病毒的锌指蛋白在病毒感染中的作用

doi:10.11843/j.issn.0366-6964.2021.011.003

Abstract

Abstract: Zinc finger(ZF) structure is a kind of common protein structure widely existing in animals, plants, microorganisms including many viruses. The characteristic group of amino acid residues in the peptide chain combines with Zn²⁺, thus forming a very short peptide space configuration which can self fold into "finger" shape. Zinc-finger proteins (ZNF) are proteins with zinc finger structure. It has been found that some viruses can encode zinc finger proteins, which can affect virus replication, packaging and release of mature virus particles, regulate and activate virus transcription and cleavage infection, and assist virus in innate immune escape. In this paper, the research progress of the role of ZNF in the process of virus infection is reviewed, which provides a reference for the further study of ZNF and the development of its targeting antiviral drugs.

Key words: zinc finger protein, zinc fingers, viral infection

CLC Number:

S852.65

DENG Xuewen, WANG Mingshu, CHENG Anchun. The Role of Zinc Finger Protein of Virus in Virus Infection[J]. Acta Veterinaria et Zootechnica Sinica, 2021, 52(11): 3014-3022.

References 94

[1]	OGO O A, TYSON J, COCKELL S J, et al. The zinc finger protein ZNF658 regulates the transcription of genes involved in zinc homeostasis and affects ribosome biogenesis through the zinc transcriptional regulatory element[J].Mol Cell Biol, 2015, 35(6):977987.
[2]	NAJAFABADI H S, ALBU M, HUGHES T R.Identification of C2H2-ZF binding preferences from ChIP-seq data using RCADE[J].Bioinformatics, 2015, 31(17):2879-2881.
[3]	BENHALEVY D, GUPTA S K, DANAN C H, et al. The Human CCHC-type zinc finger nucleic acid-binding protein binds G-rich elements in target mRNA coding sequences and promotes translation[J].Cell Rep, 2017, 18(12):2979-2990.
[4]	MALGIERI G, PALMIERI M, RUSSO L, et al. The prokaryotic zinc-finger:structure, function and comparison with the eukaryotic counterpart[J].FEBS J, 2015, 282(23):4480-4496.
[5]	WU S Y, TONG X L, LI C L, et al. BmBlimp-1 gene encoding a C2H2 zinc finger protein is required for wing development in the silkworm Bombyx mori[J].Int J Biol Sci, 2019, 15(12):2664-2675.
[6]	BHATIA S S, WEISS T C, ROMANIUK P J.Contribution of individual amino acids to the 5S RNA binding activity of the Xenopus zinc finger protein p43[J].Biochemistry, 2008, 47(32):8398-8405.
[7]	ZHANG X H, MIAO Y J, HU X D, et al. Gamma radiation-induced damage in the zinc finger of the transcription factor ⅢA[J].Bioinorg Chem Appl, 2016, 2016:1642064.
[8]	LOMBARDO C M, KUMAR M V V, DOUAT C, et al. Design and structure determination of a composite zinc finger containing a nonpeptide foldamer helical domain[J].J Am Chem Soc, 2019, 141(6):2516-2525.
[9]	CASSANDRI M, SMIRNOV A, NOVELLI F, et al. Zinc-finger proteins in health and disease[J].Cell Death Discov, 2017, 3:17071.
[10]	FEDOTOVA A A, BONCHUK A N, MOGILA V A, et al. C2H2 zinc finger proteins:the largest but poorly explored family of higher eukaryotic transcription factors[J].Acta Natur, 2017, 9(2):47-58.
[11]	BECARES M, PASCUAL-IGLESIAS A, NOGALES A, et al. Mutagenesis of Coronavirus nsp14 reveals its potential role in modulation of the innate immune response[J]. J Virol, 2016 May 12;90(11):5399-5414.
[12]	SHEKAR M, VENUGOPAL M N.Insight into a transcriptional adaptor zinc finger encoded by a putative protein in the white spot syndrome virus genome[J].Interdiscip Sci Comput Life Sci, 2019, 11(1):145-151.
[13]	ZUCK T F, THOMSON R A, SCHREIBER G B, et al. The Retrovirus Epidemiology Donor Study (REDS):rationale and methods[J].Transfusion, 2010, 35(11):944-951.
[14]	DOSTÁLKOVÁ A, KAUFMAN F, KŘÍŽOVÁ I, et al. Mutations in the basic region of the mason-Pfizer monkey virus nucleocapsid protein affect reverse transcription, genomic RNA packaging, and the virus assembly site[J].J Virol, 2018, 92(10):e00106-18.
[15]	HATAYAMA M, ARUGA J. Role of zic family proteins in transcriptional regulation and chromatin remodeling[J]. Adv Exp Med Biol, 2018;1046:353-380.
[16]	EOM K S, CHEONG J S, LEE S J.Structural analyses of zinc finger domains for specific interactions with DNA[J].J Micro Biol Biotechnol, 2016, 26(12):2019-2029.
[17]	DING P F, KHARYTONCHYK S, WALLER A, et al. Identification of the initial nucleocapsid recognition element in the HIV-1 RNA packaging signal[J].Proc Natl Acad Sci U S A, 2020, 117(30):17737-17746.
[18]	WEISS E R, GOTTLINGER H. The role of cellular factors in promoting HIV budding[J]. J Mol Biol, 2011 Jul 22;410(4):525-33.
[19]	LEE I J, STOKASIMOV E, DEMPSEY N, et al. Factors promoting nuclear envelope assembly independent of the canonical ES CRT pathway[J].J Cell Biol, 2020, 219(6):e201908232.
[20]	KIERNAN R E, VANHULLE C, SCHILTZ L, et al. HIV-1 Tat transcriptional activity is regulated by acetylation[J].EMBO J, 2014, 18(21):6106-6118.
[21]	RAO S, CINTI A, TEMZI A, et al. HIV-1 NC-induced stress granule assembly and translation arrest are inhibited by the dsRNA binding protein Staufen1[J].RNA, 2018, 24(2):219-236.
[22]	TANWAR H S, KHOO K K, GARVEY M, et al. The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV[J].PLoS Pathog, 2017, 13(2):e1006221.
[23]	KLINGLER J, ANTON H, RÉAL E, et al. How HIV-1 gag manipulates its host cell proteins:a focus on interactors of the nucle ocapsid domain[J].Viruses, 2020, 12(8):888.
[24]	COMAS-GARCIA M, DATTA S A, BAKER L, et al. Dissection of specific binding of HIV-1 Gag to the ‘packaging signal’ in viral RNA[J].eLife, 2017, 6:e27055.
[25]	NOVIKOVA M, ADAMS L J, FONTANA J, et al. Identification of a structural element in HIV-1 gag required for virus particle assembly and maturation[J].mBio, 2018, 9(5):e01567-18.
[26]	KOMA T, KOTANI O, MIYAKAWA K, et al. Allosteric regulation of HIV-1 capsid structure for gag assembly, virion production, and viral infectivity by a disordered interdomain linker[J].J Virol, 2019, 93(17):e00381-19.
[27]	SAKURAGI S, KOTANI O, YOKOYAMA M, et al. Identification of a novel cis-acting regulator of HIV-1 genome packaging[J].Int J Mol Sci, 2021, 22(7):3435.
[28]	PEDRO K D, HENDERSON A J, AGOSTO L M.Mechanisms of HIV-1 cell-to-cell transmission and the establishment of the latent reservoir[J].Virus Res, 2019, 265:115-121.
[29]	OLSON E D, MUSIER-FORSYTH K.Retroviral gag protein-RNA interactions:implications for specific genomic RNA packaging and virion assembly[J].Semin Cell Dev Biol, 2019, 86:129-139.
[30]	MEAGHER J L, TAKATA M, GONÇALVES-CARNEIRO D, et al. Structure of the zinc-finger antiviral protein in complex with RNA reveals a mechanism for selective targeting of CG-rich viral sequences[J].Proc Natl Acad Sci U S A, 2019, 116(48):24303-24309.
[31]	RAO S, HASSINE S, MONETTE A, et al. HIV-1 requires Staufen1 to dissociate stress granules and to produce infectious viral particles[J].RNA, 2019, 25(6):727-736.
[32]	RYE-MCCURDY T, OLSON E D, LIU S H, et al. Functional equivalence of retroviral MA domains in facilitating Psi RNA binding specificity by gag[J].Viruses, 2016, 8(9):256.
[33]	DILLEY K A, NIKOLAITCHIK O A, GALLI A, et al. Interactions between HIV-1 gag and viral RNA genome enhance virion assembly[J].J Virol, 2017, 91(16):e02319-16.
[34]	SETTE P, DUSSUPT V, BOUAMR F.Identification of the HIV-1 NC binding interface in Alix Bro1 reveals a role for RNA[J].J Virol, 2012, 86(21):11608-11615.
[35]	LLEWELLYN G N, HOGUE I B, GROVER J R, et al. Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cells[J].PLoS Pathogens, 2010, 6(10):e1001167.
[36]	IRACI N, ABARRINI O, SANTI C, et al. NCp7:targeting a multitask protein for next-generation anti-HIV drug development part 2.Noncovalent inhibitors and nucleic acid binders[J].Drug Discov Today, 2018, 23(3):687-695.
[37]	BOUTANT E, BONZI J, ANTON H, et al. Zinc fingers in HIV-1 gag precursor are not equivalent for gRNA recruitment at the plasma membrane[J].Biophys J, 2020 Jul 21;119(2):419-433.
[38]	ZHANG H, DORNADULA G, POMERANTZ R J.Endogenous reverse transcription of human immunodeficiency virus type 1 in physiological microenviroments:an important stage for viral infection of nondividing cells[J].J Virol, 1996, 70(5):2809-2824.
[39]	MONETTE A, NIU M J, CHEN L, et al. Pan-retroviral nucleocapsid-mediated phase separation regulates genomic RNA positioning and trafficking[J].Cell Rep, 2020, 31(3):107520.
[40]	IRIGOYEN N, DINAN A M, BRIERLEY I, et al. Ribosome profiling of the retrovirus murine leukemia virus[J].Retrovirology, 2018, 15(1):10.
[41]	DARLIX J L, LAPADAT-TAPOLSKY M, DE ROCQUIGNY H, et al. First glimpses at structure-function relationships of the nucleocapsid protein of retroviruses[J].J Mol Biol, 1995, 254(4):523-537.
[42]	GORELICK R J, FU W, GAGLIARDI T D, et al. Characterization of the block in replication of nucleocapsid protein zinc finger mutants from moloney murine leukemia virus[J].J Virol, 1999, 73(10):8185-8195.
[43]	GORELICK R J, CHABOT D J, OTT D E, et al. Genetic analysis of the zinc finger in the Moloney murine leukemia virus nucleocapsid domain:replacement of zinc-coordinating residues with other zinc-coordinating residues yields noninfectious particles containing genomic RNA[J].J Virol, 1996, 70(4):2593-2597.
[44]	STILL A, HUSEBY D, BARKLIS E.Analysis of the N-terminal region of the murine leukemia virus nucleocapsid protein[J].Virus Res, 2011, 155(1):181-188.
[45]	HOUSSET V, DE ROCQUIGNY H, ROQUES B P, et al. Basic amino acids flanking the zinc finger of Moloney murine leukemia virus nucleocapsid protein NCp10 are critical for virus infectivity[J].J Virol, 1993, 67(5):2537-2545.
[46]	GORELICK R J, BENVENISTE R E, GAGLIARDI T D, et al. Nucleocapsid protein zinc-finger mutants of simian immunodeficiency virus strain Mne produce virions that are replication defective in vitro and in vivo[J].Virology, 1999, 253(2):259-270.
[47]	AKAHATA W, IDO E, HAYAMI M.Mutational analysis of two zinc-finger motifs in the nucleocapsid protein of simian immunodeficiency virus mac239[J].J Gen Virol, 2003, 84(Pt 6):1641.
[48]	YOVANDICH J L, CHERTOVA E N, KANE B P, et al. Alteration of zinc-binding residues of simian immunodeficiency virus p8NC results in subtle differences in gag processing and virion maturation associated with degradative loss of mutant NC[J].J Virol, 2001, 75(1):115-124.
[49]	JIAO X L, SUI H Y, LYONS C, et al. Complete genome sequence of herpes simplex virus 1 strain McKrae[J].Microbiol Resour Announc, 2019, 8(39):e00993-19.
[50]	GARCÍA M, VOLKENING J, RIBLET S, et al. Genomic sequence analysis of the United States infectious laryngotracheitis vaccine strains chicken embryo origin (CEO) and tissue culture origin (TCO)[J].Virology, 2013, 440(1):64-74.
[51]	ZHANG D X, LAI M Y, CHENG A C, et al. Molecular characterization of the duck enteritis virus US10 protein[J].Virol J, 2017, 14(1):183.
[52]	WU Y, CHENG A, WANG M, et al. Complete genomic sequence of Chinese virulent duck enteritis virus[J].J Virol, 2012, 86(10):5965.
[53]	WU Y, CHENG A, WANG M, et al. Comparative genomic analysis of duck enteritis virus strains[J].J Virol, 2012, 86(24):13841-13842.
[54]	MA Y C, ZENG Q R, WANG M S, et al. US10 protein is crucial but not indispensable for duck enteritis virus infection in vitro[J].Sci Rep, 2018, 8(1):16510.
[55]	WU Y, LI Y G, WANG M S, et al. Preliminary study of the UL55 gene based on infectious Chinese virulent duck enteritis virus bacterial artificial chromosome clone[J].Virol J, 2017, 14(1):78.
[56]	GAO Y, CUI Y X, FOX T, et al. Structures and operating principles of the replisome[J].Science, 2019, 363(6429):eaav7003.
[57]	CHEN Y, LIVINGSTON C M, CARRINGTON-LAWRENCE S D, et al. A mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently[J].J Virol, 2007, 81(16):8742-8751.
[58]	LIUM E K, SILVERSTEIN S.Mutational analysis of the herpes simplex virus type 1 ICP0 C3HC4 zinc ring finger reveals a requirement for ICP0 in the expression of the essential alpha27 gene[J].J Virol, 1997, 71(11):8602-8614.
[59]	CHOTHE S K, SEBASTIAN A, THOMAS A, et al. Whole-genome sequence analysis reveals unique SNP profiles to distinguish vaccine and wild-type strains of bovine herpesvirus-1(BoHV-1)[J].Virology, 2018, 522:27-36.
[60]	INMAN M, ZHANG Y G, GEISER V, et al. The zinc ring finger in the bICP0 protein encoded by bovine herpesvirus-1 mediates toxicity and activates productive infection[J].J Gen Virol, 2001, 82(3):483-492.
[61]	SAIRA K, CHOWDHURY S, GAUDREAULT N, et al. The zinc RING finger of bovine herpesvirus 1-encoded bICP0 protein is crucial for viral replication and virulence[J].J Virol, 2008, 82(24):12060-12068.
[62]	LEHMANN K C, SNIJDER E J, POSTHUMA C C, et al. What we know but do not understand about nidovirus helicases[J]. Virus Res, 2015 Apr 16;202:12-32.
[63]	DENG Z Q, LEHMANN K C, LI X R, et al. Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase[J].Nucleic Acids Res, 2014, 42(5):3464-3477.
[64]	VAN DINTEN L C, VAN TOL H, GORBALENYA A E, et al. The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis[J].J Virol, 2000, 74(11):5213-5223.
[65]	SEYBERT A, POSTHUMA C C, VAN DINTEN L C, et al. A complex zinc finger controls the enzymatic activities of nidovirus helicases[J].J Virol, 2005, 79(2):696-704.
[66]	VAN DINTEN L C, RENSEN S, GORBALENYA A E, et al. Proteolytic processing of the open reading frame 1b-encoded part of arterivirus replicase is mediated by nsp4 serine protease and is essential for virus replication[J].J Virol, 1999, 73(3):2027-2037.
[67]	BOUVET M, IMBERT I, SUBISSI L, et al. RNA 3'-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex[J].Proc Natl Acad Sci U S A, 2012, 109(24):9372-9377.
[68]	JOSEPH J S, SAIKATENDU K S, SUBRAMANIAN V, et al. Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs[J].J Virol, 2006, 80(16):7894-7901.
[69]	OGANDO N S, ZEVENHOVEN-DOBBE J C, VAN DER MEER Y, et al. The enzymatic activity of the nsp14 exoribonuclease is critical for replication of MERS-CoV and SARS-CoV-2[J].J Virol, 2020, 94(23):e01246-20.
[70]	DU T F, NAN Y C, XIAO S Q, et al. Antiviral strategies against PRRSV infection[J].Trends Microbiol, 2017, 25(1-2):968-979.
[71]	GE Q H, CHEN X N, ZHAO YX, et al. Modulatory mechanisms of NLRP3:potential roles in inflammasome activation[J].Life Sci, 2021, 267:118918.
[72]	ALLEN I C, SCULL M A, MOORE C B, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza a virus through recognition of viral RNA[J].Immunity, 2009, 30(4):556-565.
[73]	KOMUNE N, ICHINOHE T, ITO M, et al. Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1β secretion[J].J Virol, 2011, 85(24):13019-13026.
[74]	CHEN X, BAI J, LIU X, et al. Nsp1α of porcine reproductive and respiratory syndrome virus strain BB0907 impairs the function of monocyte-derived dendritic cells via the release of soluble CD83[J]. J Virol. 2018 Jul 17;92(15):e00366-18.
[75]	CHEN Z, LIU S N, SUN W B, et al. Nuclear export signal of PRRSV NSP1α is necessary for type I IFN inhibition[J]. Virology, 2016, 499:278-287.
[76]	SUN Y NMXUE F, GUO Y, et al. Crystal structure of porcine reproductive and respiratory syndrome virus leader protease Nsp1α[J].J Virol, 2009, 83(21):10931-10940.
[77]	王超, 史西保, 王丽, 等. 猪繁殖与呼吸综合征病毒非结构蛋白1α(nsp1α)的N端锌指结构是其抑制NLRP3炎症小体活性所必需[J].畜牧兽医学报, 2015, 46(11):2032-2039.WANG C, SHI X B, WANG L, et al. The zinc-finger domain is essential for porcine reproductive and respiratory syndrome virus nonstructural protein 1α(nsp1α) to inhibit the NLRP3 inflammasome[J].Acta Veterinaria et Zootechnica Sinica, 2015, 46(11):2032-2039.(in Chinese)
[78]	SHI X B, ZHANG X Z, WANG F Y, et al. The zinc-finger domain was essential for porcine reproductive and respiratory syndrome virus nonstructural protein-1α to inhibit the production of interferon-β[J].J Interferon Cytokine Res, 2013, 33(6):328-334.
[79]	SEZGIN E, AN P, WINKLER C A.Host genetics of cytomegalovirus pathogenesis[J].Front Genet, 2019, 10:616.
[80]	ISING R, WEINHOLD S, BENNSTEIN S B, et al. HCMV infection in a mesenchymal stem cell Niche:differential impact on the development of NK cells versus ILC3[J].J Clin Med, 2019, 9(1):10.
[81]	KAUR G, TROWSDALE J, FUGGER L.Natural killer cells and their receptors in multiple sclerosis[J].Brain, 2013, 136(9):2657-2676.
[82]	ALEGRE E, RIZZO R, BORTOLOTTI D, et al. Some basic aspects of HLA-G biology[J].J Immunol Res, 2014, 2014:657625.
[83]	PARK B, SPOONER E, HOUSER B L, et al. The HCMV membrane glycoprotein US10 selectively targets HLA-G for degradation[J].J Exp Med, 2010, 207(9):2033-2041.
[84]	MA Y Y, WU L J, SHAW N, et al. Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex[J].Proc Natl Acad Sci U S A, 2015, 112(30):9436-9441.
[85]	CASE J B, ASHBROOK A W, DERMODY T S, et al. Mutagenesis of S-adenosyl-L-methionine-binding residues in coronavirus nsp14 N7-methyltransferase demonstrates differing requirements for genome translation and resistance to innate immunity[J].J Virol, 2016, 90(16):7248-7256.
[86]	MINSKAIA E, HERTZIG T, GORBALENYA A E, et al. Discovery of an RNA virus 3'→5' exoribonuclease that is critically involved in coronavirus RNA synthesis[J].Proc Natl Acad Sci U S A, 2006, 103(13):5108-5113.
[87]	BECARES M, PASCUAL-IGLESIAS A, NOGALES A, et al. Mutagenesis of coronavirus nsp14 reveals its potential role in modulation of the innate immune response[J].J Virol, 2016, 90(11):5399-5414.
[88]	CASE J B, LI Y Z, ELLIOTT R, et al. Murine hepatitis virus nsp14 exoribonuclease activity is required for resistance to innate immunity[J].J Virol, 2017, 92(1):e01531-17.
[89]	ABBEHAUSEN C.Zinc finger domains as therapeutic targets for metal-based compounds-an update[J].Metallomics, 2019, 11(1):15-28.
[90]	SCOTT T A, O'MEALLY D, GREPO N A, et al. Broadly active zinc finger protein-guided transcriptional activation of HIV-1[J].Mol Ther Methods Clin Dev, 2021, 20:18-29.
[91]	GOONAWARDANE N, NGUYEN D, SIMMONDS P.Association of zinc finger antiviral protein binding to viral genomic RNA with attenuation of replication of echovirus 7[J].mSphere, 2021, 6(1):e01138-20.
[92]	FICARELLI M, ANTZIN-ANDUETZA I, HUGH-WHITE R, et al. CpG dinucleotides inhibit HIV-1 replication through zinc finger antiviral protein (ZAP)-dependent and-independent mechanisms[J].J Virol, 2020, 94(6):e01337-19.
[93]	BLASIAK J, PAWLOWSKA E, CHOJNACKI J, et al. Zinc and autophagy in age-related macular degeneration[J]. Int J Mol Sci, 2020 Jul 15;21(14):4994.
[94]	MAEDA K, AKIRA S.Regulation of mRNA stability by CCCH-type zinc-finger proteins in immune cells[J].Int Immunol, 2017, 29(4):149-155.

The Role of Zinc Finger Protein of Virus in Virus Infection

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