The antiviral protein viperin interacts with the viral N protein to inhibit proliferation of porcine epidemic diarrhea virus.

Publisher: Springer-Verlag Country of Publication: Austria NLM ID: 7506870 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-8798 (Electronic) Linking ISSN: 03048608 NLM ISO Abbreviation: Arch Virol Subsets: MEDLINE

Original Publication: Wien, New York, Springer-Verlag.

Antiviral Agents/*metabolism ; Host Microbial Interactions/*physiology ; Nucleocapsid Proteins/*physiology ; Porcine epidemic diarrhea virus/*physiology; Animals ; Cell Line ; Coronavirus Infections/genetics ; Coronavirus Infections/immunology ; Coronavirus Infections/virology ; Host Microbial Interactions/genetics ; Host Microbial Interactions/immunology ; Immunity, Innate ; Interferons/biosynthesis ; Mice ; Mice, Inbred BALB C ; Nucleocapsid Proteins/antagonists & inhibitors ; Nucleocapsid Proteins/chemistry ; Porcine epidemic diarrhea virus/immunology ; Porcine epidemic diarrhea virus/pathogenicity ; Protein Interaction Domains and Motifs ; Proteins/chemistry ; Proteins/genetics ; Proteins/physiology ; RNA Interference ; Swine ; Virus Replication

In the early stage of virus infection, the pattern recognition receptor (PRR) signaling pathway of the host cell is activated to induce interferon production, activating interferon-stimulated genes (ISGs) that encode antiviral proteins that exert antiviral effects. Viperin is one of the innate antiviral proteins that exert broad-spectrum antiviral effects by various mechanisms. Porcine epidemic diarrhea virus (PEDV) is a coronavirus that causes huge losses to the pig industry. Research on early antiviral responses in the gastrointestinal tract is essential for developing strategies to prevent the spread of PEDV. In this study, we investigated the mechanisms of viperin in PEDV-infected IPEJ-C2 cells. Increased expression of interferon and viperin and decreased replication of PEDV with a clear reduction in the viral load were observed in PEDV-infected IPEC-J2 cells. Amino acids 1-50 of porcine viperin contain an endoplasmic reticulum signal sequence that allows viperin to be anchored to the endoplasmic reticulum and are necessary for its function in inhibiting PEDV proliferation. The interaction of the viperin S-adenosylmethionine domain with the N protein of PEDV was confirmed via confocal laser scanning microscopy and co-immunoprecipitation. This interaction might interfere with viral replication or assembly to reduce virus proliferation. Our results highlight a potential mechanism whereby viperin is able to inhibit PEDV replication and play an antiviral role in innate immunity.

J Mol Biol. 2014 Mar 20;426(6):1210-9. (PMID: 24157441)
J Clin Microbiol. 2014 Jan;52(1):234-43. (PMID: 24197882)
Curr Top Microbiol Immunol. 2005;287:1-30. (PMID: 15609507)
Zh Mikrobiol Epidemiol Immunobiol. 1956 Jan;27(1):77-83. (PMID: 13325889)
Antiviral Res. 2017 Apr;140:76-82. (PMID: 28109912)
Cold Spring Harb Perspect Biol. 2011 Mar 01;3(3):. (PMID: 21421923)
Mol Cell. 2020 Feb 20;77(4):734-747.e7. (PMID: 31812350)
Vet Microbiol. 2019 May;232:1-12. (PMID: 31030832)
Nature. 2011 Apr 28;472(7344):481-5. (PMID: 21478870)
J Med Virol. 2020 Feb;92(2):149-160. (PMID: 31517388)
J Gen Virol. 2012 Jun;93(Pt 6):1269-1277. (PMID: 22377585)
Virus Genes. 2006 Oct;33(2):215-9. (PMID: 16972037)
Emerg Infect Dis. 2012 Jan;18(1):161-3. (PMID: 22261231)
J Gen Virol. 2015 Jul;96(Pt 7):1757-67. (PMID: 25814121)
Immunity. 2011 Mar 25;34(3):352-63. (PMID: 21435586)
Arch Biochem Biophys. 2008 May 1;473(1):42-7. (PMID: 18342616)
Virus Genes. 2012 Apr;44(2):167-75. (PMID: 22270324)
Virus Res. 2014 Oct 13;191:143-52. (PMID: 25116392)
Virol J. 2015 Aug 18;12:127. (PMID: 26283628)
J Virol. 2014 Jul;88(14):7952-61. (PMID: 24807723)
Emerg Infect Dis. 2014 Apr;20(4):662-5. (PMID: 24795932)
Sci Adv. 2019 Aug 28;5(8):eaax1031. (PMID: 31489375)
Cell. 2010 May 14;141(4):668-81. (PMID: 20451243)
Annu Rev Immunol. 2011;29:163-83. (PMID: 21219184)
Immunity. 2009 Jun 19;30(6):802-16. (PMID: 19523849)
Virus Res. 2014 Nov 4;192:34-45. (PMID: 25173696)
J Cell Sci. 1996 Jul;109 ( Pt 7):1727-38. (PMID: 8832395)
J Virol. 2012 Nov;86(21):11548-57. (PMID: 22896602)
Virus Res. 2017 Oct 15;242:90-95. (PMID: 28947336)
PLoS One. 2016 May 27;11(5):e0156513. (PMID: 27232627)
J Biol Chem. 2019 Apr 26;294(17):6888-6898. (PMID: 30872404)
Vet Microbiol. 2010 Jul 29;144(1-2):41-50. (PMID: 20074871)
Nat Rev Immunol. 2015 Feb;15(2):87-103. (PMID: 25614319)
J Virol. 2015 Dec 09;90(4):2090-101. (PMID: 26656704)
J Virol. 2008 Feb;82(4):1665-78. (PMID: 18077728)
Virus Genes. 2003 May;26(3):239-46. (PMID: 12876452)
Nature. 2005 Dec 1;438(7068):590-6. (PMID: 16319878)
Proc Natl Acad Sci U S A. 2017 Jun 27;114(26):6806-6811. (PMID: 28607080)
J Virol. 2016 Aug 26;90(18):8281-92. (PMID: 27384656)
Fish Shellfish Immunol. 2019 Mar;86:1026-1034. (PMID: 30584907)
J Virol. 2017 Dec 14;92(1):. (PMID: 29046456)
FEBS Lett. 2010 Mar 19;584(6):1263-7. (PMID: 20176015)

2018YFD0500500 the National Key Research and Development Program of China; No. 30771613 the National Natural Science Foundation in China

0 (Antiviral Agents)
0 (Nucleocapsid Proteins)
0 (Proteins)
9008-11-1 (Interferons)

Date Created: 20200729 Date Completed: 20200921 Latest Revision: 20220218

20221213

PMC7382991

10.1007/s00705-020-04747-8

32719955