Type I Interferon Induced and Antagonized by Foot-and-Mouth Disease Virus

Overview

Journal Front Microbiol

Specialty Microbiology

Date 2018 Aug 29

PMID 30150977

Citations 11

Authors

Xiao-Xia Ma

Li-Na Ma

Qiu-Yan Chang

Peng Ma

Lin-Jie Li

Yue-Ying Wang

Zhong-Ren Ma

Xin Cao

Affiliations

Soon will be listed here.

Abstract

Viral infections trigger the innate immune system, serving as the first line of defense, and are characterized by the production of type I interferon (IFN). Type I IFN is expressed in a broad spectrum of cells and tissues in the host and includes various subtypes (IFN-α, IFN-β, IFN-δ, IFN-ε, IFN-κ, IFN-τ, IFN-ω, IFN-ν, and IFN-ζ). Since the discovery of type I IFN, our knowledge of the biology of type I IFN has accumulated immensely, and we now have a substantial amount of information on the molecular mechanisms of the response and induction of type I IFN, as well as the strategies utilized by viruses to evade the type I IFN response. Foot-and-mouth disease virus (FMDV) can selectively alter cellular pathways to promote viral replication and evade antiviral immune activation of type I IFN. RNA molecules generated by FMDV are sensed by the cellular receptor for pathogen-associated molecular patterns (PAMPs). FMDV preferentially activates different sensor molecules and various signal transduction pathways. Based on knowledge of the virus or RNA pathogen specificity as well as the function-structure relationship of RNA sensing, it is necessary to summarize numerous signaling adaptors that are reported to participate in the regulation of IFN gene activation.

Citing Articles

Development of a primary cell model derived from porcine dorsal soft palate for foot-and-mouth disease virus research and diagnosis.

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Isolation and characterization of the mink interferon-epsilon gene and its antiviral activity.

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The Swine IFN System in Viral Infections: Major Advances and Translational Prospects.

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References

Toka F, Golde W . Cell mediated innate responses of cattle and swine are diverse during foot-and-mouth disease virus (FMDV) infection: a unique landscape of innate immunity. Immunol Lett. 2013; 152(2):135-43. PMC: 7112845. DOI: 10.1016/j.imlet.2013.05.007. View

Bhatt M, Mohapatra J, Pandey L, Mohanty N, Das B, Prusty B . Mutational analysis of foot and mouth disease virus nonstructural polyprotein 3AB-coding region to design a negative marker virus. Virus Res. 2017; 243:36-43. DOI: 10.1016/j.virusres.2017.10.010. View

Zhou J, Zhang J, Ding Y, Chen H, Ma L, Liu Y . Characteristics of codon usage bias in two regions downstream of the initiation codons of foot-and-mouth disease virus. Biosystems. 2010; 101(1):20-8. DOI: 10.1016/j.biosystems.2010.04.001. View

Jackson S, Redeker A, Arens R, van Baarle D, van den Berg S, Benedict C . CMV immune evasion and manipulation of the immune system with aging. Geroscience. 2017; 39(3):273-291. PMC: 5505894. DOI: 10.1007/s11357-017-9986-6. View

Papon L, Oteiza A, Imaizumi T, Kato H, Brocchi E, Lawson T . The viral RNA recognition sensor RIG-I is degraded during encephalomyocarditis virus (EMCV) infection. Virology. 2009; 393(2):311-8. DOI: 10.1016/j.virol.2009.08.009. View

Huang L, Liu Q, Zhang L, Zhang Q, Hu L, Li C . Encephalomyocarditis Virus 3C Protease Relieves TRAF Family Member-associated NF-κB Activator (TANK) Inhibitory Effect on TRAF6-mediated NF-κB Signaling through Cleavage of TANK. J Biol Chem. 2015; 290(46):27618-32. PMC: 4646013. DOI: 10.1074/jbc.M115.660761. View

Venkataraman T, Valdes M, Elsby R, Kakuta S, Caceres G, Saijo S . Loss of DExD/H box RNA helicase LGP2 manifests disparate antiviral responses. J Immunol. 2007; 178(10):6444-55. DOI: 10.4049/jimmunol.178.10.6444. View

Buenz E, Howe C . Picornaviruses and cell death. Trends Microbiol. 2005; 14(1):28-36. DOI: 10.1016/j.tim.2005.11.003. View

Xu L, Wang Y, Han K, Li L, Zhai Z, Shu H . VISA is an adapter protein required for virus-triggered IFN-beta signaling. Mol Cell. 2005; 19(6):727-40. DOI: 10.1016/j.molcel.2005.08.014. View

10.

Pichlmair A, Schulz O, Tan C, Rehwinkel J, Kato H, Takeuchi O . Activation of MDA5 requires higher-order RNA structures generated during virus infection. J Virol. 2009; 83(20):10761-9. PMC: 2753146. DOI: 10.1128/JVI.00770-09. View

11.

Zhou J, Zhang J, Chen H, Ma L, Liu Y . Analysis of synonymous codon usage in foot-and-mouth disease virus. Vet Res Commun. 2010; 34(4):393-404. DOI: 10.1007/s11259-010-9359-4. View

12.

Lotufo C, Bergmann I, Mattion N, Wilda M, Grigera P . Recombinant foot-and-mouth disease virus (FMDV) non-structural protein 3A fused to enhanced green fluorescent protein (EGFP) as a candidate probe to identify FMDV-infected cattle in serosurveys. Arch Virol. 2017; 162(8):2279-2286. DOI: 10.1007/s00705-017-3359-4. View

13.

Ma X, Feng Y, Gu Y, Zhou J, Ma Z . Effect of the nucleotides surrounding the start codon on the translation of foot-and-mouth disease virus RNA. Acta Virol. 2016; 60(2):151-5. DOI: 10.4149/av_2016_02_151. View

14.

Zhao T, Yang L, Sun Q, Arguello M, Ballard D, Hiscott J . The NEMO adaptor bridges the nuclear factor-kappaB and interferon regulatory factor signaling pathways. Nat Immunol. 2007; 8(6):592-600. DOI: 10.1038/ni1465. View

15.

Karin M, Ben-Neriah Y . Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol. 2000; 18:621-63. DOI: 10.1146/annurev.immunol.18.1.621. View

16.

Li D, Wei J, Yang F, Liu H, Zhu Z, Cao W . Foot-and-mouth disease virus structural protein VP3 degrades Janus kinase 1 to inhibit IFN-γ signal transduction pathways. Cell Cycle. 2016; 15(6):850-60. PMC: 4845950. DOI: 10.1080/15384101.2016.1151584. View

17.

Guzylack-Piriou L, Bergamin F, Gerber M, McCullough K, Summerfield A . Plasmacytoid dendritic cell activation by foot-and-mouth disease virus requires immune complexes. Eur J Immunol. 2006; 36(7):1674-83. DOI: 10.1002/eji.200635866. View

18.

Hemmi H, Takeuchi O, Sato S, Yamamoto M, Kaisho T, Sanjo H . The roles of two IkappaB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection. J Exp Med. 2004; 199(12):1641-50. PMC: 2212809. DOI: 10.1084/jem.20040520. View

19.

Berke I, Li Y, Modis Y . Structural basis of innate immune recognition of viral RNA. Cell Microbiol. 2012; 15(3):386-94. DOI: 10.1111/cmi.12061. View

20.

Husser L, Alves M, Ruggli N, Summerfield A . Identification of the role of RIG-I, MDA-5 and TLR3 in sensing RNA viruses in porcine epithelial cells using lentivirus-driven RNA interference. Virus Res. 2011; 159(1):9-16. DOI: 10.1016/j.virusres.2011.04.005. View