基于碳水化合物的佐剂作用机制研究进展

doi:10.11843/j.issn.0366-6964.2024.02.008

畜牧兽医学报 ›› 2024, Vol. 55 ›› Issue (2): 491-501.doi: 10.11843/j.issn.0366-6964.2024.02.008

基于碳水化合物的佐剂作用机制研究进展

周梦婷¹, 宋银娟^1*, 许健¹, 李斌², 冉多良², 储岳峰^1,2*

1. 中国农业科学院兰州兽医研究所, 兰州大学动物医学与生物安全学院, 动物疫病防控全国重点实验室, 兰州 730046;
2. 新疆农业大学动物医学学院, 乌鲁木齐 830052

收稿日期:2023-05-30 出版日期:2024-02-23 发布日期:2024-02-27
通讯作者: 储岳峰,主要从事动物重要细菌病和人兽共患细菌病研究与防控技术产品开发,E-mail:chuyuefeng@caas.cn;宋银娟,主要从事动物结核病致病机制及防控技术研究,E-mail:songyinjuan@caas.cn
作者简介:周梦婷(2000-),女,新疆石河子人,硕士生,主要从事牛结核病防控技术研究,E-mail:1615390902@qq.com
基金资助:
国家自然科学基金(32202806);甘肃省科技重大专项(22ZD6NA001);中国农业科学院基本科研业务费(1102311600420532023;1610312022010);中国农业科学院青年英才培育项目(NKLS2020-119);中国农业科学院创新工程项目(CAAS-ASTIP-2021-LVRI);2022年新疆维吾尔自治区科技特派员服务项目

Advances in Carbohydrate-based Adjuvant Mechanisms of Action

ZHOU Mengting¹, SONG Yinjuan^1*, XU Jian¹, LI Bin², RAN Duoliang², CHU Yuefeng^1,2*

1. State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046, China;
2. College of Animal Medicine, Xinjiang Agricultural University, Urumqi 830052, China

Received:2023-05-30 Online:2024-02-23 Published:2024-02-27

摘要/Abstract

摘要： 佐剂是指添加到疫苗中以刺激和增强免疫应答强度或改变免疫应答类型的物质。目前疫苗佐剂种类较多,包括铝佐剂、油乳佐剂和脂质体佐剂等,但临床使用的佐剂很少同时具备高效和低毒两大特点,因此迫切需要一种有效且安全的佐剂。基于碳水化合物的佐剂具有良好的生物相容性和易代谢的优点,同时,基于碳水化合物的佐剂种类广泛,且每种都有不同免疫特性,如基于多糖的佐剂可以增强巨噬细胞的吞噬活性及抗原提呈能力等。并且基于碳水化合物的佐剂还可与Toll样受体、C型凝集素受体等多种受体结合发挥上述免疫活性,但其作用机制尚不完全清楚。故本文基于碳水化合物的佐剂作用机制相关研究进展进行总结梳理,以期为相关佐剂的进一步研究提供参考。

关键词: 基于碳水化合物的佐剂, 多糖佐剂, 作用机制, 研究进展

Abstract: Adjuvants are substances added to vaccines to stimulate and enhance the intensity of immune responses or to change the type of immune responses. Currently, there are many types of vaccine adjuvants, including aluminum adjuvants, oil-in-water emulsion adjuvants, and liposome adjuvants, but few adjuvants used clinically have both high efficiency and low toxicity. Therefore, there is an urgent need for an effective and safe adjuvant. Carbohydrate-based adjuvants have the advantages of good biocompatibility and easy metabolism. Moreover, carbohydrate-based adjuvants have a wide range of types, and each type has different immune properties. For example, polysaccharide-based adjuvants can enhance macrophage phagocytic activity and antigen presentation ability. Carbohydrate-based adjuvants can also interact with various receptors such as Toll-like receptors and C-type lectin receptors to exert the above immune activities, but their mechanism of action is not yet fully understood. Therefore, this article summarizes the research progress on the mechanism of action of carbohydrate-based adjuvants, in order to provide reference for further research on adjuvants.

Key words: carbohydrate-based adjuvants, polysaccharide adjuvant, mechanism of action, research progress

中图分类号:

S852.4

周梦婷, 宋银娟, 许健, 李斌, 冉多良, 储岳峰. 基于碳水化合物的佐剂作用机制研究进展[J]. 畜牧兽医学报, 2024, 55(2): 491-501.

ZHOU Mengting, SONG Yinjuan, XU Jian, LI Bin, RAN Duoliang, CHU Yuefeng. Advances in Carbohydrate-based Adjuvant Mechanisms of Action[J]. Acta Veterinaria et Zootechnica Sinica, 2024, 55(2): 491-501.

参考文献

[1] REED S G, ORR M T, FOX C B. Key roles of adjuvants in modern vaccines[J]. Nat Med, 2013, 19(12):1597-1608.
[2] TREGONING J S, RUSSELL R F, KINNEAR E. Adjuvanted influenza vaccines[J]. Hum Vaccin Immunother, 2018, 14(3):550-564.
[3] KLUCKER M F, DALENÇON F, PROBECK P, et al. AF03, an alternative squalene emulsion-based vaccine adjuvant prepared by a phase inversion temperature method[J]. J Pharm Sci, 2012, 101(12):4490-4500.
[4] REYES C, PATARROYO M A. Adjuvants approved for human use:what do we know and what do we need to know for designing good adjuvants?[J]. Eur J Pharmacol, 2023, 945:175632.
[5] PETROVSKY N, COOPER P D. Carbohydrate-based immune adjuvants[J]. Exp Rev Vac, 2011, 10(4):523-537.
[6] GARCIA-VELLO P, SPECIALE I, CHIODO F, et al. Carbohydrate-based adjuvants[J]. Drug Discovery Today Technol, 2020, 35-36:57-68.
[7] JOHNSON-WEAVER B T, MCRITCHIE S, MERCIER K A, et al. Effect of endotoxin and alum adjuvant vaccine on peanut allergy[J]. J Allergy Clin Immunol, 2018, 141(2):791-794. e8.
[8] TZIANABOS A O. Polysaccharide immunomodulators as therapeutic agents:structural aspects and biologic function[J]. Clin Microbiol Rev, 2000, 13(4):523-533.
[9] MORENO-MENDIETA S, GUILLÉN D, HERNÁNDEZ-PANDO R, et al. Potential of glucans as vaccine adjuvants:a review of the α-glucans case[J]. Carbohydr Polym, 2017, 165:103-114.
[10] LARA-LEMUS R, ALVARADO-VÁSQUEZ N, ZENTENO E, et al. Effect of Histoplasma capsulatum glucans on host innate immunity[J]. Rev Iberoam Micol, 2014, 31(1):76-80.
[11] GAGLIARDI M C, LEMASSU A, TELONI R, et al. Cell wall-associated alpha-glucan is instrumental for Mycobacterium tuberculosis to block CD1 molecule expression and disable the function of dendritic cell derived from infected monocyte[J]. Cell Microbiol, 2007, 9(8):2081-2092.
[12] BITTENCOURT V C B, FIGUEIREDO R T, DA SILVA R B, et al. An α-glucan of Pseudallescheria boydii is involved in fungal phagocytosis and toll-like receptor activation[J]. J Biol Chem, 2006, 281(32):22614-22623.
[13] GEURTSEN J, CHEDAMMI S, MESTERS J, et al. Identification of mycobacterial α-glucan as a novel ligand for DC-SIGN:involvement of mycobacterial capsular polysaccharides in host immune modulation[J]. J Immunol, 2009, 183(8):5221-5231.
[14] GELLER A, SHRESTHA R, YAN J. Yeast-derived β-glucan in cancer:novel uses of a traditional therapeutic[J]. Int J Mol Sci, 2019, 20(15):3618.
[15] JIN Y M, LI P L, WANG F S. β-glucans as potential immunoadjuvants:a review on the adjuvanticity, structure-activity relationship and receptor recognition properties[J]. Vaccine, 2018, 36(35):5235-5244.
[16] RODRIGUES M V, ZANUZZO F S, KOCH J F A, et al. Development of fish immunity and the role of β-glucan in immune responses[J]. Molecules, 2020, 25(22):5378.
[17] BAJIC G, YATIME L, SIM R B, et al. Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3[J]. Proc Natl Acad Sci U S A, 2013, 110(41):16426-16431.
[18] GOODRIDGE H S, WOLF A J, UNDERHILL D M. β-glucan recognition by the innate immune system[J]. Immunol Rev, 2009, 230(1):38-50.
[19] XIA Y, VETVICKA, YAN J, et al. The beta-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells[J]. J Immunol, 1999, 162(4):2281-2290.
[20] BAERT K, SONCK E, GODDEERIS B M, et al. Cell type-specific differences in β-glucan recognition and signalling in porcine innate immune cells[J]. Dev Comp Immunol, 2015, 48(1):192-103.
[21] VERA J, FENUTRÍA R, CAÑADAS O, et al. The CD5 ectodomain interacts with conserved fungal cell wall components and protects from zymosan-induced septic shock-like syndrome[J]. Proc Natl Acad Sci U S A, 2009, 106(5):1506-1511.
[22] YANG C, GAO J, DONG H, et al. Expressions of scavenger receptor, CD14 and protective mechanisms of carboxymethyl-β-1, 3-glucan in posttraumatic endotoxemia in mice[J]. J Trauma, 2008, 65(6):1471-1477.
[23] TSIKITIS V L, MARTIN A, ALBINA J, et al. Ligation of the lactosylceramide receptor (CDw17) promotes neutrophil migration[J]. J Am Coll Surg, 2004, 199(S3):44.
[24] GOMAA K, KRAUS J, ROSSKOPF F, et al. Antitumour and immunological activity of a β1→3/1→6 glucan from Glomerella cingulata[J]. J Cancer Res Clin Oncol, 1992, 118(2):136-140.
[25] PENCE B D, HESTER S N, DONOVAN S M, et al. Dietary whole glucan particles do not affect antibody or cell-mediated immune responses to influenza virus vaccination in mice[J]. Immunol Invest, 2012, 41(3):275-289.
[26] YOUNES I, RINAUDO M. Chitin and chitosan preparation from marine sources. Structure, properties and applications[J]. Mar Drugs, 2015, 13(3):1133-1174.
[27] RINAUDO M. Chitin and chitosan:properties and applications[J]. Prog Polym Sci, 2006, 31(7):603-632.
[28] SUZUKI K, OKAWA Y, HASHIMOTO K. Protecting effect of chitin and chitosan on experimentally induced murine candidiasis[J]. Microbiol Immunol, 1984, 28(8):903-912.
[29] BUETER C L, LEE C K, WANG J P, et al. Spectrum and mechanisms of inflammasome activation by chitosan[J]. J Immunol, 2014, 192(12):5943-5951.
[30] CARROLL E C, JIN L, MORI A, et al. The vaccine adjuvant chitosan promotes cellular immunity via DNA sensor cGAS-STING-dependent induction of type I interferons[J]. Immunity, 2016, 44(3):597-608.
[31] LI X M, XING R E, XU C J, et al. Immunostimulatory effect of chitosan and quaternary chitosan:a review of potential vaccine adjuvants[J]. Carbohydr Polym, 2021, 264:118050.
[32] GONG X C, GAO Y, SHU J H, et al. Chitosan-based nanomaterial as immune adjuvant and delivery carrier for vaccines[J]. Vaccines (Basel), 2022;10(11):1906.
[33] DMOUR I, ISLAM N. Recent advances on chitosan as an adjuvant for vaccine delivery[J]. Int J Biol Macromol, 2022, 200:498-519.
[34] YVKSEL S, PEKCAN M, PURALI N, et al. Development and in vitro evaluation of a new adjuvant system containing Salmonella typhi porins and chitosan[J]. Int J Pharm, 2020, 578:119129.
[35] COHEN J. The immunopathogenesis of sepsis[J]. Nature, 2002, 420(6917):885-891.
[36] GARCIA-VELLO P, DI LORENZO F, ZUCCHETTA D, et al. Lipopolysaccharide lipid A:a promising molecule for new immunity-based therapies and antibiotics[J]. Pharmacol Ther, 2022, 230:107970.
[37] GAO J, GUO Z W. Progress in the synthesis and biological evaluation of lipid A and its derivatives[J]. Med Res Rev, 2018, 38(2):556-601.
[38] DOOLING K L, GUO A, PATEL M, et al. Recommendations of the advisory committee on immunization practices for use of herpes zoster vaccines[J]. MMWR Morb Mortal Wkly Rep, 2018, 67(3):103-108.
[39] BLANCO-PÉREZ F, GORETZKI A, WOLFHEIMER S, et al. The vaccine adjuvant MPLA activates glycolytic metabolism in mouse mDC by a JNK-dependent activation of mTOR-signaling[J]. Mol Immunol, 2019, 106:159-169.
[40] FERNÁNDEZ-TEJADA A, TAN D S, GIN D Y. Development of improved vaccine adjuvants based on the saponin natural product QS-21 through chemical synthesis[J]. Acc Chem Res, 2016, 49(9):1741-1756.
[41] MARCIANI D J. Elucidating the mechanisms of action of saponin-derived adjuvants[J]. Trends Pharmacol Sci, 2018, 39(6):573-585.
[42] LACAILLE-DUBOIS M A. Updated insights into the mechanism of action and clinical profile of the immunoadjuvant QS-21:a review[J]. Phytomedicine, 2019, 60:152905.
[43] MARTY-ROIX R, VLADIMER G I, POULIOT K, et al. Identification of QS-21 as an Inflammasome-activating molecular component of saponin adjuvants[J]. J Biol Chem, 2016, 291(3):1123-1136.
[44] FERNÁNDEZ-TEJADA A, CHEA E K, GEORGE C, et al. Development of a minimal saponin vaccine adjuvant based on QS-21[J]. Nat Chem, 2014, 6(7):635-643.
[45] MISHRA A K, DRIESSEN N N, APPELMELK B J, et al. Lipoarabinomannan and related glycoconjugates:structure, biogenesis and role in Mycobacterium tuberculosis physiology and host-pathogen interaction[J]. FEMS Microbiol Rev, 2011, 35(6):1126-1157.
[46] ISHIKAWA E, MORI D, YAMASAKI S. Recognition of mycobacterial lipids by immune receptors[J]. Trends Immunol, 2017, 38(1):66-76.
[47] MAZUREK J, IGNATOWICZ L, KALLENIUS G, et al. Divergent effects of mycobacterial cell wall glycolipids on maturation and function of human monocyte-derived dendritic cells[J]. PLoS One, 2012, 7(8):e42515.
[48] YONEKAWA A, SAIJO S, HOSHINO Y, et al. Dectin-2 is a direct receptor for mannose-capped lipoarabinomannan of mycobacteria[J]. Immunity, 2014, 41(3):402-413.
[49] MIYAKE Y, OH-HORA M, YAMASAKI S. C-Type lectin receptor MCL facilitates mincle expression and signaling through complex formation[J]. J Immunol, 2015, 194(11):5366-5374.
[50] WERNINGHAUS K, BABIAK A, GROSS O, et al. Adjuvanticity of a synthetic cord factor analogue for subunit Mycobacterium tuberculosis vaccination requires FcRγ-Syk-Card9-dependent innate immune activation[J]. J Exp Med, 2009, 206(1):89-97.
[51] THAKUR A, PINTO F E, HANSEN H S, et al. Intrapulmonary (i. pulmon.) pull immunization with the tuberculosis subunit vaccine candidate H56/CAF01 after intramuscular (i. m.) priming elicits a distinct innate myeloid response and activation of antigen-presenting cells than i. m. or i. pulmon. prime immunization alone[J]. Front Immunol, 2020, 11:803.
[52] RITTER K, BEHRENDS J, ERDMANN H, et al. Interleukin-23 instructs protective multifunctional CD4 T cell responses after immunization with the Mycobacterium tuberculosis subunit vaccine H1 DDA/TDB independently of interleukin-17A[J]. J Mol Med (Berl), 2021, 99(11):1585-1602.
[53] MARINA-GARCÍA N, FRANCHI L, KIM Y G, et al. Clathrin-and dynamin-dependent endocytic pathway regulates muramyl dipeptide internalization and NOD2 activation[J]. J Immunol, 2009, 182(7):4321-4327.
[54] IWICKA E, HAJTUCH J, DZIERZBICKA K, et al. Muramyl dipeptide-based analogs as potential anticancer compounds:strategies to improve selectivity, biocompatibility, and efficiency[J]. Front Oncol, 2022, 12:970967.
[55] CAO L T, LI J, ZHANG J R, et al. Beta-glucan enhanced immune response to Newcastle disease vaccine and changed mRNA expression of spleen in chickens[J]. Poult Sci, 2023, 102(2):102414.
[56] LIU Y, LIU X L, YANG L, et al. Adjuvanticity of β-glucan for vaccine against Trichinella spiralis[J]. Front Cell Dev Biol, 2021, 9:701708.
[57] KHADEMI F, TAHERI R A, YOUSEFI AVARVAND A, et al. Are chitosan natural polymers suitable as adjuvant/delivery system for anti-tuberculosis vaccines?[J]. Microb Pathog, 2018, 121:218-223.
[58] YANG Y, XING R E, LIU S, et al. Chitosan, hydroxypropyltrimethyl ammonium chloride chitosan and sulfated chitosan nanoparticles as adjuvants for inactivated Newcastle disease vaccine[J]. Carbohydr Polym, 2020, 229:115423.
[59] WANG Z B, SHAN P, LI S Z, et al. The mechanism of action of acid-soluble chitosan as an adjuvant in the formulation of nasally administered vaccine against HBV[J]. RSC Adv, 2016, 6(99):96785-96797.
[60] SHU M Y, ZHAO L H, SHI K L, et al. Chitosan particle stabilized Pickering emulsion/interleukin-12 adjuvant system for Pgp3 subunit vaccine elicits immune protection against genital chlamydial infection in mice[J]. Front Immunol, 2022, 13:989620.
[61] GARÇON N, CHOMEZ P, VAN MECHELEN M. Glaxosmithkline adjuvant systems in vaccines:concepts, achievements and perspectives[J]. Expert Rev Vaccines, 2007, 6(5):723-739.
[62] KHULLAR N, GUPTA C M, SEHGAL S. Immune response studies in relation to protection induced by using MDP as an adjuvant in malaria[J]. Immunol Invest, 1988, 17(1):1-17.

基于碳水化合物的佐剂作用机制研究进展

Advances in Carbohydrate-based Adjuvant Mechanisms of Action

RichHTML

PDF

可视化

摘要/Abstract

引用本文

使用本文

参考文献

相关文章 15

编辑推荐

Metrics

本文评价

[1]	刘元红, 胡玉欢, 张莉, 杨萍瑞, 胡卫东, 马琪, 毕师诚. 白术-肉苁蓉治疗便秘的网络药理学分析及试验验证[J]. 畜牧兽医学报, 2024, 55(2): 834-845.
[2]	张旭梅, 魏玉荣, 许丞惠, 杨彤, 史慧君, 付强, 杨莉. 基于网络药理学和试验验证分析小檗碱治疗鸡沙门菌感染的作用机制[J]. 畜牧兽医学报, 2023, 54(8): 3557-3570.
[3]	周炜炜, 王雪峰, 张梦洁, 杨娟, 孙悦龙, 张祖烽, 张宇欣, 豆佳红, 王梓颖, 戴小枫, 李秀梅. 基于生物网络功能模块整合组方规律分析四黄止痢颗粒治疗仔猪腹泻的作用机制[J]. 畜牧兽医学报, 2023, 54(7): 3031-3043.
[4]	毕睿晨, 刘相泽, 胡泽琼, 杨美雪, 乔嘉宁, 黄嘉, 郭芳申, 孔令华, 王忠. 植物多酚在家禽领域应用研究进展[J]. 畜牧兽医学报, 2023, 54(11): 4488-4501.
[5]	夏春秋, 万发春, 刘磊, 沈维军, 肖定福. 缬氨酸的生物学功能及其在畜禽日粮中的应用[J]. 畜牧兽医学报, 2023, 54(11): 4502-4513.
[6]	杨志梅, 梁成成, 张殿琦, 李雪峰, 昝林森. m⁶A修饰调控circRNA的研究进展[J]. 畜牧兽医学报, 2023, 54(10): 4016-4027.
[7]	孙栋, 屈莎, 李璇, 唐善虎, 李思宁, 郝刚. 抗菌肽Tachyplesin Ⅰ及衍生物对大肠杆菌细胞膜作用机制的对比研究[J]. 畜牧兽医学报, 2022, 53(9): 3180-3189.
[8]	孙康泰, 刘彬, 刘军, 蒋大伟, 姚志鹏, 葛毅强, 邓小明. 基于文献计量的“十三五”国家重点研发计划“畜禽专项”研究进展与热点趋势分析[J]. 畜牧兽医学报, 2022, 53(9): 2819-2832.
[9]	田薇, 李秀梅, 杨娟, 王小莹, 周炜炜, 李中媛, 戴小枫. 基于网络药理学研究板蓝根抑菌活性成分及其作用机制[J]. 畜牧兽医学报, 2022, 53(8): 2782-2793.
[10]	赵志显, 常雪蕊, 郭勇, 龙城, 盛熙晖, 王相国, 邢凯, 肖龙菲, 林自力, 倪和民, 齐晓龙. 种公鸡精液品质营养调控的研究进展[J]. 畜牧兽医学报, 2022, 53(8): 2435-2443.
[11]	孙严金, 薛亚男, 仲涛, 王林杰, 李利, 张红平, 占思远. HuR的功能及其对肌肉生长发育的调控作用[J]. 畜牧兽医学报, 2022, 53(5): 1345-1353.
[12]	刘贺娟, 史晨曦, 王静, 王美乐, 王栋涵, 魏战勇, 尹素改. 基于网络药理学探讨黄芩素对猪丁型冠状病毒感染的潜在作用机制[J]. 畜牧兽医学报, 2022, 53(11): 4097-4109.
[13]	吴香云, 刘亚娜, 周喆麒, 潘源虎, 郝海红, 程古月, 王玉莲. 多糖类化合物的抗菌作用及其机制研究进展[J]. 畜牧兽医学报, 2020, 51(6): 1167-1176.
[14]	董朕, 白东东, 刘利利, 白玉彬, 王玮玮, 张继瑜, 周绪正. 基于网络药理学分析归芪益母汤治疗牛气血两虚证的作用机制[J]. 畜牧兽医学报, 2018, 49(12): 2733-2744.
[15]	占思远，李利，王林杰，仲涛，张红平. 骨骼肌发育调控相关lncRNAs研究进展[J]. 畜牧兽医学报, 2016, 47(4): 637-644.