Enhancing the antivirus activity of chimeric canine interferon with ricin subunit B by using nanoparticle formulations. Issue 21 (27th March 2020)

• Record Type: Journal Article
• Authors: Sun, Chengbiao; Dong, Mingxin; Song, Yucong; Zhang, Jianxu; Wang, Yan; Chang, Ying; Yu, Haotian; Xu, Na; Xie, Zhigang; Liu, Wensen
• Is Part Of: RSC advances. Volume 10:Issue 21(2020)
• Page Start: 12671
• Page End: 12679
• Publication Date: 2020-03-27
• Subjects: Chemistry -- Periodicals; 540.5
• DOI: 10.1039/c9ra10557c
• Languages: English
• ISSNs: 2046-2069

Abstract

Abstract : Despite interferon alpha having a broad spectrum of antiviral activity and strong antiproliferative activity, its applications are severely limited due to the intrinsic properties of proteins, such as poor stability and short serum half-life. Abstract : Despite interferon alpha having a broad spectrum of antiviral activity and strong antiproliferative activity, its applications are severely limited due to the intrinsic properties of proteins, such as poor stability and short serum half-life. In our study, canine interferon alpha ( CaIFNα ) gene was fused with the ricin toxin B chain ( RTB ) to form rCaIFNα / RTB, which encodes a 463-amino acid protein containing a 15-amino acid encoded (G4 S)3 flexible linker. After expression in prokaryote, purification and renaturation, the cytotoxicity and antiviral activity of rCaIFNα/RTB were investigated in Madin–Darby canine kidney (MDCK) cells. rCaIFNα/RTB exerted a superior anti-vesicular stomatitis virus (VSV) activity on MDCK cells. Furthermore, we have developed a nanoparticle formulation of rCaIFNα/RTB by using polyethylenimine (PEI) through electrostatic interaction. rCaIFNα/RTB@PEI10000 is more stable than rCaIFNα/RTB at various pH and temperature levels, and it possesses enhanced antiviral activity. Our findings facilitate further research on the role of type I IFN in antiviral defense responses in Canis lupus familiaris .