Abstract
Chitin and chitosan are two related polysaccharides that provide important structural stability to fungal cell walls. Often embedded deeply within the cell wall structure, these molecules anchor other components at the cell surface. Chitin-directed organization of the cell wall layers allows the fungal cell to effectively monitor and interact with the external environment. For fungal pathogens, this interaction includes maintaining cellular strategies to avoid excessive detection by the host innate immune system. In turn, mammalian and plant hosts have developed their own strategies to process fungal chitin, resulting in chitin fragments of varying molecular size. The size-dependent differences in the immune activation behaviors of variably sized chitin molecules help to explain how chitin and related chitooligomers can both inhibit and activate host immunity. Moreover, chitin and chitosan have recently been exploited for many biomedical applications, including targeted drug delivery and vaccine development.
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References
Amnuaykanjanasin A, Epstein L (2003) A class V chitin synthase gene, chsA is essential for conidial and hyphal wall strength in the fungus Colletotrichum graminicola (Glomerella graminicola). Fungal Genet Biol 38(3):272–285. https://doi.org/10.1016/S1087-1845(02)00563-7
Aranaz I, Mengíbar M, Harris R, Paños I, Miralles B, Acosta N, Galed G, Heras Á (2009) Functional characterization of chitin and chitosan. Curr Chem Biol 3
Arellano M, Cartagena-Lirola H, Nasser Hajibagheri MA, Duran A, Henar Valdivieso M (2000) Proper ascospore maturation requires the chs1+ chitin synthase gene in Schizosaccharomyces pombe. Mol Microbiol 35(1):79–89. https://doi.org/10.1046/j.1365-2958.2000.01678.x
Baker LG, Specht CA, Donlin MJ, Lodge JK (2007) Chitosan, the deacetylated form of chitin, is necessary for cell wall integrity in Cryptococcus neoformans. Eukaryot Cell 6(5):855–867. https://doi.org/10.1128/EC.00399-06
Baker LG, Specht CA, Lodge JK (2011) Cell wall chitosan is necessary for virulence in the opportunistic pathogen Cryptococcus neoformans. Eukaryot Cell 10(9):1264–1268. https://doi.org/10.1128/EC.05138-11
Banks I, Specht C, Donlin M, Gerik K, Levitz S, Lodge J (2005) A chitin synthase and its regulator protein are critical for chitosan production and growth of the fungal pathogen Cryptococcus neoformans. Eukaryot Cell 4(11):1902–1912. https://doi.org/10.1128/EC.4.11.1902
Beauvais A, Schmidt C, Guadagnini S, Roux P, Perret E, Henry C, Latgé JP (2007) An extracellular matrix glues together the aerial-grown hyphae of Aspergillus fumigatus. Cell Microbiol 9(6):1588–1600. https://doi.org/10.1111/j.1462-5822.2007.00895.x
Bierbaum S, Superti-Furga A, Heinzmann A (2006) Genetic polymorphisms of chitotriosidase in Caucasian children with bronchial asthma. Int J Immunogenet 33(3):201–204. https://doi.org/10.1111/j.1744-313X.2006.00597.x
Bierbaum S, Nickel R, Koch A, Lau S, Deichmann KA, Wahn U, Superti-Furga A, Heinzmann A (2005) Polymorphisms and haplotypes of acid mammalian chitinase are associated with bronchial asthma. https://doi.org/10.1164/rccm.200506-890OC
Boot RG, Blommaart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Aerts JM (2001) Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem 276(9):6770–6778. https://doi.org/10.1074/jbc.M009886200
Boot Rolf G, Bussink AP, Verhoek M, De Boer PAJ, Moorman AFM, Aerts JMFG (2005) Marked differences in tissue-specific expression of chitinases in mouse and man. J Histochem Cytochem 53(10):1283–1292. https://doi.org/10.1369/jhc.4A6547.2005
Bowen AR, Chen-Wu JL, Momany M, Young R, Szaniszlo PJ, Robbins PW (1992) Classification of fungal chitin synthases. Proc Natl Acad Sci USA 89(2):519–523. https://doi.org/10.1073/pnas.89.2.519
Bowman SM, Free SJ (2006) The structure and synthesis of the fungal cell wall. BioEssays: News Rev Mol Cell Dev Biol 28(8):799–808. https://doi.org/10.1002/bies.20441
Bowman SM, Piwowar A, El M, Dabbous A, Vierula J, Free SJ (2006) Mutational analysis of the Glycosylphosphatidylinositol (GPI) anchor pathway demonstrates that GPI-anchored proteins are required for cell wall biogenesis and normal hyphal growth in Neurospora crassa. Eukaryot Cell 5(3):587–600. https://doi.org/10.1128/EC.5.3.587-600.2006
Brown HE, Ost KS, Esher SK, Pianalto KM, Saelens JW, Guan Z, Alspaugh JA (2018) Identifying a novel connection between the fungal plasma membrane and pH-sensing. Mol Microbiol. https://doi.org/10.1111/mmi.13998
Brown JA, Catley BJ (1992) Monitoring polysaccharide synthesis in Candida albicans. Carbohyd Res 227:195–202. https://doi.org/10.1016/0008-6215(92)85071-7
Bueter CL, Lee CK, Rathinam VAK, Healy GJ, Taron CH, Specht CA, Levitz SM (2011) Chitosan but not chitin activates the inflammasome by a mechanism dependent upon phagocytosis. J Biol Chem 286(41):35447–35455. https://doi.org/10.1074/jbc.M111.274936
Bueter CL, Lee CK, Wang JP, Ostroff GR, Specht CA, Levitz SM (2014) Spectrum and mechanisms of inflammasome activation by chitosan. J Immunol (Baltimore, Md. : 1950), 192(12):5943–5951. https://doi.org/10.4049/jimmunol.1301695
Bulawa CE, Miller DW, Henry LK, Becker JM (1995) Attenuated virulence of chitin-deficient mutants of Candida albicans. Proc Natl Acad Sci USA 92(23):10570–10574. https://doi.org/10.1073/pnas.92.23.10570
Bulik DA, Olczak M, Lucero HA, Osmond BC, Robbins PW, Specht CA (2003) Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress. Eukaryot Cell 2(5):886–900. https://doi.org/10.1128/EC.2.5.886-900.2003
Cabib E, Silverman SJ, Shaw Ja (1992) Chitinase and chitin synthase 1: counterbalancing activities in cell separation of Saccharomyces cerevisiae. J Gen Microbiol 138(1):97–102. https://doi.org/10.1099/00221287-138-1-97
Cash HL, Whitham CV, Behrendt CL, Hooper LV (2006) Symbiotic bacteria direct expression of an intestinal bactericidal lectin. Science (New York, N.Y.) 313(5790):1126–1130. https://doi.org/10.1126/science.1127119
Chai LYA, Vonk AG, Kullberg BJ, Verweij PE, Verschueren I, van der Meer JWM, Netea MG (2011) Aspergillus fumigatus cell wall components differentially modulate host TLR2 and TLR4 responses. Microbes Infect 13(2):151–159. https://doi.org/10.1016/j.micinf.2010.10.005
Choi E, Zimmerman P, Foster C, Zhu S, Kumaraswami V, Nutman T, Chanock S (2001) Genetic polymorphisms in molecules of innate immunity and susceptibility to infection with Wuchereria bancrofti in South India. Genes Immun 2(5):248–253. https://doi.org/10.1038/sj.gene.6363767
Chuang JS, Schekman RW (1996) Differential trafficking and timed localization of two chitin synthase proteins, Chs2p and Chs3p. J Cell Biol 135(3):597–610. https://doi.org/10.1083/jcb.135.3.597
Curto M-Á, Sharifmoghadam MR, Calpena E, De León N, Hoya M, Doncel C, Valdivieso M-H (2014) Membrane organization and cell fusion during mating in fission yeast requires multipass membrane protein Prm1. Genetics 196(4):1059–1076. https://doi.org/10.1534/genetics.113.159558
Da Silva CA, Chalouni C, Williams A, Hartl D, Lee CG, Elias JA (2009) Chitin is a size-dependent regulator of macrophage TNF and IL-10 production. J Immunol 182(6):3573–3582. https://doi.org/10.4049/jimmunol.0802113
Da Silva CA, Hartl D, Liu W, Lee CG, Elias JA (2008) TLR-2 and IL-17A in chitin-induced macrophage activation and acute inflammation. J Immunol 181(6):4279–4286. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2577310&tool=pmcentrez&rendertype=abstract
DeMarini DJ, Adams AEM, Fares H, De Virgilio C, Valle G, Chuang JS, Pringle JR (1997) A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall. J Cell Biol 139(1):75–93. https://doi.org/10.1083/jcb.139.1.75
Elias JA, Homer RJ, Hamid Q, Lee CG (2005) Chitinases and chitinase-like proteins in TH2 inflammation and asthma. J Allergy Clin Immunol 116(3):497–500. https://doi.org/10.1016/J.JACI.2005.06.028
Esher SK, Ost KS, Kohlbrenner MA, Pianalto KM, Telzrow CL, Campuzano A, Alspaugh JA (2018) Defects in intracellular trafficking of fungal cell wall synthases lead to aberrant host immune recognition. PLoS Pathog 14(6):e1007126. https://doi.org/10.1371/journal.ppat.1007126
Fischer R, Zekert N, Takeshita N (2008) Polarized growth in fungi—interplay between the cytoskeleton, positional markers and membrane domains. Mol Microbiol 68(4):813–826. https://doi.org/10.1111/j.1365-2958.2008.06193.x
Fontaine T, Delangle A, Simenel C, Coddeville B, van Vliet SJ, van Kooyk Y, Latgé J-P (2011) Galactosaminogalactan, a new immunosuppressive polysaccharide of Aspergillus fumigatus. PLoS Pathog 7(11):e1002372. https://doi.org/10.1371/journal.ppat.1002372
Fortwendel JR, Juvvadi PR, Pinchai N, Perfect BZ, Alspaugh JA, Perfect JR, Steinbach WJ (2009) Differential effects of inhibiting chitin and 1,3-{beta}-D-glucan synthesis in ras and calcineurin mutants of Aspergillus fumigatus. Antimicrob Agents Chemother 53(2):476–482. https://doi.org/10.1128/AAC.01154-08
Free SJ (2013) Fungal cell wall organization and biosynthesis. Adv Genet 81:33–82. https://doi.org/10.1016/B978-0-12-407677-8.00002-6
Gastebois A, Clavaud C, Aimanianda V, Latgé JP (2009) Aspergillus fumigatus: cell wall polysaccharides, their biosynthesis and organization. Future Microbiol 4:583–595. https://doi.org/10.2217/fmb.09.29
Gharieb MM, Sabha, El-Sabbagh M, Shalaby MA, Darwesh OM (2015) Production of chitosan from different species of zygomycetes and its antimicrobial activity. Int J Sci Eng Res 6(4). Retrieved from http://www.ijser.org
Gholizadeh Aghdam M (2010) Title: extraction of chitosan from fungal cell wall by sulfuric acid-studying the effect of deacetylation degree and temperature on recovery chitosan author. Retrieved from http://www.diva-portal.org/smash/get/diva2:1312010/FULLTEXT01.pdf
Gonçalves IR, Brouillet S, Soulié MC, Gribaldo S, Sirven C, Charron N, Choquer M (2016) Genome-wide analyses of chitin synthases identify horizontal gene transfers towards bacteria and allow a robust and unifying classification into fungi. BMC Evol Biol 16(1):1–17. https://doi.org/10.1186/s12862-016-0815-9
Gorzelanny C, Pöppelmann B, Pappelbaum K, Moerschbacher BM, Schneider SW (2010) Human macrophage activation triggered by chitotriosidase-mediated chitin and chitosan degradation. Biomaterials 31(33):8556–8563. https://doi.org/10.1016/j.biomaterials.2010.07.100
Gottlieb S, Altboum Z, Savage D, Segal E (1991) Adhesion of Candida albicans to epithelial cells effect of polyoxin D. Mycopathologia 115(3):197–205. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1749403
Gow NAR, Latge J-P, Munro CA (2017). The fungal cell wall: structure, biosynthesis, and function. Microbiol Spectr 5(3). https://doi.org/10.1128/microbiolspec.funk-0035-2016
He X, Li K, Xing R, Liu S, Hu L, Li P (2016) The production of fully deacetylated chitosan by compression method. Egypt J Aquat Res 42(1):75–81. https://doi.org/10.1016/j.ejar.2015.09.003
Hollak CE, van Weely S, van Oers MH, Aerts JM (1994) Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease. J Clin Invest 93(3):1288–1292. https://doi.org/10.1172/JCI117084
Huang C, Nong S, Mansour MK, Specht CA, Levitz SM (2002) Purification and characterization of a second immunoreactive mannoprotein from Cryptococcus neoformans that stimulates T-cell responses. Infect Immun 70(10):5485–5493. https://doi.org/10.1128/IAI.70.10.5485-5493.2002
Ifuku S, Nogi M, Abe K, Yoshioka M, Morimoto M, Saimoto H, Yano H (2009) Preparation of Chitin nanofibers with a uniform width as α-chitin from crab shells. Biomacromol 10(6):1584–1588. https://doi.org/10.1021/bm900163d
Ifuku S, Nomura R, Morimoto M, Saimoto H (2011) Preparation of chitin nanofibers from mushrooms. Materials 4(8):1417–1425. https://doi.org/10.3390/ma4081417
Ike M, Isami K, Tanabe Y, Nogawa M, Ogasawara W, Okada H, Morikawa Y (2006) Cloning and heterologous expression of the exo-β-D-glucosaminidase-encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-7. Appl Microbiol Biotechnol 72(4):687–695. https://doi.org/10.1007/s00253-006-0320-y
Jach G, Görnhardt B, Mundy J, Logemann J, Pinsdorf E, Leah R., … Maas, C. (1995). Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J: Cell Mol Biol 8(1):97–109. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/7655510
Jiang D, Liang J, Fan J, Yu S, Chen S, Luo Y, Noble PW (2005) Regulation of lung injury and repair by toll-like receptors and hyaluronan. Nat Med 11(11):1173–1179. https://doi.org/10.1038/nm1315
Klis FM, Boorsma A, De Groot PWJ (2006) Cell wall construction in Saccharomyces cerevisiae. Yeast 23(3):185–202. https://doi.org/10.1002/yea.1349
Koller B, Müller-Wiefel AS, Rupec R, Korting HC, Ruzicka T (2011) Chitin modulates innate immune responses of keratinocytes. PLoS ONE 6(2):e16594. https://doi.org/10.1371/journal.pone.0016594
Korolenko TA, Zhanaeva SY, Falameeva OV, Kaledin VI, Filyushina EE, Buzueva II, Paul GA (2000) Chitotriosidase as a marker of macrophage stimulation. Bull Exp Biol Med 130(4):948–950. https://doi.org/10.1007/BF02682034
Kzhyshkowska J, Gratchev A, Goerdt S (2007) Human chitinases and chitinase-like proteins as indicators for inflammation and cancer. Biomarker Insights 2:128–146. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/19662198
Latgé JP, Calderone R (2005) The fungal cell wall. In: Kües U, Fischer R (eds) The mycota I. Growth, differentiation and sexuality. Springer-Verlag, pp 79–104
Latgé JP (2007) The cell wall: a carbohydrate armour for the fungal cell. Mol Microbiol 66:279–290. https://doi.org/10.1111/j.1365-2958.2007.05872.x
Lenardon MD, Munro CA, Gow NAR (2010) Chitin synthesis and fungal pathogenesis. Curr Opin Microbiol 13(4):416–423. https://doi.org/10.1016/j.mib.2010.05.002
Lesage G, Bussey H (2006) Cell wall assembly in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 70(2):317–343. https://doi.org/10.1128/mmbr.00038-05
Li S, Chen L, Wang C, Xia W (2008) Expression, purification and characterization of endo-type chitosanase of Aspergillus sp. CJ22-326 from Escherichia coli. Carbohydr Res 343(17):3001–3004. https://doi.org/10.1016/j.carres.2008.08.032
Liu R, Xu C, Zhang Q, Wang S, Fang W (2017) Evolution of the chitin synthase gene family correlates with fungal morphogenesis and adaption to ecological niches. Sci Rep 7. https://doi.org/10.1038/srep44527
Lopez-Romero E, Ruiz-Herrera J (1986) The role of chitin in fungal growth and morphogenesis. In: Chitin in nature and technology, pp 55–62. https://doi.org/10.1007/978-1-4613-2167-5_8
Loussert C, Schmitt C, Prevost M-C, Balloy V, Fadel E, Philippe B, Beauvais A (2010) In vivo biofilm composition of Aspergillus fumigatus. Cell Microbiol 12(3):405–410. https://doi.org/10.1111/j.1462-5822.2009.01409.x
Maddi A, Free SJ (2010) α-1,6-mannosylation of N-linked oligosaccharide present on cell wall proteins is required for their incorporation into the cell wall in the filamentous fungus Neurospora crassa. Eukaryot Cell 9(11):1766–1775. https://doi.org/10.1128/EC.00134-10
Magnelli PE, Cipollo JF, Robbins PW (2005) A glucanase-driven fractionation allows redefinition of Schizosaccharomyces pombe cell wall composition and structure: assignment of diglucan. Anal Biochem 336(2):202–212. https://doi.org/10.1016/j.ab.2004.09.022
Malaguarnera L, Musumeci M, Di Rosa M, Scuto A, Musumeci S (2005) Interferon-gamma, tumor necrosis factor-alpha, and lipopolysaccharide promote chitotriosidase gene expression in human macrophages. J Clin Lab Anal 19(3):128–132. https://doi.org/10.1002/jcla.20063
Martínez-Rucobo FW, Eckhardt-Strelau L, Terwisscha van Scheltinga AC (2009) Yeast chitin synthase 2 activity is modulated by proteolysis and phosphorylation. Biochem J 417(2):547–554. https://doi.org/10.1042/BJ20081475
Matsuo Y, Tanaka K, Nakagawa T, Matsuda H, Kawamukai M (2004) Genetic analysis of chs1+ and chs2+ encoding chitin synthases from Schizosaccharomyces pombe. Biosci Biotechnol Biochem 68(7):1489–1499. https://doi.org/10.1271/bbb.68.1489
McNeela EA, Jabbal-Gill I, Illum L, Pizza M, Rappuoli R, Podda A, Mills KHG (2004) Intranasal immunization with genetically detoxified diphtheria toxin induces T cell responses in humans: enhancement of Th2 responses and toxin-neutralizing antibodies by formulation with chitosan. Vaccine 22(8):909–914. https://doi.org/10.1016/j.vaccine.2003.09.012
Mélida H, Sain D, Stajich JE, Bulone V (2015) Deciphering the uniqueness of Mucoromycotina cell walls by combining biochemical and phylogenomic approaches. Environ Microbiol 17(5):1649–1662. https://doi.org/10.1111/1462-2920.12601
Mellado E, Aufauvre-Brown A, Gow NAR, Holden DW (1996) The Aspergillus fumigatus chsC and chsG genes encode Class III chitin synthases with different functions. Mol Microbiol 20(3):667–679. https://doi.org/10.1046/j.1365-2958.1996.5571084.x
Minke R, Blackwell J (1978) The structure of α-chitin. J Mol Biol 120(2):167–181. https://doi.org/10.1016/0022-2836(78)90063-3
Mora-Montes HM, Netea MG, Ferwerda G, Lenardon MD, Brown GD, Mistry AR, Gow NAR (2011) Recognition and blocking of innate immunity cells by Candida albicans chitin. Infect Immun 79(5):1961–1970. https://doi.org/10.1128/IAI.01282-10
Munro CA, Gow NAR (1995). Chitin biosynthesis as a target for antifungals. In: Dixon GK, Copping LG, Hollomon DW (eds) Antifungal agents: discovery and mode of action. Bios Scientific, Oxford, pp 161–171
Munro CA, Gow NAR (2001) Chitin synthesis in human pathogenic fungi. Medical Mycol Suppl 39:41–53. https://doi.org/10.1080/mmy.39.1.41.53
Munro CA, Winter K, Buchan A, Henry K, Becker JM, Brown AJ, Bulawa CE, Gow NA (2001) Chs1 of Candida albicans is an essential chitin synthase required for synthesis of the septum and for cell integrity. Mol Microbiol 39(5):1414–1426. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/11251855
Munro CA, Winter K, Buchan A, Henry K, Becker JM, Brown AJP, Gow NAR (2001b) Chs1 of Candida albicans is an essential chitin synthase required for synthesis of the septum and for cell integrity. Mol Microbiol 39(5):1414–1426. https://doi.org/10.1046/j.1365-2958.2001.02347.x
Munro CA, Winter K, Buchan A, Henry K, Becker JM, Brown AJP, Gow NAR (2004) Chs1 of Candida albicans is an essential chitin synthase required for synthesis of the septum and for cell integrity. Mol Microbiol 39(5):1414–1426. https://doi.org/10.1046/j.1365-2958.2001.02347.x
Mushi NE, Butchosa N, Salajkova M, Zhou Q, Berglund LA (2014) Nanostructured membranes based on native chitin nanofibers prepared by mild process. Carbohyd Polym 112:255–263. https://doi.org/10.1016/j.carbpol.2014.05.038
Muszkieta L, Aimanianda V, Mellado E, Gribaldo S, Alcàzar-Fuoli L, Szewczyk E, Latgé JP (2014) Deciphering the role of the chitin synthase families 1 and 2 in the in vivo and in vitro growth of Aspergillus fumigatus by multiple gene targeting deletion. Cell Microbiol 16(12):1784–1805. https://doi.org/10.1111/cmi.12326
Muszkieta L, Fontaine T, Beau R, Mouyna I, Vogt MS, Trow J, Cormack BP, Essen LO, Jouvion G, Latgé J-P (2019) The Glycosylphosphatidylinositol-anchored DFG family is essential for the insertion of galactomannan into the β-(1,3)-glucan–chitin core of the cell wall of Aspergillus fumigatus. https://doi.org/10.1128/mSphere.00397-19
Muzzarelli RA (2010). Chitins and chitosans as immunoadjuvants and non-allergenic drug carriers. Mar Drugs 8(2):292–312. https://doi.org/10.3390/md8020292
Niño-vega GA, Carrero L, San-Blas G (2004) Isolation of the CHS4 gene of Paracoccidioides brasiliensis and its accommodation in a new class of chitin synthases. Med Mycol 42(1):51–57. https://doi.org/10.1080/1369378031000153811
Nishimura K, Ishihara C, Ukei S, Tokura S, Azuma I (1986a) Stimulation of cytokine production in mice using deacetylated chitin. Vaccine 4(3):151–156. https://doi.org/10.1016/0264-410X(86)90002-2
Nishimura K, Nishimura S-I, Seo H, Nishi N, Tokura S, Azuma I (1986b) Macrophage activation with multi-porous beads prepared from partially deacetylated chitin. J Biomed Mater Res 20(9):1359–1372. https://doi.org/10.1002/jbm.820200910
O’Meara TR, Holmer SM, Selvig K, Dietrich F, Alspaugh JA (2013) Cryptococcus neoformans Rim101 is associated with cell wall remodeling and evasion of the host immune responses. MBio 4(1). https://doi.org/10.1128/mBio.00522-12
O’Meara TR, Norton D, Price MS, Hay C, Clements MF, Nichols CB, Alspaugh JA (2010) Interaction of Cryptococcus neoformans Rim101 and protein kinase A regulates capsule. PLoS Pathog 6(2):e1000776. https://doi.org/10.1371/journal.ppat.1000776
Ost KS, Esher SK, Leopold Wager CM, Walker L, Wagener J, Munro C, Wormley FL, Alspaugh JA (2017) Rim pathway-mediated alterations in the fungal cell wall influence immune recognition and inflammation. MBio 8(1):e02290-16. https://doi.org/10.1128/mBio.02290-16
Overdijk B, Van Steijn GJ, Odds FC (1996) Chitinase levels in guinea pig blood are increased after systemic infection with Aspergillus fumigatus. Glycobiology 6(6):627–634. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/8922958
Ozdemir C, Yazi D, Aydogan M, Akkoc T, Bahceciler NN, Strong P, Barlan IB (2006) Treatment with chitin microparticles is protective against lung histopathology in a murine asthma model. Clin Exp Allergy 36(7):960–968. https://doi.org/10.1111/j.1365-2222.2006.02515.x
Perez-Garcia LA, Diaz-Jimenez DF, Lopez-Esparza A, Mora-Montes HM (2011) Role of cell wall polysaccharides during recognition of Candida albicans by the innate immune system. J Glycobiology 1(1). https://doi.org/10.4172/2168-958X.1000102
Pham T-H, Langmann S, Schwarzfischer L, El Chartouni C, Lichtinger M, Klug M, Rehli M (2007) CCAAT enhancer-binding protein beta regulates constitutive gene expression during late stages of monocyte to macrophage differentiation. J Biol Chem 282(30):21924–21933. https://doi.org/10.1074/jbc.M611618200
Pianalto KM, Billmyre RB, Telzrow CL, Alspaugh JA (2019) Roles for stress response and cell wall biosynthesis pathways in caspofungin tolerance in Cryptococcus neoformans. Genetics genetics.302290.2019. https://doi.org/10.1534/genetics.119.302290
Ramanathan M, Lee W-K, Lane AP (2006) Increased expression of acidic mammalian chitinase in chronic rhinosinusitis with nasal polyps. Am J Rhinol 20(3):330–335. https://doi.org/10.2500/ajr.2006.20.2869
Read RC, Naylor SC, Potter CW, Bond J, Jabbal-Gill I, Fisher A, Jennings R (2005) Effective nasal influenza vaccine delivery using chitosan. Vaccine 23(35):4367–4374. https://doi.org/10.1016/J.VACCINE.2005.04.021
Reese TA, Liang H, Tager AM, Luster AD, Van Rooijen N, Voehringer D, Locksley RM (2007) Chitin induces accumulation in tissue of innate immune cells associated with allergy. Nature 447(7140):92–96. https://doi.org/10.1038/nature05746
Renkema GH, Boot RG, Strijland A, Donker-Koopman WE, Berg M, Muijsers AO, Aerts JMFG (1997) Synthesis, sorting, and processing into distinct isoforms of human macrophage chitotriosidase. Eur J Biochem 244(2):279–285. https://doi.org/10.1111/j.1432-1033.1997.00279.x
Rieg N, Fonzi WA, Belanger PH, Fu Y, Rieg G, Fonzi WA, Filler SG (1998) Expression of the Candida albicans gene ALS1 in Saccharomyces cerevisiae induces adherence to endothelial and epithelial cells. Infect Immun 66(4):1783–1786
Rizzetto L, Ifrim DC, Moretti S, Tocci N, Cheng SC, Quintin J, Cavalieri D (2016) Fungal chitin induces trained immunity in human monocytes during cross-talk of the host with Saccharomyces cerevisiae. J Biol Chem 291(15):7961–7972. https://doi.org/10.1074/jbc.M115.699645
Rodrigues ML, Alvarez M, Fonseca FL, Casadevall A (2008) Binding of the wheat germ lectin to Cryptococcus neoformans suggests an association of chitinlike structures with yeast budding and capsular glucuronoxylomannan. Eukaryot Cell 7(4):602–609. https://doi.org/10.1128/EC.00307-07
Rodríguez-Martín A, Acosta R, Liddell S, Núñez F, Benito MJ, Asensio MA (2010) Characterization of the novel antifungal chitosanase PgChP and the encoding gene from Penicillium chrysogenum. Appl Microbiol Biotechnol 88(2):519–528. https://doi.org/10.1007/s00253-010-2767-0
Rogg LE, Fortwendel JR, Juvvadi PR, Lilley A, Steinbach WJ (2011) The chitin synthase genes chsA and chsC are not required for cell wall stress responses in the human pathogen Aspergillus fumigatus. Biochem Biophys Res Commun 411(3):549–554. https://doi.org/10.1016/j.bbrc.2011.06.180
Rogg LE, Fortwendel JR, Juvvadi PR, Steinbach WJ (2012) Regulation of expression, activity and localization of fungal chitin synthases. Med Mycol 50(1):2–17. https://doi.org/10.3109/13693786.2011.577104
Roncero C (2002) The genetic complexity of chitin synthesis in fungi. Curr Genet 41(6):367–378. https://doi.org/10.1007/s00294-002-0318-7
Ruiz-Herrera J, Ortiz-Castellanos L (2010) Analysis of the phylogenetic relationships and evolution of the cell walls from yeasts and fungi. FEMS Yeast Res 10:225–243. https://doi.org/10.1111/j.1567-1364.2009.00589.x
Sánchez-León E, Verdín J, Freitag M, Roberson RW, Bartnicki-Garcia S, Riquelme M (2011) Traffic of chitin synthase 1 (CHS-1) to the spitzenkörper and developing septa in hyphae of Neurospora crassa: actin dependence and evidence of distinct microvesicle populations. Eukaryot Cell 10(5):683–695. https://doi.org/10.1128/EC.00280-10
Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornøe I, Mollenhauer J, Holmskov U (2009) Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin. J Immunol 183(6):3800–3809. https://doi.org/10.4049/jimmunol.0901526
Schmidt CS, White CJ, Ibrahim AS, Filler SG, Fu Y, Yeaman MR, Hennessey JP (2012) NDV-3, a recombinant alum-adjuvanted vaccine for Candida and Staphylococcus aureus, is safe and immunogenic in healthy adults. Vaccine 30(52):7594–7600. https://doi.org/10.1016/j.vaccine.2012.10.038
Schuster M, Treitschke S, Kilaru S, Molloy J, Harmer NJ, Steinberg G (2012) Myosin-5, kinesin-1 and myosin-17 cooperate in secretion of fungal chitin synthase. EMBO J 31(1):214–227. https://doi.org/10.1038/emboj.2011.361
Seetharaman J, Kanigsberg A, Slaaby R, Leffler H, Barondes SH, Rini JM (1998) X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution. J Biol Chem 273(21):13047–13052. https://doi.org/10.1074/JBC.273.21.13047
Segal E, Gottfried L, Lehrer N (1988) Candidal vaginitis in hormone-treated mice: prevention by a chitin extract. Mycopathologia 102(3):157–163. https://doi.org/10.1007/BF00437398
Semenuk T, Krist P, Pavlícek J, Bezouska K, Kuzma M, Novák P, Kren V (2001) Synthesis of chitooligomer-based glycoconjugates and their binding to the rat natural killer cell activation receptor NKR-P1. Glycoconj J 18(10):817–826. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12441671
Shaw JA, Mol PC, Bowers B, Silverman SJ, Valdivieso MH, Durán A, Cabib E (1991) The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle. J Cell Biol 114(1):111–123. https://doi.org/10.1083/jcb.114.1.111
Sheetz MP, Singer SJ (1974) Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc Nat Acad Sci USA 71(11):4457–4461. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/4530994
Sheu YJ, Barral Y, Snyder M (2000) Polarized growth controls cell shape and bipolar bud site selection in Saccharomyces cerevisiae. Mol Cell Biol 20(14):5235–5247. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/10866679
Shibata Y, Foster LA, Metzger WJ, Myrvik QN (1997) Alveolar macrophage priming by intravenous administration of chitin particles, polymers of N-acetyl-d-glucosamine, in mice. Infect Immun 65(5):1734–1741. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/9125555
Shibata Y, Foster LA, Bradfield JF, Myrvik QN (2000) Oral administration of chitin down-regulates serum IgE levels and lung eosinophilia in the allergic mouse. J Immunology (Baltimore, Md. : 1950) 164(3):1314–1321
Shibata Y, Metzger WJ, Myrvik QN (1997) Chitin particle-induced cell-mediated immunity is inhibited by soluble mannan: mannose receptor-mediated phagocytosis initiates IL-12 production. J Immunol (Baltimore, Md. : 1950), 159(5):2462–2467. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/9278339
Shor E, Wang Y, Perlin DS, Xue C (2016) Cryptococcus flips its lid—membrane phospholipid asymmetry modulates antifungal drug resistance and virulence. Microbial Cell (Graz, Austria), 3(8):358–360. https://doi.org/10.15698/mic2016.08.521
Somashekar D, Joseph R (1996) Chitosanases—properties and applications: a review. Biores Technol 55(1):35–45. https://doi.org/10.1016/0960-8524(95)00144-1
Specht CA, Lee CK, Huang H, Hester MM, Liu J, Luckie BA, Levitz SM (2017). Vaccination with recombinant cryptococcus proteins in glucan particles protects mice against cryptococcosis in a manner dependent upon mouse strain and Cryptococcal species. MBio 8(6):e01872-17. https://doi.org/10.1128/MBIO.01872-17
Strong P, Clark H, Reid K (2002) Intranasal application of chitin microparticles down-regulates symptoms of allergic hypersensitivity to Dermatophagoides pteronyssinus and Aspergillus fumigatus in murine models of allergy. Clin Exp Allergy 32(12):1794–1800. https://doi.org/10.1046/j.1365-2222.2002.01551.x
Sudoh M, Yamazaki T, Masubuchi K, Taniguchi M, Shimma N, Arisawa M, Yamada-Okabe H (2000) Identification of a novel inhibitor specific to the fungal chitin synthase. Inhibition of chitin synthase 1 arrests the cell growth, but inhibition of chitin synthase 1 and 2 is lethal in the pathogenic fungus Candida albicans. J Biol Chem 275(42):32901–32905. https://doi.org/10.1074/jbc.M003634200
Sugiyama J, Boisset C, Hashimoto M, Watanabe T (1999) Molecular directionality of β-chitin biosynthesis. J Mol Biol 286(1):247–255. https://doi.org/10.1006/jmbi.1998.2458
Takeshita N, Ohta A, Horiuchi H (2005) CsmA, a class V chitin synthase with a myosin motor-like domain, is localized through direct interaction with the actin cytoskeleton in Aspergillus nidulans. Mol Biol Cell 16(4):1961–1970. https://doi.org/10.1091/mbc.E04-09-0761
Takeshita N, Wernet V, Tsuizaki M, Grün N, Hoshi HO, Ohta A, Fischer R, Horiuchi H (2015) Transportation of Aspergillus nidulans class III and V chitin synthases to the hyphal tips depends on conventional kinesin. PLoS ONE 10(5). https://doi.org/10.1371/journal.pone.0125937
Teh EM, Chai CC, Yeong FM (2009). Retention of Chs2p in the ER requires N-terminal CDK1-phosphorylation sites. Cell Cycle (Georgetown, Tex.) 8(18):2964–2974. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/19713768
Treitschke S, Doehlemann G, Schuster M, Steinberga G (2010) The myosin motor domain of fungal chitin synthase v is dispensable for vesicle motility but required for virulence of the maize pathogen Ustilago maydis. Plant Cell 22(7):2476–2494. https://doi.org/10.1105/tpc.110.075028
Upadhya R, Baker LG, Lam WC, Specht CA, Donlin MJ, Lodge JK (2018) Cryptococcus neoformans cda1 and its chitin deacetylase activity are required for fungal pathogenesis. MBio 9(6). https://doi.org/10.1128/mBio.02087-18
Valdivia RH, Baggott D, Chuang JS, Schekman RW (2002) The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins. Dev Cell 2(3):283–294. https://doi.org/10.1016/S1534-5807(02)00127-2
Valdivieso MH, Mol PC, Shaw JA, Cabib E, Duran A (1991) CAL1, a gene required for activity of chitin synthase 3 in Saccharomyces cerevisiae. J Cell Biol 114(1):101–109. https://doi.org/10.1083/jcb.114.1.101
Van Dyken SJ, Garcia D, Porter P, Huang X, Quinlan PJ, Blanc PD, Corry DB, Locksley RM (2011) Fungal chitin from asthma-associated home environments induces eosinophilic lung infiltration. J Immunol (Baltimore, Md. : 1950), 187(5):2261–2267. https://doi.org/10.4049/jimmunol.1100972
van Eijk M, van Roomen CPAA, Renkema GH, Bussink AP, Andrews L, Blommaart EFC, Aerts JMFG (2005) Characterization of human phagocyte-derived chitotriosidase, a component of innate immunity. Int Immunol 17(11):1505–1512. https://doi.org/10.1093/intimm/dxh328
van Meer G (2011) Dynamic transbilayer lipid asymmetry. Cold Spring Harb Perspect Biol 3(5):1–11. https://doi.org/10.1101/cshperspect.a004671
Vega K, Kalkum M (2012) Chitin, chitinase responses, and invasive fungal infections. Int J Microbiol 2012:920459. https://doi.org/10.1155/2012/920459
Vicencio AG, Narain S, Du Z, Zeng WY, Ritch J, Casadevall A, Goldman DL (2008) Pulmonary cryptococcosis induces chitinase in the rat. Respir Res 9(1):40. https://doi.org/10.1186/1465-9921-9-40
Wagener J, Malireddi RKS, Lenardon MD, Köberle M, Vautier S, MacCallum DM, Gow NAR (2014) Fungal chitin dampens inflammation through IL-10 induction mediated by NOD2 and TLR9 activation. PLoS Pathog 10(4):e1004050. https://doi.org/10.1371/journal.ppat.1004050
Walker LA, Munro CA, de Bruijn I, Lenardon MD, McKinnon A, Gow NAR (2008) Stimulation of chitin synthesis rescues Candida albicans from echinocandins. PLoS Pathog 4(4):e1000040. https://doi.org/10.1371/journal.ppat.1000040
Walton FJ, Idnurm A, Heitman J (2005) Novel gene functions required for melanization of the human pathogen Cryptococcus neoformans. Mol Microbiol 57(5):1381–1396. https://doi.org/10.1111/j.1365-2958.2005.04779.x
Warr GA (1980) A macrophage receptor for (mannose/glucosamine)-glycoproteins of potential importance in phagocytic activity. Biochem Biophys Res Commun 93(3):737–745. https://doi.org/10.1016/0006-291X(80)91139-0
Weber I, Aßmann D, Thines E, Steinberg G (2006) Polar localizing class V myosin chitin synthases are essential during early plant infection in the plant pathogenic fungus Ustilago maydis. Plant Cell 18(1):225–242. https://doi.org/10.1105/tpc.105.037341
Xu X-L, Lee RTH, Fang H-M, Wang Y-M, Li R, Zou H, Wang Y (2008) Bacterial peptidoglycan triggers Candida albicans hyphal growth by directly activating the adenylyl cyclase Cyr1p. Cell Host Microbe 4(1):28–39. https://doi.org/10.1016/j.chom.2008.05.014
Yen M-T, Yang J-H, Mau J-L (2009) Physicochemical characterization of chitin and chitosan from crab shells. Carbohyd Polym 75(1):15–21. https://doi.org/10.1016/j.carbpol.2008.06.006
Zhang Y-Z, Chen Q, Liu C-H, Liu Y-B, Yi P, Niu K-X, Zheng Y-L (2016) Chitin synthase gene FgCHS8 affects virulence and fungal cell wall sensitivity to environmental stress in Fusarium graminearum. Fungal Biol 120(5):764–774. https://doi.org/10.1016/j.funbio.2016.02.002
Zhu Z, Zheng T, Homer RJ, Kim Y-K, Chen NY, Cohn L, Hamid Q, Elias JA (2004) Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13 pathway activation. Science (New York, N.Y.), 304(5677):1678–1682. https://doi.org/10.1126/science.1095336
Ziman M, Chuang JS, Schekman RW (1996) Chs1p and Chs3p, two proteins involved in chitin synthesis, populate a compartment of the Saccharomyces cerevisiae endocytic pathway. Mol Biol Cell 7(12):1909–1919. https://doi.org/10.1091/mbc.7.12.1909
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Brown, H.E., Esher, S.K., Alspaugh, J.A. (2019). Chitin: A “Hidden Figure” in the Fungal Cell Wall. In: Latgé, JP. (eds) The Fungal Cell Wall . Current Topics in Microbiology and Immunology, vol 425. Springer, Cham. https://doi.org/10.1007/82_2019_184
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