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Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus
Although feline coronavirus (FCoV) causes feline infectious peritonitis (FIP), which is a fatal infectious disease, there are no effective therapeutic medicines or vaccines. Previously, in vitro studies have shown that cyclosporin (CsA) and FK506 inhibit virus replication in diverse coronaviruses. C...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier B.V.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7113879/ https://www.ncbi.nlm.nih.gov/pubmed/26675666 http://dx.doi.org/10.1016/j.antiviral.2015.11.013 |
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author | Tanaka, Yoshikazu Amano, Arisa Morisaki, Masateru Sato, Yuka Sasaki, Takashi |
author_facet | Tanaka, Yoshikazu Amano, Arisa Morisaki, Masateru Sato, Yuka Sasaki, Takashi |
author_sort | Tanaka, Yoshikazu |
collection | PubMed |
description | Although feline coronavirus (FCoV) causes feline infectious peritonitis (FIP), which is a fatal infectious disease, there are no effective therapeutic medicines or vaccines. Previously, in vitro studies have shown that cyclosporin (CsA) and FK506 inhibit virus replication in diverse coronaviruses. CsA and FK506 are targets of clinically relevant immunosuppressive drugs and bind to cellular cyclophilins (Cyps) or FK506 binding proteins (FKBPs), respectively. Both Cyp and FKBP have peptidyl-prolyl cis-trans isomerase (PPIase) activity. However, protein interacting with NIMA (Pin1), a member of the parvulin subfamily of PPIases that differs from Cyps and FKBPs, is essential for various signaling pathways. Here we demonstrated that genetic silencing or knockout of Pin1 resulted in decreased FCoV replication in vitro. Dipentamethylene thiuram monosulfide, a specific inhibitor of Pin1, inhibited FCoV replication. These data indicate that Pin1 modulates FCoV propagation. |
format | Online Article Text |
id | pubmed-7113879 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71138792020-04-02 Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus Tanaka, Yoshikazu Amano, Arisa Morisaki, Masateru Sato, Yuka Sasaki, Takashi Antiviral Res Article Although feline coronavirus (FCoV) causes feline infectious peritonitis (FIP), which is a fatal infectious disease, there are no effective therapeutic medicines or vaccines. Previously, in vitro studies have shown that cyclosporin (CsA) and FK506 inhibit virus replication in diverse coronaviruses. CsA and FK506 are targets of clinically relevant immunosuppressive drugs and bind to cellular cyclophilins (Cyps) or FK506 binding proteins (FKBPs), respectively. Both Cyp and FKBP have peptidyl-prolyl cis-trans isomerase (PPIase) activity. However, protein interacting with NIMA (Pin1), a member of the parvulin subfamily of PPIases that differs from Cyps and FKBPs, is essential for various signaling pathways. Here we demonstrated that genetic silencing or knockout of Pin1 resulted in decreased FCoV replication in vitro. Dipentamethylene thiuram monosulfide, a specific inhibitor of Pin1, inhibited FCoV replication. These data indicate that Pin1 modulates FCoV propagation. Elsevier B.V. 2016-02 2015-12-07 /pmc/articles/PMC7113879/ /pubmed/26675666 http://dx.doi.org/10.1016/j.antiviral.2015.11.013 Text en Copyright © 2015 Elsevier B.V. All rights reserved. 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 Tanaka, Yoshikazu Amano, Arisa Morisaki, Masateru Sato, Yuka Sasaki, Takashi Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus |
title | Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus |
title_full | Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus |
title_fullStr | Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus |
title_full_unstemmed | Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus |
title_short | Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus |
title_sort | cellular peptidyl-prolyl cis/trans isomerase pin1 facilitates replication of feline coronavirus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7113879/ https://www.ncbi.nlm.nih.gov/pubmed/26675666 http://dx.doi.org/10.1016/j.antiviral.2015.11.013 |
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