Abstract
Glucans are a group of polysaccharides that are isolated from plants and microorganisms that have interesting specificities on physicochemical properties that make each one useful polymers for food and other industrial applications, but that regard some key resemblance, the β-1➔3-glucopyranose presence and the modulation of the immune system. Versatile, accept a wide range of conjugable groups, and its being receiving more and more attention as investigations reveals the mechanisms and the relation between structure and function that move specific events in response to antigens. This chapter review a short period of time, mostly the last 3 years on the research of this immunomodulators polysaccharides as therapeutic agents and vaccine adjuvants.
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Abraham A, Ostroff G, Levitz SM, Oyston PCF. A novel vaccine platform using glucan particles for induction of protective responses against Francisella tularensis and other pathogens. Clin Exp Immunol. 2019;198(2):143–52. https://doi.org/10.1111/cei.13356.
Adachi Y, Ishii T, Ikeda Y, Hoshino A, Tamura H, Aketagawa J, et al. Characterization of beta-glucan recognition site on C-type lectin, Dectin 1. Infect Immun. 2004;72(7):4159–71. https://doi.org/10.1128/IAI.72.7.4159-4171.2004.
Alipour M, Baneshi M, Hosseinkhani S, Mahmoudi R, Jabari Arabzadeh A, Akrami M, et al. Recent progress in biomedical applications of RGD-based ligand: from precise cancer theranostics to biomaterial engineering: a systematic review. J Biomed Mater Res A. 2020;108(4):839–50. https://doi.org/10.1002/jbm.a.36862.
Anaya EU, Amin AE, Wester MJ, Danielson ME, Michel KS, Neumann AK.. Dectin-1 molecular aggregation and signaling is sensitive to β-glucan structure and glucan exposure on Candida albicans cell walls. BioRxiv. 2020;824995. https://doi.org/10.1101/824995.
Arts RJW, Carvalho A, La Rocca C, Palma C, Rodrigues F, Silvestre R, et al. Immunometabolic pathways in BCG-induced trained immunity. Cell Rep. 2016;17(10):2562–71. https://doi.org/10.1016/j.celrep.2016.11.011.
Borges O, Silva M, de Sousa A, Borchard G, Junginger HE, Cordeiro-da-Silva A. Alginate coated chitosan nanoparticles are an effective subcutaneous adjuvant for hepatitis B surface antigen. Int Immunopharmacol. 2008;8(13–14):1773–80. https://doi.org/10.1016/j.intimp.2008.08.013.
Brown GD, Gordon S. A new receptor for β-glucans. Nature. 2001;413(6851):36–7. https://doi.org/10.1038/35092620.
Brown GD, Taylor PR, Reid DM, Willment JA, Williams DL, Martinez-Pomares L, et al. Dectin-1 is a major β-glucan receptor on macrophages. J Exp Med. 2002;196(3):407–12. https://doi.org/10.1084/jem.20020470.
Brown J, O’Callaghan CA, Marshall ASJ, Gilbert RJC, Siebold C, Gordon S, et al. Structure of the fungal β-glucan-binding immune receptor Dectin-1: implications for function. Protein Sci. 2007;16(6):1042–52. https://doi.org/10.1110/ps.072791207.
Brown GD, Willment JA, Whitehead L. C-type lectins in immunity and homeostasis. Nat Rev Immunol. 2018;18(6):374–89. https://doi.org/10.1038/s41577-018-0004-8.
CDC. Vaccine excipient summary. Johns Hopkins University. 2019. Retrieved from http://www.fda.gov/BiologicsBloodVaccines/Vaccines/ApprovedProducts/ucm093833.htm
Cebadera Miranda E, Castillo Ruiz-Cabello MV, Cámara Hurtado M. Food biopharmaceuticals as part of a sustainable bioeconomy: edible vaccines case study. New Biotechnol. 2020;59:74–9. https://doi.org/10.1016/J.NBT.2020.06.005.
Cheng SC, Quintin J, Cramer RA, Shepardson KM, Saeed S, Kumar V, et al. MTOR- and HIF-1α-mediated aerobic glycolysis as metabolic basis for trained immunity. Science. 2014;345(6204):1250684. https://doi.org/10.1126/science.1250684.
Daley D, Mani VR, Mohan N, Akkad N, Ochi A, Heindel DW, et al. Dectin 1 activation on macrophages by galectin 9 promotes pancreatic carcinoma and peritumoral immune tolerance. Nat Med. 2017;23(5):556–67. https://doi.org/10.1038/nm.4314.
De Smet R, Demoor T, Verschuere S, Dullaers M, Ostroff GR, Leclercq G, et al. β-Glucan microparticles are good candidates for mucosal antigen delivery in oral vaccination. J Control Release. 2013;172(3):671–8. https://doi.org/10.1016/j.jconrel.2013.09.007.
DeBerardinis RJ, Chandel NS. We need to talk about the Warburg effect. Nat Metab. 2020;2(2):127–9. https://doi.org/10.1038/s42255-020-0172-2.
Di Luzio NR, Williams DL. Protective effect of glucan against systemic Staphylococcus aureus septicemia in normal and leukemic mice. Infect Immun. 1978;20(3):804–10. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/352959
Di Luzio NR, Williams DL. Glucan-induced modification of the increased susceptibility of cyclophosphamide-treated mice to Staphylococcus aureus infection. Cancer Immunol Immunother. 1979;6(2):73–9. https://doi.org/10.1007/BF00200135.
Dickinson E. Colloid science of mixed ingredients. Soft Matter. 2006;2(8):642–52. https://doi.org/10.1039/b605670a.
Du B, Meenu M, Liu H, Xu B. A concise review on the molecular structure and function relationship of β-glucan. Int J Mol Sci. Multidisciplinary Digital Publishing Institute. 2019;20(16):4032. https://doi.org/10.3390/ijms20164032.
Dulal HP, Adachi Y, Ohno N, Yamaguchi Y. β-Glucan-induced cooperative oligomerization of Dectin-1 C-type lectin-like domain. Glycobiology. 2018;28(8):612–23. https://doi.org/10.1093/glycob/cwy039.
Effendi WI, Nagano T, Hasan H, Yudhawati R. Immunoregulatory property of C-type Lectin-like receptors in fibrosing interstitial lung diseases. Int J Mol Sci. 2020;21(10):3665. https://doi.org/10.3390/ijms21103665.
Elola MT, Ferragut F, Méndez-Huergo SP, Croci DO, Bracalente C, Rabinovich GA. Galectins: multitask signaling molecules linking fibroblast, endothelial and immune cell programs in the tumor microenvironment; 2018. https://doi.org/10.1016/j.cellimm.2018.03.008.
Fei C, Pemberton JG, Lillico DME, Zwozdesky MA, Stafford JL. Biochemical and functional insights into the integrated regulation of innate immune cell responses by teleost leukocyte immune-type receptors. Biology. Multidisciplinary Digital Publishing Institute. 2016;5(1):13. https://doi.org/10.3390/biology5010013.
Goodridge HS, Underhill DM, Touret N. Mechanisms of Fc receptor and Dectin-1 activation for phagocytosis. Traffic. Wiley. 2012;13(8):1062–71. https://doi.org/10.1111/j.1600-0854.2012.01382.x.
Gour N, Lajoie S, Smole U, White M, Hu D, Goddard P, et al. Dysregulated invertebrate tropomyosin-Dectin-1 interaction confers susceptibility to allergic diseases. Sci Immunol. 2018;3(20):eaam9841. https://doi.org/10.1126/sciimmunol.aam9841.
Gudmundsdottir AB, Brynjolfsdottir A, Olafsdottir ES, Hardardottir I, Freysdottir J. Exopolysaccharides from Cyanobacterium aponinum induce a regulatory dendritic cell phenotype and inhibit SYK and CLEC7A expression in dendritic cells, T cells and keratinocytes. Int Immunopharmacol. 2019;69:328–36. https://doi.org/10.1016/J.INTIMP.2019.01.044.
Hanashima S, Ikeda A, Tanaka H, Adachi Y, Ohno N, Takahashi T, Yamaguchi Y. NMR study of short β(1–3)-glucans provides insights into the structure and interaction with Dectin-1. Glycoconj J. 2014;31(3):199–207. https://doi.org/10.1007/s10719-013-9510-x.
Hester MM, Lee CK, Abraham A, Khoshkenar P, Ostroff GR, Levitz SM, Specht CA. Protection of mice against experimental cryptococcosis using glucan particle-based vaccines containing novel recombinant antigens. Vaccine. 2020;38(3):620–6. https://doi.org/10.1016/j.vaccine.2019.10.051.
Hossain M, Wall K. Use of dendritic cell receptors as targets for enhancing anti-cancer immune responses. Cancers. 2019;11(3):418. https://doi.org/10.3390/cancers11030418.
Huang Y, Ren Q. Research progress in innate immunity of freshwater crustaceans. Dev Comp Immunol. 2020;104:103569. https://doi.org/10.1016/j.dci.2019.103569.
Ishikawa E, Mori D, Yamasaki S. Recognition of mycobacterial lipids by immune receptors. Trends Immunol. 2017;38(1):66–76. https://doi.org/10.1016/J.IT.2016.10.009.
Jayachandran M, Chen J, Chung SSM, Xu B. A critical review on the impacts of β-glucans on gut microbiota and human health. J Nutr Biochem. Elsevier. 2018;61:101–10. https://doi.org/10.1016/j.jnutbio.2018.06.010.
Junter GA, Karakasyan C. Polysaccharides against viruses: Immunostimulatory properties and the delivery of antiviral vaccines and drugs. Crit Rev Ther Drug Carrier Syst. 2020;37(1):1–64. https://doi.org/10.1615/CritRevTherDrugCarrierSyst.2019027229.
Karsten CM, Pandey MK, Figge J, Kilchenstein R, Taylor PR, Rosas M, et al. Anti-inflammatory activity of IgG1 mediated by Fc galactosylation and association of FcγRIIB and Dectin-1. Nat Med. 2012;18(9):1401–6. https://doi.org/10.1038/nm.2862.
Kumar P, Ahmad S. Glucan-induced immunity in mice against Plasmodium berghei. Ann Trop Med Parasitol. 1985;79(2):211–3. https://doi.org/10.1080/00034983.1985.11811908.
Lang S, Huang X. Carbohydrate conjugates in vaccine developments. Front Chem. 2020;8:284. https://doi.org/10.3389/fchem.2020.00284.
Lefèvre L, Lugo-Villarino G, Meunier E, Valentin A, Olagnier D, Authier H, et al. The C-type Lectin receptors Dectin-1, MR, and SIGNR3 contribute both positively and negatively to the macrophage response to Leishmania infantum. Immunity. 2013;38(5):1038–49. https://doi.org/10.1016/J.IMMUNI.2013.04.010.
Li D, Bai C, Zhang Q, Li Z, Shao D, Li X. β-1,3-Glucan/CR3/SYK pathway-dependent LC3B-II accumulation enhanced the fungicidal activity in human neutrophils. J Microbiol. 2019;57(4):263–70. https://doi.org/10.1007/s12275-019-8298-1.
Maheshwari G, Sowrirajan S, Joseph B. β-Glucan, a dietary fiber in effective prevention of lifestyle diseases – an insight. Bioact Carbohydr Diet Fibre. Elsevier. 2019;19:100187. https://doi.org/10.1016/j.bcdf.2019.100187.
Miyamoto N, Mochizuki S, Sakurai K. A novel polysaccharide carrier for functional oligonucleotides: immunocyte targeting through β-glucan receptors. ACS Symp Ser. 2019;1309:79–92. https://doi.org/10.1021/bk-2019-1309.ch004.
Moorlag SJCFM, Khan N, Novakovic B, Kaufmann E, Jansen T, van Crevel R, et al. β-glucan induces protective trained immunity against Mycobacterium tuberculosis infection: a key role for IL-1. Cell Rep. 2020;31(7):107634. https://doi.org/10.1016/j.celrep.2020.107634.
Mulder WJM, Ochando J, Joosten LAB, Fayad ZA, Netea MG. Therapeutic targeting of trained immunity. Nat Rev Drug Discov. 2019;18(7):553–66. https://doi.org/10.1038/s41573-019-0025-4.
Netea MG, Domínguez-Andrés J, Barreiro LB, Chavakis T, Divangahi M, Fuchs E, et al. Defining trained immunity and its role in health and disease. Nat Rev Immunol. 2020;20(6):375–88. https://doi.org/10.1038/s41577-020-0285-6.
Philippini RR, Martiniano SE, dos Santos JC, da Silva SS, Chandel AK. Fermentative production of beta-glucan: properties and potential applications. In: Molina G, Gupta V, Singh B, Gathergood N, editors. Bioprocessing for biomolecules production. Chichester: Wiley; 2019. p. 303–20. https://doi.org/10.1002/9781119434436.ch15.
Qi J, Qi J, Yin Y, Yu W, Shen L, Xu J, Hu T. Conjugation of β-glucan with the hydrazone and disulfide linkers markedly improves the immunogenicity of Zika virus e protein. Mol Pharm. 2020;17(6):1933–44. https://doi.org/10.1021/acs.molpharmaceut.0c00010.
Rémy V, Largeron N, Quilici S, Carroll S. The economic value of vaccination: why prevention is wealth. J Mark Access Health Policy. 2015;3(1):29284. https://doi.org/10.3402/jmahp.v3.29284.
Reynolds JA, Kastello MD, Harrington DG, Crabbs CL, Peters CJ, Jemski JV, et al. Glucan-induced enhancement of host resistance to selected infectious diseases. Infect Immun. 1980;30(1):51–7. https://doi.org/10.1128/iai.30.1.51-57.1980.
Ruiz-Herrera J, Ortiz-Castellanos L. Cell wall glucans of fungi. A review. Cell Surface. Elsevier. 2019;5:100022. https://doi.org/10.1016/j.tcsw.2019.100022.
Sánchez-Ramón S, Conejero L, Netea MG, Sancho D, Palomares Ó, Subiza JL. Trained immunity-based vaccines: a new paradigm for the development of broad-spectrum anti-infectious formulations. Front Immunol. Frontiers. 2018;9:2936. https://doi.org/10.3389/fimmu.2018.02936.
Schmitz F, Heit A, Dreher S, Eisenächer K, Mages J, Haas T, et al. Mammalian target of rapamycin (mTOR) orchestrates the defense program of innate immune cells. Eur J Immunol. 2008;38(11):2981–92. https://doi.org/10.1002/eji.200838761.
Schött U, Kander T, Bentzer P. Effects of dextran-70 and albumin on coagulation in experimental hemorrhage in the Guinea pig. Shock. 2018;50(3):366–72. https://doi.org/10.1097/SHK.0000000000001025.
Serezani CH, Kane S, Collins L, Morato-Marques M, Osterholzer JJ, Peters-Golden M. Macrophage Dectin-1 expression is controlled by leukotriene B4 via a GM-CSF/PU.1 axis. J Immunol. 2012;189(2):906–15. https://doi.org/10.4049/jimmunol.1200257.
Sivakamavalli J, Selvaraj C, Singh SK, Park K, Kwak IS, Vaseeharan B. Effect of amino acid substitution in the Penaeus monodon LGBP and specificity through mutational analysis. Int J Pept Res Ther. 2019:1–13. https://doi.org/10.1007/s10989-019-09960-x.
Soares E, Cordeiro R, Faneca H, Borges O. Polymeric nanoengineered HBsAg DNA vaccine designed in combination with β-glucan. Int J Biol Macromol. 2019a;122:930–9. https://doi.org/10.1016/j.ijbiomac.2018.11.024.
Soares E, Groothuismink ZMA, Boonstra A, Borges O. Glucan particles are a powerful adjuvant for the HBsAg, favoring antiviral immunity. Mol Pharm. 2019b;16(5):1971–81. https://doi.org/10.1021/acs.molpharmaceut.8b01322.
Son S, Nam J, Zenkov I, Ochyl LJ, Xu Y, Scheetz L, et al. Sugar-nanocapsules imprinted with microbial molecular patterns for mRNA vaccination. Nano Lett. 2020;20(3):1499–509. https://doi.org/10.1021/acs.nanolett.9b03483.
Soto ER, Kim HC, Yagita H, De Jesus M, Ostroff GR. Polydopamine coating of glucan particles increases uptake into Peyer’s patches. ACS Appl Bio Mater. 2019;2(9):3748–54. https://doi.org/10.1021/acsabm.9b00379.
Strasser D, Neumann K, Bergmann H, Marakalala MJ, Guler R, Rojowska A, et al. Syk kinase-coupled C-type lectin receptors engage protein kinase C-δ to elicit card9 adaptor-mediated innate immunity. Immunity. 2012;36(1):32–42. https://doi.org/10.1016/J.IMMUNI.2011.11.015.
Sun B, Yu S, Zhao D, Guo S, Wang X, Zhao K. Polysaccharides as vaccine adjuvants; 2018. https://doi.org/10.1016/j.vaccine.2018.07.040.
Tchobanian A, Van Oosterwyck H, Fardim P. Polysaccharides for tissue engineering: current landscape and future prospects. Carbohydr Polym. 2019;205:601–25. https://doi.org/10.1016/j.carbpol.2018.10.039.
Tone K, Stappers MHT, Willment JA, Brown GD. C-type lectin receptors of the Dectin-1 cluster: physiological roles and involvement in disease. Eur J Immunol. Wiley. 2019;49(12):2127–33. https://doi.org/10.1002/eji.201847536.
Tong X, Qi X, Mao R, Pan W, Zhang M, Wu X, et al. Construction of functional curdlan hydrogels with bio-inspired polydopamine for synergistic periodontal antibacterial therapeutics. Carbohydr Polym. 2020;245:116585. https://doi.org/10.1016/j.carbpol.2020.116585.
Venkatachalam G, Arumugam S, Doble M. Industrial production and applications of α/β linear and branched glucans. Indian Chem Eng. 2020a:1–15. https://doi.org/10.1080/00194506.2020.1798820.
Venkatachalam G, Arumugam S, Doble M. Synthesis, characterization, and biological activity of aminated zymosan. ACS Omega. 2020b;5(26):15973–82. https://doi.org/10.1021/acsomega.0c01243.
Vetvicka V, Vannucci L, Sima P, Richter J. Beta glucan: supplement or drug? From laboratory to clinical trials. Molecules. 2019;24(7):1251. https://doi.org/10.3390/molecules24071251.
Vetvicka V, Vannucci L, Sima P. β-glucan as a new tool in vaccine development. Scand J Immunol. Wiley. 2020;91(2):e12833. https://doi.org/10.1111/sji.12833.
Wagener M, Hoving JC, Ndlovu H, Marakalala MJ. Dectin-1-Syk-CARD9 signaling pathway in TB immunity. Front Immunol. 2018;9:225. https://doi.org/10.3389/fimmu.2018.00225.
Wang W, Song X, Wang L, Song L. Pathogen-derived carbohydrate recognition in molluscs immune defense. Int J Mol Sci. Multidisciplinary Digital Publishing Institute. 2018;19(3):721. https://doi.org/10.3390/ijms19030721.
Weis WI, Drickamer K. Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem. 1996;65:441–73. https://doi.org/10.1146/annurev.bi.65.070196.002301.
Xu L, Zhang J. Bacterial glucans: production, properties, and applications. Appl Microbiol Biotechnol. 2016;100(21):9023–36. https://doi.org/10.1007/s00253-016-7836-6.
Yan JK, Cai WD, Wang C, Yu YB, Zhang HN, Yang Y, Wang WH. Macromolecular behavior, structural characteristics and rheological properties of alkali-neutralization curdlan at different concentrations. Food Hydrocoll. 2020;105:105785. https://doi.org/10.1016/j.foodhyd.2020.105785.
Yuan H, Lan P, He Y, Li C, Ma X. Effect of the modifications on the physicochemical and biological properties of β-glucan-a critical review. Molecules. Multidisciplinary Digital Publishing Institute. 2020;25(1):57. https://doi.org/10.3390/molecules25010057.
Żelechowska P, Różalska S, Wiktorska M, Brzezińska-Błaszczyk E, Agier J. Curdlan stimulates tissue mast cells to synthesize pro-inflammatory mediators, generate ROS, and migrate via Dectin-1 receptor. Cell Immunol. 2020;351:104079. https://doi.org/10.1016/J.CELLIMM.2020.104079.
Zhang Y, Kong H, Fang Y, Nishinari K, Phillips GO. Schizophyllan: a review on its structure, properties, bioactivities and recent developments. Bioact Carbohydr Diet Fibre. 2013;1(1):53–71. https://doi.org/10.1016/j.bcdf.2013.01.002.
Zhu F, Du B, Xu B. A critical review on production and industrial applications of beta-glucans. Food Hydrocoll. Elsevier. 2016;52:275–88. https://doi.org/10.1016/j.foodhyd.2015.07.003.
Zielke C, Lu Y, Poinsot R, Nilsson L. Interaction between cereal β-glucan and proteins in solution and at interfaces. Colloids Surf B: Biointerfaces. 2018;162:256–64. https://doi.org/10.1016/j.colsurfb.2017.11.059.
Zielke C, Lu Y, Nilsson L. Aggregation and microstructure of cereal β-glucan and its association with other biomolecules. Colloids Surf A Physicochem Eng Asp. 2019;560:402–9. https://doi.org/10.1016/j.colsurfa.2018.10.042.
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Tischer, C.A. (2022). Glucans. In: Oliveira, J.M., Radhouani, H., Reis, R.L. (eds) Polysaccharides of Microbial Origin. Springer, Cham. https://doi.org/10.1007/978-3-030-42215-8_2
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