Papers

Peer-reviewed Lead author Corresponding author
Feb, 2016

Cellular peptidyl-prolyl cis/trans isomerase Pin1 facilitates replication of feline coronavirus

ANTIVIRAL RESEARCH
  • Yoshikazu Tanaka
  • ,
  • Arisa Amano
  • ,
  • Masateru Morisaki
  • ,
  • Yuka Sato
  • ,
  • Takashi Sasaki

Volume
126
Number
First page
1
Last page
7
Language
English
Publishing type
Research paper (scientific journal)
DOI
10.1016/j.antiviral.2015.11.013
Publisher
ELSEVIER SCIENCE BV

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 (PPlase) activity. However, protein interacting with NIMA (Finn a member of the parvulin subfamily of PPlases 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. (C) 2015 Elsevier B.V. All rights reserved.

Link information
DOI
https://doi.org/10.1016/j.antiviral.2015.11.013
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/26675666
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000369680000001&DestApp=WOS_CPL
ID information
  • DOI : 10.1016/j.antiviral.2015.11.013
  • ISSN : 0166-3542
  • eISSN : 1872-9096
  • Pubmed ID : 26675666
  • Web of Science ID : WOS:000369680000001

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