口蹄疫病毒利用自身蛋白逃逸宿主天然免疫应答的研究进展

doi:10.11843/j.issn.0366-6964.2020.11.002

Abstract

Abstract: Foot-and-mouth disease (FMD) is an acute, hot, and highly contagious infectious disease caused by foot-and-mouth disease virus (FMDV) infection of cloven-hoofed animals. FMDV has seven serotypes and it spreads rapidly, which seriously affects the development of animal husbandry. FMDV is the prototype member of the Aphthovirus genus within the Picornaviridae family, and its genome encodes 4 structural proteins and 10 non-structural proteins. After infecting the host, FMDV uses its proteins to affect the host innate immune response through a variety of pathways and methods, which is beneficial to the microenvironment of FMDV replication. These strategies include FMDV involvement in autophagy, endoplasmic reticulum stress and stress granule formation of cellular processes, subverting the functions of various host proteins, such as hijacking, cleaving host proteins or interfering with the expression of host proteins, removing ubiquitin from host proteins, and inhibiting the phosphorylation of host proteins, which are also the focus of current research. Based on the existing research results, we summarized the research progress of FMDV protein in suppressing the innate immunity of host in recent years, intending to provide a reference for the research and prevention of FMDV.

Key words: foot-and-mouth disease virus, viral protein, innate immunity, cellular processes, immunity evasion

CLC Number:

S852.659.6

LI Xian, ZHANG Fudong, ZHANG Zhongwang, ZHANG Yongguang, PAN Li. Recent Advance on Foot-and-Mouth Disease Virus Utilizes Self-proteins to Evade Innate Immunity Response of Host[J]. Acta Veterinaria et Zootechnica Sinica, 2020, 51(11): 2622-2632.

References 78

[1]	LI D, ZHANG J, YANG W P, et al. Poly (rC) binding protein 2 interacts with VP0 and increases the replication of the foot-and-mouth disease virus[J]. Cell Death Dis, 2019, 10(7):516.
[2]	KNOWLES N J, SAMUEL A R. Molecular epidemiology of foot-and-mouth disease virus[J]. Virus Res, 2003, 91(1):65-80.
[3]	MEDINA G N, SEGUNDO F D S, STENFELDT C, et al. The different tactics of foot-and-mouth disease virus to evade innate immunity[J]. Front Microbiol, 2018, 9:2644.
[4]	KAWAI T, AKIRA S. The role of pattern-recognition receptors in innate immunity:update on Toll-like receptors[J]. Nat Immunol, 2010, 11(5):373-384.
[5]	KUMAR H, KAWAI T, AKIRA S. Pathogen recognition by the innate immune system[J]. Int Rev Immunol, 2011, 30(1):16-34.
[6]	PODRALSKA M, CIESIELSKA S, KLUIVER J, et al. Non-coding RNAs in cancer radiosensitivity:MicroRNAs and lncRNAs as regulators of radiation-induced signaling pathways[J]. Cancers, 2020, 12(6):1662.
[7]	SCHMEISSER H, BEKISZ J, ZOON K C. New function of type I IFN:induction of autophagy[J]. J Interf Cytok Res, 2014, 34(2):71-78.
[8]	SHI C S, KEHRL J H. MyD88 and trif target beclin 1 to trigger autophagy in macrophages[J]. J Biol Chem, 2008, 283(48):33175-33182.
[9]	JONES S A, MILLS K H G, HARRIS J. Autophagy and inflammatory diseases[J]. Immunol Cell Biol, 2013, 91(3):250-258.
[10]	GOVINDARAJAN S, VERHEUGEN E, VENKEN K, et al. ER stress in antigen-resenting cells promotes NKT cell activation through endogenous neutral lipids[J]. EMBO Rep, 2020, 21(6):e48927.
[11]	HAN S C, MAO L J, LIAO Y, et al. Sec62 suppresses foot-and-mouth disease virus proliferation by promotion of IRE1α-RIG-I antiviral signaling[J]. J Immunol, 2019, 203(2):429-440.
[12]	RANJITHA H B, AMMANATHAN V, GULERIA N, et al. Foot-and-mouth disease virus induces PERK-mediated autophagy to suppress the antiviral interferon response[J]. J Cell Sci, 2021, 134(5):jcs240622.
[13]	SUN P, ZHANG S M, QIN X D, et al. Foot-and-mouth disease virus capsid protein VP2 activates the cellular EIF2S1-ATF4 pathway and induces autophagy via HSPB1[J]. Autophagy, 2018, 14(2):336-346.
[14]	YANG W P, LI D, RU Y, et al. Foot-and-mouth disease virus 3A protein causes upregulation of autophagy-related protein LRRC25 to inhibit the G3BP1-mediated RIG-like Helicase-signaling pathway[J]. J Virol, 2020, 94(8):e02086-19.
[15]	VISSER L J, MEDINA G N, RABOUW H H, et al. Foot-and-mouth disease virus leader protease cleaves G3BP1 and G3BP2 and inhibits stress granule formation[J]. J Virol, 2019, 93(2):e00922-18.
[16]	YE X, PAN T, WANG D, et al. Foot-and-mouth disease virus counteracts on internal ribosome entry site suppression by G3BP1 and inhibits G3BP1-mediated stress granule assembly via post-translational mechanisms[J]. Front Immunol, 2018, 9:1142.
[17]	DUBUISSON J, COSSET F L. Virology and cell biology of the hepatitis C virus life cycle-an update[J]. J Hepatol, 2014, 61(1S):S3-S13.
[18]	LINDENBACH B D. Virion assembly and release[J]. Curr Top Microbiol Immunol, 2013, 369:199-218.
[19]	BARTENSCHLAGER R, PENIN F, LOHMANN V, et al. Assembly of infectious hepatitis C virus particles[J]. Trends Microbiol, 2011, 19(2):95-103.
[20]	WALTER P, RON D. The unfolded protein response:from stress pathway to homeostatic regulation[J]. Science, 2011, 334(6059):1081-1086.
[21]	DICKS N, GUTIERREZ K, MICHALAK M, et al. Endoplasmic reticulum stress, genome damage, and cancer[J]. Front Oncol, 2015, 5:11.
[22]	RON D, WALTER P. Signal integration in the endoplasmic reticulum unfolded protein response[J]. Nat Rev Mol Cell Biol, 2007, 8(7):519-529.
[23]	DASH S, AYDIN Y, WU T. Integrated stress response in hepatitis C promotes Nrf2-related chaperone-mediated autophagy:a novel mechanism for host-microbe survival and HCC development in liver cirrhosis[J]. Semin Cell Dev Biol, 2020, 101:20-35.
[24]	MEYER H A, GRAU H, KRAFT R, et al. Mammalian Sec61 is associated with Sec62 and Sec63[J]. J Biol Chem, 2000, 275(19):14550-14557.
[25]	TYEDMERS J, LERNER M, WIEDMANN M, et al. Polypeptide-binding proteins mediate completion of co-translational protein translocation into the mammalian endoplasmic reticulum[J]. EMBO Rep, 2003, 4(5):505-510.
[26]	LINXWEILER M, SCHICK B, ZIMMERMANN R. Let's talk about Secs:Sec61, Sec62 and Sec63 in signal transduction, oncology and personalized medicine[J]. Signal Transd Target Ther, 2017, 2(2):17002.
[27]	BIRGISDOTTIR Å B, LAMARK T, JOHANSEN T. The LIR motif-crucial for selective autophagy[J]. J Cell Sci, 2013, 126(15):3237-3247.
[28]	FUMAGALLI F, NOACK J, BERGMANN T J, et al. Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery[J]. Nat Cell Biol, 2016, 18(11):1173-1184.
[29]	GUO H C, JIN Y, HAN S C, et al. Quantitative proteomic analysis of BHK-21 cells infected with Foot-and-Mouth Disease Virus serotype Asia 1[J]. PLoS One, 2015, 10(7):e0132384.
[30]	KHAN T, RELITTI N, BRINDISI M, et al. Autophagy modulators for the treatment of oral and esophageal squamous cell carcinomas[J]. Med Res Rev, 2020, 40(3):1002-1060.
[31]	KAUR J, DEBNATH J. Autophagy at the crossroads of catabolism and anabolism[J]. Nat Rev Mol Cell Biol, 2015, 16(8):461-472.
[32]	LEE H K, LUND J M, RAMANATHAN B, et al. Autophagy-dependent viral recognition by plasmacytoid dendritic cells[J]. Science, 2007, 315(5817):1398-1401.
[33]	CHIRAMEL A I, BRADY N R, BARTENSCHLAGER R. Divergent roles of autophagy in virus infection[J]. Cells, 2013, 2(1):83-104.
[34]	SCHLEGEL A, GIDDINGS T H Jr, LADINSKY M S, et al. Cellular origin and ultrastructure of membranes induced during poliovirus infection[J]. J Virol, 1996, 70(10):6576-6588.
[35]	MCCORMICK C, KHAPERSKYY D A. Translation inhibition and stress granules in the antiviral immune response[J]. Nat Rev Immunol, 2017, 17(10):647-660.
[36]	KEDERSHA N, IVANOV P, ANDERSON P. Stress granules and cell signaling:more than just a passing phase?[J]. Trends Biochem Sci, 2013, 38(10):494-506.
[37]	REINEKE L C, DOUGHERTY J D, PIERRE P, et al. Large G3BP-induced granules trigger eIF2α phosphorylation[J]. Mol Biol Cell, 2012, 23(18):3499-3510.
[38]	ONOMOTO K, JOGI M, YOO J S, et al. Critical role of an antiviral stress granule containing RIG-I and PKR in viral detection and innate immunity[J]. PLoS One, 2012, 7(8):e43031.
[39]	LANGEREIS M A, FENG Q, VAN KUPPEVELD F J. MDA5 localizes to stress granules, but this localization is not required for the induction of type I interferon[J]. J Virol, 2013, 87(11):6314-6325.
[40]	KIM W J, BACK S H, KIM V, et al. Sequestration of TRAF2 into stress granules interrupts tumor necrosis factor signaling under stress conditions[J]. Mol Cell Biol, 2005, 25(6):2450-2462.
[41]	REINEKE L C, LLOYD R E. The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses[J]. J Virol, 2015, 89(5):2575-2589.
[42]	LI X Y, WANG J C, LIU J, et al. Engagement of soluble resistance-related calcium binding protein (sorcin) with foot-and-mouth disease virus (FMDV) VP1 inhibits type I interferon response in cells[J]. Vet Microbiol, 2013, 166(1-2):35-46.
[43]	ZHANG W, YANG F, ZHU Z X, et al. Cellular DNAJA3, a novel VP1-interacting protein, inhibits foot-and-mouth disease virus replication by inducing lysosomal degradation of VP1 and attenuating its antagonistic role in the Beta interferon signaling pathway[J]. J Virol, 2019, 93(13):e00588-19.
[44]	LI D, YANG W P, YANG F, et al. The VP3 structural protein of foot-and-mouth disease virus inhibits the IFN-β signaling pathway[J]. FASEB J, 2016, 30(5):1757-1766.
[45]	LI D, WEI J, YANG F, et al. Foot-and-mouth disease virus structural protein VP3 degrades Janus kinase 1 to inhibit IFN-γ signal transduction pathways[J]. Cell Cycle, 2016, 15(6):850-860.
[46]	RODRÍGUEZ PULIDO M, SÁNCHEZ-APARICIO M T, MARTÍNEZ-SALAS E, et al. Innate immune sensor LGP2 is cleaved by the Leader protease of foot-and-mouth disease virus[J]. PLoS Pathog, 2018, 14(6):e1007135.
[47]	SWATEK K N, AUMAYR M, PRUNEDA J N, et al. Irreversible inactivation of ISG15 by a viral leader protease enables alternative infection detection strategies[J]. Proc Natl Acad Sci U S A, 2018, 115(10):2371-2376.
[48]	LI D, LEI C Q, XU Z S, et al. Foot-and-mouth disease virus non-structural protein 3A inhibits the interferon-β signaling pathway[J]. Sci Rep, 2016, 6(1):21888.
[49]	FU S Z, YANG W P, RU Y, et al. DDX56 cooperates with FMDV 3A to enhance FMDV replication by inhibiting the phosphorylation of IRF3[J]. Cell Signal, 2019, 64:109393.
[50]	ZHU Z X, LI C T, DU X L, et al. Foot-and-mouth disease virus infection inhibits LGP2 protein expression to exaggerate inflammatory response and promote viral replication[J]. Cell Death Dis, 2017, 8(4):e2747.
[51]	ZHU Z X, WANG G Q, YANG F, et al. Foot-and-Mouth Disease Virus viroporin 2B antagonizes RIG-I-mediated antiviral effects by inhibition of its protein expression[J]. J Virol, 2016, 90(24):11106-11121.
[52]	LIU H S, XUE Q, CAO W J, et al. Foot-and-mouth disease virus nonstructural protein 2B interacts with cyclophilin A, modulating virus replication[J]. FASEB J, 2018, 32(12):6706-6723.
[53]	LI C T, ZHU Z X, DU X L, et al. Foot-and-mouth disease virus induces lysosomal degradation of host protein kinase PKR by 3C proteinase to facilitate virus replication[J]. Virology, 2017, 509:222-231.
[54]	FAN X X, HAN S C, YAN D, et al. Foot-and-mouth disease virus infection suppresses autophagy and NF-кB antiviral responses via degradation of ATG5-ATG12 by 3Cpro[J]. Cell Death Dis, 2017, 8(1):e2561.
[55]	LIU H S, ZHU Z X, XUE Q, et al. Foot-and-mouth disease virus antagonizes NOD2-mediated antiviral effects by inhibiting NOD2 protein expression[J]. J Virol, 2019, 93(11):e00124-19.
[56]	GRUBMAN M J, BAXT B. Foot-and-mouth disease[J]. Clin Microbiol Rev, 2004, 17(2):465-493.
[57]	BERINSTEIN A, ROIVAINEN M, HOVI T, et al. Antibodies to the Vitronectin receptor (integrin alpha V beta 3) inhibit binding and infection of foot-and-mouth disease virus to cultured cells[J]. J Virol, 1995, 69(4):2664-2666.
[58]	NEFF S, SÁ-CARVALHO D, RIEDE E, et al. Foot-and-mouth disease virus virulent for cattle utilizes the integrin αvβ3 as its receptor[J]. J Virol, 1998, 72(5):3587-3594.
[59]	SETH R B, SUN L J, EA C K, et al. Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3[J]. Cell, 2005, 122(5):669-682.
[60]	LIU S Q, CAI X, WU J X, et al. Phosphorylation of innate immune adaptor proteins MAVS, STING, and TRIF induces IRF3 activation[J]. Science, 2015, 347(6227):aaa2630.
[61]	STEINBERGER J, SKERN T. The leader proteinase of foot-and-mouth disease virus:structure-function relationships in a proteolytic virulence factor[J]. Biol Chem, 2014, 395(10):1179-1185.
[62]	FREIMANIS G L, DI NARDO A, BANKOWSKA K, et al. Genomics and outbreaks:foot and mouth disease[J]. Rev Sci Tech, 2016, 35(1):175-189.
[63]	RODRÍGUEZ PULIDO M, SÁIZ M. Molecular mechanisms of foot-and-mouth disease virus targeting the host antiviral response[J]. Front Cell Infect Microbiol, 2017, 7:252.
[64]	LIU Y Q, ZHU Z X, ZHNAG M T, et al. Multifunctional roles of leader protein of foot-and-mouth disease viruses in suppressing host antiviral responses[J]. Vet Res, 2015, 46(1):127.
[65]	FALK M M, GRIGERA P R, BERGMANN I E, et al. Foot-and-mouth disease virus protease 3C induces specific Proteolytic cleavage of host cell histone H3[J]. J Virol, 1990, 64(2):748-756.
[66]	BELSHAM G J, MCINERNEY G M, ROSS-SMITH N. Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells[J]. J Virol, 2000, 74(1):272-280.
[67]	WANG D, FANG L R, LI K, et al. Foot-and-mouth disease virus 3C protease cleaves NEMO to impair innate immune signaling[J]. J Virol, 2012, 86(17):9311-9322.
[68]	LAWRENCE P, SCHAFER E A, RIEDER E. The nuclear protein Sam68 is cleaved by the FMDV 3C protease redistributing Sam68 to the cytoplasm during FMDV infection of host cells[J]. Virology, 2012, 425(1):40-52.
[69]	DU Y J, BI J S, LIU J Y, et al. 3Cpro of foot-and-mouth disease virus antagonizes the interferon signaling pathway by blocking STAT1/STAT2 nuclear translocation[J]. J Virol, 2014, 88(9):4908-4920.
[70]	GLADUE D P, LARGO E, DE LA ARADA I, et al. Molecular characterization of the viroporin function of foot-and-mouth disease virus nonstructural protein 2B[J]. J Virol, 2018, 92(23):e01360-18.
[71]	AO D, GUO H C, SUN S Q, et al. Viroporin activity of the foot-and-mouth disease virus non-structural 2B protein[J]. PLoS One, 2015, 10(5):e0125828.
[72]	ISAACSON M K, PLOEGH H L. Ubiquitination, ubiquitin-like modifiers, and Deubiquitination in viral infection[J]. Cell Host Microbe, 2009, 5(6):559-570.
[73]	HEATON S M, BORG N A, DIXIT V M. Ubiquitin in the activation and attenuation of innate antiviral immunity[J]. J Exp Med, 2016, 213(1):1-13.
[74]	ZHAO C, COLLINS M N, HSIANG T Y, et al. Interferon-induced ISG15 pathway:an ongoing virus-host battle[J]. Trends Microbiol, 2013, 21(4):181-186.
[75]	DURFEE L A, LYON N, SEO K, et al. The ISG15 conjugation system broadly targets newly synthesized proteins:implications for the antiviral function of ISG15[J]. Mol Cell, 2010, 38(5):722-732.
[76]	SUNG Y Y, KIM H K. Illicium verum extract suppresses IFN-γ-induced ICAM-1 expression via blockade of JAK/STAT pathway in HaCaT human keratinocytes[J]. J Ethnopharmacol, 2013, 149(3):626-632.
[77]	RAGHAVAN B, COOK C H, TRGOVCICH J. The Carboxy terminal region of the human cytomegalovirus Immediate Early 1(IE1) protein disrupts Type II Inteferon signaling[J]. Viruses, 2014, 6(4):1502-1524.
[78]	GOODBOURN S, DIDCOCK L, RANDALL R E. Interferons:cell signalling, immune modulation, antiviral response and virus countermeasures[J]. J Gen Virol, 2000, 81(10):2341-2364.

Recent Advance on Foot-and-Mouth Disease Virus Utilizes Self-proteins to Evade Innate Immunity Response of Host

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