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 inAntimicrobial agents and chemotherapy Vol. 60; no. 3; pp. 1902 - 1906
Main Authors Zhao, Dongming, Fukuyama, Satoshi, Sakai-Tagawa, Yuko, Takashita, Emi, Shoemaker, Jason E., Kawaoka, Yoshihiro
Format Journal Article
LanguageEnglish
Published 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.
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
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  surname: Zhao
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  organization: Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan
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  surname: Shoemaker
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  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
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  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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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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StartPage 1902
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
URI https://www.ncbi.nlm.nih.gov/pubmed/26711748
https://journals.asm.org/doi/10.1128/AAC.02055-15
https://www.proquest.com/docview/1768562524
https://pubmed.ncbi.nlm.nih.gov/PMC4776003
Volume 60
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