C646, a Novel p300/CREB-Binding Protein-Specific Inhibitor of Histone Acetyltransferase, Attenuates Influenza A Virus Infection
New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and drug-resistant viruses. Here, we evaluated C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase (HAT), as an...
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Published in | Antimicrobial agents and chemotherapy Vol. 60; no. 3; pp. 1902 - 1906 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
American Society for Microbiology
01.03.2016
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Abstract | New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and drug-resistant viruses. Here, we evaluated C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase (HAT), as an anti-influenza virus agent
in vitro
and
in vivo
and explored how C646 affects the viral life cycle and host response. Our studies highlight the value of targeting HAT activity for anti-influenza drug development. |
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AbstractList | New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and drug-resistant viruses. Here, we evaluated C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase (HAT), as an anti-influenza virus agent in vitro and in vivo and explored how C646 affects the viral life cycle and host response. Our studies highlight the value of targeting HAT activity for anti-influenza drug development.New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and drug-resistant viruses. Here, we evaluated C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase (HAT), as an anti-influenza virus agent in vitro and in vivo and explored how C646 affects the viral life cycle and host response. Our studies highlight the value of targeting HAT activity for anti-influenza drug development. New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and drug-resistant viruses. Here, we evaluated C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase (HAT), as an anti-influenza virus agent in vitro and in vivo and explored how C646 affects the viral life cycle and host response. Our studies highlight the value of targeting HAT activity for anti-influenza drug development. New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and drug-resistant viruses. Here, we evaluated C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase (HAT), as an anti-influenza virus agent in vitro and in vivo and explored how C646 affects the viral life cycle and host response. Our studies highlight the value of targeting HAT activity for anti-influenza drug development. |
Author | Zhao, Dongming Takashita, Emi Shoemaker, Jason E. Kawaoka, Yoshihiro Sakai-Tagawa, Yuko Fukuyama, Satoshi |
Author_xml | – sequence: 1 givenname: Dongming surname: Zhao fullname: Zhao, Dongming organization: Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan, ERATO Infection-Induced Host Responses Project, Japan Science and Technology Agency, Saitama, Japan – sequence: 2 givenname: Satoshi surname: Fukuyama fullname: Fukuyama, Satoshi organization: Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan, ERATO Infection-Induced Host Responses Project, Japan Science and Technology Agency, Saitama, Japan – sequence: 3 givenname: Yuko surname: Sakai-Tagawa fullname: Sakai-Tagawa, Yuko organization: Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan – sequence: 4 givenname: Emi surname: Takashita fullname: Takashita, Emi organization: Influenza Virus Research Center, National Institute of Infectious Diseases, Musashimurayama, Tokyo, Japan – sequence: 5 givenname: Jason E. surname: Shoemaker fullname: Shoemaker, Jason E. organization: Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan, ERATO Infection-Induced Host Responses Project, Japan Science and Technology Agency, Saitama, Japan – sequence: 6 givenname: Yoshihiro surname: Kawaoka fullname: Kawaoka, Yoshihiro organization: Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan, ERATO Infection-Induced Host Responses Project, Japan Science and Technology Agency, Saitama, Japan, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, Wisconsin, USA, Department of Special Pathogens, International Research Center for Infectious Diseases, Institute of Medical Science, University of Tokyo, Tokyo, Japan |
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Cites_doi | 10.1074/jbc.M409024200 10.1371/journal.pone.0062482 10.1056/NEJMra1002842 10.1074/jbc.M301580200 10.1007/s00018-012-1254-4 10.1016/j.chembiol.2010.03.006 10.1183/09031936.05.00117504 10.1016/j.drudis.2009.06.008 10.1016/j.chom.2014.11.002 10.1164/rccm.2110060 10.1016/j.chembiol.2007.04.011 10.1016/j.foodchem.2009.09.011 10.1126/science.1229455 10.7326/0003-4819-156-7-201204030-00411 10.1099/vir.0.81766-0 10.1074/jbc.M402839200 10.1038/sj.leu.2401983 10.1128/JVI.01886-15 10.1038/sj.onc.1206376 10.1186/1752-0509-7-97 10.1128/MCB.22.13.4450-4462.2002 10.1073/pnas.1019109108 10.1146/annurev.pharmtox.45.120403.095825 10.1038/nprot.2014.180 10.1093/infdis/jiq012 10.1038/sj.onc.1210599 10.1016/S1473-3099(11)70295-X 10.1128/JVI.01140-10 10.1164/rccm.200305-659OC 10.1158/1541-7786.MCR-07-0324 10.1074/jbc.M114.559708 10.1128/AAC.04836-14 10.1099/vir.0.037648-0 10.1128/JVI.76.10.4699-4708.2002 |
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Copyright | Copyright © 2016, American Society for Microbiology. All Rights Reserved. Copyright © 2016, American Society for Microbiology. All Rights Reserved. 2016 American Society for Microbiology |
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DocumentTitleAlternate | C646 Suppresses Influenza A Virus Infection, Zhao et al C646 Suppresses Influenza A Virus Infection |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Citation Zhao D, Fukuyama S, Sakai-Tagawa Y, Takashita E, Shoemaker JE, Kawaoka Y. 2016. C646, a novel p300/CREB-binding protein-specific inhibitor of histone acetyltransferase, attenuates influenza A virus infection. Antimicrob Agents Chemother 60:1902–1906. doi:10.1128/AAC.02055-15. |
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Snippet | New strategies to develop novel broad-spectrum antiviral drugs against influenza virus infections are needed due to the emergence of antigenic variants and... |
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SubjectTerms | Animals Antiviral Agents Antiviral Agents - pharmacology Benzoates Benzoates - pharmacology Cell Line CREB-Binding Protein CREB-Binding Protein - antagonists & inhibitors CREB-Binding Protein - metabolism Dogs E1A-Associated p300 Protein E1A-Associated p300 Protein - antagonists & inhibitors E1A-Associated p300 Protein - metabolism HEK293 Cells Histone Acetyltransferases Histone Acetyltransferases - antagonists & inhibitors Humans Influenza A virus Influenza A virus - drug effects Madin Darby Canine Kidney Cells Mice Mice, Inbred BALB C Orthomyxoviridae Infections Orthomyxoviridae Infections - drug therapy Pyrazoles Pyrazoles - pharmacology |
Title | C646, a Novel p300/CREB-Binding Protein-Specific Inhibitor of Histone Acetyltransferase, Attenuates Influenza A Virus Infection |
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