食源性病原菌激发固有免疫细胞胞外诱捕网的研究进展

doi:10.11843/j.issn.0366-6964.2021.07.004

摘要/Abstract

摘要： 固有免疫细胞在外源物质刺激后向细胞胞外环境释放由染色质DNA和多种胞内颗粒蛋白组成的纤维样网状物质，称为胞外诱捕网（extracellular traps，ETs）。ETs是一种新型的宿主防御机制，能够捕获或杀灭病原菌，有效控制病原菌的扩散，从而使机体免受感染。大肠杆菌、沙门菌等食源性人兽共患病病原体引发的疾病是全球广泛关注的公共卫生问题。本文就食源性病原菌激发固有免疫细胞ETs的形成、ETs的生物学活性以及细菌部分蛋白对ETs形成的影响等研究进展进行综述，以期为食源性疾病的防控提供相关理论参考。

关键词: 食源性病原菌, 胞外诱捕网, 固有免疫细胞, 防御机制

Abstract: Innate immune cells release fibrous net substances which are composed of chromatin DNA and various intracellular protein components to the extracellular environment after being stimulated by exogenous substances. Those substances are called extracellular traps (ETs). ETs are new types of host defense mechanism that can capture or kill pathogens, control the spread of pathogens, and protect the body from infection. Diseases caused by foodborne zoonotic pathogens, such as Escherichia coli and Salmonella, are public health issues of widespread concern worldwide. This article reviews the research progress of the formation of ETs stimulated by foodborne pathogens, the biological activity of ETs, and the influence of some bacterial proteins on the formation of ETs. This article is intended to provide theoretical reference for the prevention and control of foodborne diseases.

Key words: foodborne pathogens, extracellular traps, innate immune cells, defense mechanism

中图分类号:

S852.42

钱满, 廖成水, 张春杰. 食源性病原菌激发固有免疫细胞胞外诱捕网的研究进展[J]. 畜牧兽医学报, 2021, 52(7): 1800-1808.

QIAN Man, LIAO Chengshui, ZHANG Chunjie. Research Progress on Extracellular Traps of Innate Immune Cells Stimulated by Foodborne Pathogens[J]. Acta Veterinaria et Zootechnica Sinica, 2021, 52(7): 1800-1808.

参考文献 61

[1]	LIANG X F, LIU L, WANG Y, et al. Autophagy-driven NETosis is a double-edged sword-review[J]. Biomed Pharmacother, 2020, 126:110065.
[2]	廖成水, PASCAL B, 刘明远, 等. 胞外捕获器:固有免疫细胞第三种防御机制的研究进展[J]. 畜牧兽医学报, 2016, 47(9):1768-1774.LIAO C S, PASCAL B, LIU M Y, et al. Research progress on extracellular traps:the third kinds of defence mechanisms of innate immune cells[J]. Acta Veterinaria et Zootechnica Sinica, 2016, 47(9):1768-1774. (in Chinese)
[3]	HALDER L D, ABDELFATAH M A, JO E A H, et al. Factor H binds to extracellular DNA traps released from human blood monocytes in response to Candida albicans[J]. Front Immunol, 2017, 7:671.
[4]	LIU P, WU X P, LIAO C S, et al. Escherichia coli and Candida albicans induced macrophage extracellular trap-like structures with limited microbicidal activity[J]. PLoS One, 2014, 9(2):e90042.
[5]	NG T H, CHANG S H, WU M H, et al. Shrimp hemocytes release extracellular traps that kill bacteria[J]. Dev Comp Immunol, 2013, 41(4):644-651.
[6]	BYSTRZYCKA W, SIECZKOWSKA S, MANDA-HANDZLIK A, et al. Influence of different bacteria strains isolated from septic children on release and degradation of extracellular traps by neutrophils from healthy adults[M]//POKORSKI M. Current Trends in Immunity and Respiratory Infections. Advances in Experimental Medicine and Biology. Cham:Springer, 2018, 1108:1-12.
[7]	MARIN-ESTEBAN V, TURBICA I, DUFOUR G, et al. Afa/Dr diffusely adhering Escherichia coli strain C1845 induces neutrophil extracellular traps that kill bacteria and damage human enterocyte-like cells[J]. Infect Immun, 2012, 80(5):1891-1899.
[8]	YU Y B, KWON K, PIEPER R. Detection of neutrophil extracellular traps in urine[M]//PEARSON M. Proteus Mirabilis. New York:Humana, 2019:241-257.
[9]	PATRAS K A, HA A D, ROOHOLFADA E, et al. Augmentation of urinary lactoferrin enhances host innate immune clearance of uropathogenic Escherichia coli[J]. J Innate Immun, 2019, 11(6):481-495.
[10]	GRINBERG N, ELAZAR S, ROSENSHINE I, et al. β-Hydroxybutyrate abrogates formation of bovine neutrophil extracellular traps and bactericidal activity against mammary pathogenic Escherichia coli[J]. Infect Immun, 2008, 76(6):2802-2807.
[11]	BRANZK N, LUBOJEMSKA A, HARDISON S E, et al. Neutrophils sense microbe size and selectively release neutrophil extracellular traps in response to large pathogens[J]. Nat Immunol, 2014, 15(11):1017-1025.
[12]	CRANE J K, BROOME J E, LIS A. Biological activities of uric acid in infection due to enteropathogenic and shiga-toxigenic Escherichia coli[J]. Infect Immun, 2016, 84(4):976-988.
[13]	PIEPER J, LOCKE M, RUZAIKE G, et al. In vitro and in vivo generation of heterophil extracellular traps after Salmonella exposure[J]. Vet Immunol Immunopathol, 2017, 188:1-11.
[14]	REDMOND S B, CHUAMMITRI P, ANDREASEN C B, et al. Genetic control of chicken heterophil function in advanced intercross lines:associations with novel and with known Salmonella resistance loci and a likely mechanism for cell death in extracellular trap production[J]. Immunogenetics, 2011, 63(7):449-458.
[15]	ZHAO X C, TANG X D, GUO N, et al. Biochanin a enhances the defense against Salmonella enterica infection through AMPK/ULK1/mTOR-mediated autophagy and extracellular traps and reversing SPI-1-dependent macrophage (MΦ) M2 polarization[J]. Front Cell Infect Microbiol, 2018, 8:318.
[16]	CHUAMMITRI P, REDMOND S B, KIMURA K, et al. Heterophil functional responses to dietary immunomodulators vary in genetically distinct chicken lines[J]. Vet Immunol Immunopathol, 2011, 142(3-4):219-227.
[17]	CAMPILLO-NA V M, LEYVA-PAREDES K, DONIS-MATURANO L, et al. Listeria monocytogenes induces mast cell extracellular traps[J]. Immunobiology, 2017, 222(2):432-439.
[18]	WANG C, WANG Y, SHI X C, et al. The TRAPs from microglial vesicles protect against Listeria infection in the CNS[J]. Front Cell Neurosci, 2019, 13:199.
[19]	MUNAFO D B, JOHNSON J L, BRZEZINSKA A A, et al. DNase I inhibits a late phase of reactive oxygen species production in neutrophils[J]. J Innate Immun, 2009, 1(6):527-542.
[20]	CHEN S T, LI F J, HSU T Y, et al. CLEC5A is a critical receptor in innate immunity against Listeria infection[J]. Nat Commun, 2017, 8(1):299.
[21]	MARGAROLI C, OBERLE S, LAVANCHY C, et al. Role of proapoptotic BH3-only proteins in Listeria monocytogenes infection[J]. Eur J Immunol, 2016, 46(6):1427-1437.
[22]	DAINICHI T, NAKAJIMA S, IWATA M, et al. NET effects of NETs:New concepts[J]. J Invest Dermatol, 2020, 140(5):939-941.
[23]	BITSCHAR K, STAUDENMAIER L, KLINK L, et al. Staphylococcus aureus skin colonization is enhanced by the interaction of neutrophil extracellular traps with keratinocytes[J]. J Invest Dermatol, 2020, 140(5):1054-1065.e4.
[24]	THAMMAVONGSA V, MISSIAKAS D M, SCHNEEWIND O. Staphylococcus aureus degrades neutrophil extracellular traps to promote immune cell death[J]. Science, 2013, 342(6160):863-866.
[25]	HSU C C, HSU R B, OHNIWA R L, et al. Neutrophil extracellular traps enhance Staphylococcus aureus vegetation formation through interaction with platelets in infective endocarditis[J]. Thromb Haemost, 2019, 119(5):786-796.
[26]	BJÖRNSDOTTIR H, RUDIN A D, KLOSE F P, et al. Phenol-soluble modulin α peptide toxins from aggressive Staphylococcus aureus induce rapid formation of neutrophil extracellular traps through a reactive oxygen species-independent pathway[J]. Front Immunol, 2017, 8:257.
[27]	HOPPENBROUWERS T, SULTAN A R, ABRAHAM T E, et al. Staphylococcal protein a is a key factor in neutrophil extracellular traps formation[J]. Front Immunol, 2018, 9:165.
[28]	MALACHOWA N, KOBAYASHI S D, FREEDMAN B, et al. Staphylococcus aureus leukotoxin GH promotes formation of neutrophil extracellular traps[J]. J Immunol, 2013, 191(12):6022-6029.
[29]	BHATTACHARYA M, BERENDS E T M, ZHENG X H, et al. Leukocidins and the nuclease nuc prevent neutrophil-mediated killing of Staphylococcus aureus biofilms[J]. Infect Immun, 2020, 88(10):e00372-20.
[30]	PILSCZEK F H, SALINA D, POON K K H, et al. A novel mechanism of rapid nuclear neutrophil extracellular trap formation in response to Staphylococcus aureus[J]. J Immunol, 2010, 185(12):7413-7425.
[31]	WANG T, ZHAO Y Y, FAN F L, et al. Dexamethasone inhibits S. aureus-induced neutrophil extracellular pathogen-killing mechanism, possibly through Toll-Like receptor regulation[J]. Front Immunol, 2017, 8:60.
[32]	SCHILCHER K, ANDREONI F, UCHIYAMA S, et al. Increased neutrophil extracellular trap-mediated Staphylococcus aureus clearance through inhibition of nuclease activity by clindamycin and immunoglobulin[J]. J Infect Dis, 2014, 210(3):473-482.
[33]	WANG X D, LI X Y, CHEN L Y, et al. Interleukin-33 facilitates cutaneous defense against Staphylococcus aureus by promoting the development of neutrophil extracellular trap[J]. Int Immunopharmacol, 2020, 81:106256.
[34]	MA F, YI L, YU N, et al. Streptococcus suis serotype 2 biofilms inhibit the formation of neutrophil extracellular traps[J]. Front Cell Infect Microbiol, 2017, 7:86.
[35]	ALEXANDER L E C, MAISEY H C, TIMMER A M, et al. M1T1 group A streptococcal pili promote epithelial colonization but diminish systemic virulence through neutrophil extracellular entrapment[J]. J Mol Med, 2010, 88(4):371-381.
[36]	TANAKA M, KINOSHITA-DAITOKU R, KIGA K, et al. Group A Streptococcus establishes pharynx infection by degrading the deoxyribonucleic acid of neutrophil extracellular traps[J]. Sci Rep, 2020, 10(1):3251.
[37]	WALKER M J, HOLLANDS A, SANDERSON-SMITH M L, et al. DNase Sda1 provides selection pressure for a switch to invasive group A streptococcal infection[J]. Nat Med, 2007, 13(8):981-985.
[38]	MA F, GUO X, FAN H J. Extracellular Nucleases of Streptococcus equi subsp. zooepidemicus degrade neutrophil extracellular traps and impair macrophage activity of the host[J]. Appl Environ Microbiol, 2016, 83(2):e02468-16.
[39]	DONG Y L, JIN C F, DING Z Q, et al. TLR4 regulates ROS and autophagy to control neutrophil extracellular traps formation against Streptococcus pneumoniae in acute otitis media[J]. Pediatr Res, 2020.doi:10. 1038/s41390-020-0964-9.
[40]	MORI Y, YAMAGUCHI M, TERAO Y, et al. α-enolase of Streptococcus pneumoniae induces formation of neutrophil extracellular traps[J]. J Biol Chem, 2012, 287(13):10472-10481.
[41]	ULLAH I, RITCHIE N D, EVANS T J. The interrelationship between phagocytosis, autophagy and formation of neutrophil extracellular traps following infection of human neutrophils by Streptococcus pneumoniae[J]. Innate Immun, 2017, 23(5):413-423.
[42]	HAAS B, GRENIER D. Isolation, characterization and biological properties of membrane vesicles produced by the swine pathogen Streptococcus suis[J]. PLoS One, 2015, 10(6):e0130528.
[43]	MARTINEZ P J, FARHAN A, MUSTAFA M, et al. PspA facilitates evasion of pneumococci from bactericidal activity of neutrophil extracellular traps (NETs)[J]. Microb Pathog, 2019, 136:103653.
[44]	DÖHRMANN S, ANIK S, OLSON J, et al. Role for streptococcal collagen-like protein 1 in M1T1 group A Streptococcus resistance to neutrophil extracellular traps[J]. Infect Immun, 2014, 82(10):4011-4020.
[45]	FILIO-RODRÍGUEZ G, ESTRADA-GARCÍ I, ARCE-PAREDES P, et al. In vivo induction of neutrophil extracellular traps by Mycobacterium tuberculosis in a guinea pig model[J]. Innate Immun, 2017, 23(7):625-637.
[46]	ONG C W M, FOX K, ETTORRE A, et al. Hypoxia increases neutrophil-driven matrix destruction after exposure to Mycobacterium tuberculosis[J]. Sci Rep, 2018, 8(1):11475.
[47]	FLOYD M, WINN M, CULLEN C, et al. Swimming motility mediates the formation of neutrophil extracellular traps induced by flagellated Pseudomonas aeruginosa[J]. PLoS Pathog, 2016, 12(11):e1005987.
[48]	MARTÍZ-ALEMÁN S, BUSTAMANTE A E, JIMENEZ-VALDES R J, et al. Pseudomonas aeruginosa isolates from cystic fibrosis patients induce neutrophil extracellular traps with different morphologies that could correlate with their disease severity[J]. Int J Med Microbiol, 2020, 310(7):151451.
[49]	BRUNS S, KNIEMEYER O, HASENBERG M, et al. Production of extracellular traps against Aspergillus fumigatus in vitro and in infected lung tissue is dependent on invading neutrophils and influenced by hydrophobin RodA[J]. PLoS Pathog, 2010, 6(4):e1000873.
[50]	SHARMA A, SIMONSON T J, JONDLE C N, et al. Mincle-mediated neutrophil extracellular trap formation by regulation of autophagy[J]. J Infect Dis, 2017, 215(7):1040-1048.
[51]	BRAIAN C, HOGEA V, STENDAHL O. Mycobacterium tuberculosis-induced neutrophil extracellular traps activate human macrophages[J]. J Innate Immun, 2013, 5(6):591-602.
[52]	DANG G H, CUI Y Y, WANG L, et al. Extracellular sphingomyelinase Rv0888 of Mycobacterium tuberculosis contributes to pathological lung injury of Mycobacterium smegmatis in mice via inducing formation of neutrophil extracellular traps[J]. Front Immunol, 2018, 9:677.
[53]	FRANCIS R J, BUTLER R E, STEWART G R. Mycobacterium tuberculosis ESAT-6 is a leukocidin causing Ca2+ influx, necrosis and neutrophil extracellular trap formation[J]. Cell Death Dis, 2014, 5(10):e1474.
[54]	WONG K W, JACOBS W R Jr. Mycobacterium tuberculosis exploits human interferon γ to stimulate macrophage extracellular trap formation and necrosis[J]. J Infect Dis, 2013, 208(1):109-119.
[55]	THANABALASURIAR A, SCOTT B N V, PEISELER M, et al. Neutrophil extracellular traps confine Pseudomonas aeruginosa ocular biofilms and restrict brain invasion[J]. Cell Host Microbe, 2019, 25(4):526-536.e4.
[56]	MCCORMICK A, HEESEMANN L, WAGENER J, et al. NETs formed by human neutrophils inhibit growth of the pathogenic mold Aspergillus fumigatus[J]. Microbes Infect, 2010, 12(12-13):928-936.
[57]	SEPER A, HOSSEINZADEH A, GORKIEWICZ G, et al. Vibrio cholerae evades neutrophil extracellular traps by the activity of two extracellular nucleases[J]. PLoS Pathog, 2013, 9(9):e1003614.
[58]	WILTON M, HALVERSON T W R, CHARRON-MAZENOD L, et al. Secreted phosphatase and deoxyribonuclease are required by Pseudomonas aeruginosa to defend against neutrophil extracellular traps[J]. Infect Immun, 2018, 86(9):e00403-18.
[59]	CASUTT-MEYER S, RENZI F, SCHMALER M, et al. Oligomeric coiled-coil adhesin yada is a double-edged sword[J]. PLoS One, 2010, 5(12):e15159.
[60]	刘春晓, 胡庆华. 中性粒细胞胞外诱捕网及其参与的免疫炎症性疾病研究进展[J]. 药学研究, 2020, 39(7):405-410.LIU C X, HU Q H. Research progress on neutrophil extracellular traps and related immune-inflammatory diseases[J]. Journal of Pharmaceutical Research, 2020, 39(7):405-410. (in Chinese)
[61]	FOUSERT E, TOES R, DESAI J. Neutrophil extracellular traps (NETs) take the central stage in driving autoimmune responses[J]. Cells, 2020, 9(4):915.