity was directly proportional to the enzymatic activity of tyrosinases, as no antiviral capacity was observed in the inactive form of the enzymes. The tyrosinases approach could represent a new antiviral inhibition mechanism, through a plausible catalytic mechanism of selective hydroxylation of the key role of tyrosine residues in viral proteases.https://www.mdpi.com/1424-8247/14/8/759hepatitis C virustyrosinaseantiviral agentpharmaceuticalsenzymatic activityoxidation |
| spellingShingle | David Lopez-Tejedor Rafael Claveria-Gimeno Adrian Velazquez-Campoy Olga Abian Jose M. Palomo In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus Pharmaceuticals hepatitis C virus tyrosinase antiviral agent pharmaceuticals enzymatic activity oxidation |
| title | In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus |
| title_full | In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus |
| title_fullStr | In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus |
| title_full_unstemmed | In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus |
| title_short | In Vitro Antiviral Activity of Tyrosinase from Mushroom <i>Agaricus bisporus</i> against Hepatitis C Virus |
| title_sort | in vitro antiviral activity of tyrosinase from mushroom i agaricus bisporus i against hepatitis c virus |
| topic | hepatitis C virus tyrosinase antiviral agent pharmaceuticals enzymatic activity oxidation |
| url | https://www.mdpi.com/1424-8247/14/8/759 |
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