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Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development

An anti-influenza compound, DP2392-E10 based on inhibition of the nuclear export function of the viral nucleoprotein-nuclear export signal 3 (NP-NES3) domain was successfully identified by our previous high-throughput screening system. Here, we demonstrated that DP2392-E10 exerts its antiviral effec...

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Autores principales: Chutiwitoonchai, Nopporn, Mano, Takafumi, Kakisaka, Michinori, Sato, Hirotaka, Kondoh, Yasumitsu, Osada, Hiroyuki, Kotani, Osamu, Yokoyama, Masaru, Sato, Hironori, Aida, Yoko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111614/
https://www.ncbi.nlm.nih.gov/pubmed/28399435
http://dx.doi.org/10.1016/j.virol.2017.04.001
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author Chutiwitoonchai, Nopporn
Mano, Takafumi
Kakisaka, Michinori
Sato, Hirotaka
Kondoh, Yasumitsu
Osada, Hiroyuki
Kotani, Osamu
Yokoyama, Masaru
Sato, Hironori
Aida, Yoko
author_facet Chutiwitoonchai, Nopporn
Mano, Takafumi
Kakisaka, Michinori
Sato, Hirotaka
Kondoh, Yasumitsu
Osada, Hiroyuki
Kotani, Osamu
Yokoyama, Masaru
Sato, Hironori
Aida, Yoko
author_sort Chutiwitoonchai, Nopporn
collection PubMed
description An anti-influenza compound, DP2392-E10 based on inhibition of the nuclear export function of the viral nucleoprotein-nuclear export signal 3 (NP-NES3) domain was successfully identified by our previous high-throughput screening system. Here, we demonstrated that DP2392-E10 exerts its antiviral effect by inhibiting replication of a broad range of influenza A subtypes. In regard to the molecular mechanism, we revealed that DP2392-E10 inhibits nuclear export of both viral NP and nuclear export protein (NEP). More specifically, in vitro pull-down assays revealed that DP2392-E10 directly binds cellular CRM1, which mediates nuclear export of NP and NEP. In silico docking suggested that DP2392-E10 binds at a region close to the HEAT9 and HEAT10 domains of CRM1. Together, these results indicate that the CRM1-mediated nuclear export function of influenza virus represents a new potential target for antiviral drug development, and also provide a core structure for a novel class of inhibitors that target this function.
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spelling pubmed-71116142020-04-02 Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development Chutiwitoonchai, Nopporn Mano, Takafumi Kakisaka, Michinori Sato, Hirotaka Kondoh, Yasumitsu Osada, Hiroyuki Kotani, Osamu Yokoyama, Masaru Sato, Hironori Aida, Yoko Virology Article An anti-influenza compound, DP2392-E10 based on inhibition of the nuclear export function of the viral nucleoprotein-nuclear export signal 3 (NP-NES3) domain was successfully identified by our previous high-throughput screening system. Here, we demonstrated that DP2392-E10 exerts its antiviral effect by inhibiting replication of a broad range of influenza A subtypes. In regard to the molecular mechanism, we revealed that DP2392-E10 inhibits nuclear export of both viral NP and nuclear export protein (NEP). More specifically, in vitro pull-down assays revealed that DP2392-E10 directly binds cellular CRM1, which mediates nuclear export of NP and NEP. In silico docking suggested that DP2392-E10 binds at a region close to the HEAT9 and HEAT10 domains of CRM1. Together, these results indicate that the CRM1-mediated nuclear export function of influenza virus represents a new potential target for antiviral drug development, and also provide a core structure for a novel class of inhibitors that target this function. Elsevier Inc. 2017-07 2017-04-08 /pmc/articles/PMC7111614/ /pubmed/28399435 http://dx.doi.org/10.1016/j.virol.2017.04.001 Text en © 2017 Elsevier Inc. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Chutiwitoonchai, Nopporn
Mano, Takafumi
Kakisaka, Michinori
Sato, Hirotaka
Kondoh, Yasumitsu
Osada, Hiroyuki
Kotani, Osamu
Yokoyama, Masaru
Sato, Hironori
Aida, Yoko
Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development
title Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development
title_full Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development
title_fullStr Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development
title_full_unstemmed Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development
title_short Inhibition of CRM1-mediated nuclear export of influenza A nucleoprotein and nuclear export protein as a novel target for antiviral drug development
title_sort inhibition of crm1-mediated nuclear export of influenza a nucleoprotein and nuclear export protein as a novel target for antiviral drug development
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111614/
https://www.ncbi.nlm.nih.gov/pubmed/28399435
http://dx.doi.org/10.1016/j.virol.2017.04.001
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