Show legend Show as text

Structure type: structural motif or average structure
Aglycon: ID 45022 (core)
Compound class: N-mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_474450,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7120
  Murciano C, Moyes DL, Runglall M, Islam A, Mille C, Fradin C, Poulain D, Gow NA, Naglik JR "Candida albicans cell wall glycosylation may be indirectly required for activation of epithelial cell proinflammatory responses" - Infection and Immunity 79(12) (2011) 4902-4911
  

  Oral epithelial cells discriminate between the yeast and hyphal forms of Candida albicans via the mitogen-activated protein kinase (MAPK) signaling pathway. This occurs through phosphorylation of the MAPK phosphatase MKP1 and activation of the c-Fos transcription factor by the hyphal form. Given that fungal cell wall polysaccharides are critical in host recognition and immune activation in myeloid cells, we sought to determine whether β-glucan and N- or O-glycosylation was important in activating the MAPK/MKP1/c-Fos hypha-mediated response mechanism and proinflammatory cytokines in oral epithelial cells. Using a series of β-glucan and N- and O-mannan mutants, we found that N-mannosylation (via Δoch1 and Δpmr1 mutants) and O-mannosylation (via Δpmt1 and Δmnt1 Δmnt2 mutants), but not phosphomannan (via a Δmnn4 mutant) or β-1,2 mannosylation (via Δbmt1 to Δbmt6 mutants), were required for MKP1/c-Fos activation, proinflammatory cytokine production, and cell damage induction. However, the N- and O-mannan mutants showed reduced adhesion or lack of initial hypha formation at 2 h, resulting in little MKP1/c-Fos activation, or restricted hypha formation/pseudohyphal formation at 24 h, resulting in minimal proinflammatory cytokine production and cell damage. Further, the α-1,6-mannose backbone of the N-linked outer chain (corresponding to a Δmnn9 mutant) may be required for epithelial adhesion, while the α-1,2-mannose component of phospholipomannan (corresponding to a Δmit1 mutant) may contribute to epithelial cell damage. β-Glucan appeared to play no role in adhesion, epithelial activation, or cell damage. In summary, N- and O-mannosylation defects affect the ability of C. albicans to induce proinflammatory cytokines and damage in oral epithelial cells, but this may be due to indirect effects on fungal pathogenicity rather than mannose residues being direct activators of the MAPK/MKP1/c-Fos hypha-mediated immune response.

  cell wall, glycosylation

  NCBI PubMed ID: 21930756
  Publication DOI: 10.1128/IAI.05591-11
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: julian.naglik@kcl.ac.uk
  Institutions: Department of Oral Immunology, King’s College London Dental Institute, King’s College London, London, UK, Department of Molecular and Cell Biology, Institute of Medical Sciences, Foresterhill, University of Aberdeen, Aberdeen, UK, INSERM U, Pôle Recherche, Lille, France
  Methods: Western blotting, cytokine assay, cell growth, adherence assay, differential interference contrast microscopy, cell damage assay
  
   
  
  Candida albicans SC5314
  CSDB ID 45023 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: ID 45022 (core)
Compound class: N-mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_474450,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7120
  Murciano C, Moyes DL, Runglall M, Islam A, Mille C, Fradin C, Poulain D, Gow NA, Naglik JR "Candida albicans cell wall glycosylation may be indirectly required for activation of epithelial cell proinflammatory responses" - Infection and Immunity 79(12) (2011) 4902-4911
  

  Oral epithelial cells discriminate between the yeast and hyphal forms of Candida albicans via the mitogen-activated protein kinase (MAPK) signaling pathway. This occurs through phosphorylation of the MAPK phosphatase MKP1 and activation of the c-Fos transcription factor by the hyphal form. Given that fungal cell wall polysaccharides are critical in host recognition and immune activation in myeloid cells, we sought to determine whether β-glucan and N- or O-glycosylation was important in activating the MAPK/MKP1/c-Fos hypha-mediated response mechanism and proinflammatory cytokines in oral epithelial cells. Using a series of β-glucan and N- and O-mannan mutants, we found that N-mannosylation (via Δoch1 and Δpmr1 mutants) and O-mannosylation (via Δpmt1 and Δmnt1 Δmnt2 mutants), but not phosphomannan (via a Δmnn4 mutant) or β-1,2 mannosylation (via Δbmt1 to Δbmt6 mutants), were required for MKP1/c-Fos activation, proinflammatory cytokine production, and cell damage induction. However, the N- and O-mannan mutants showed reduced adhesion or lack of initial hypha formation at 2 h, resulting in little MKP1/c-Fos activation, or restricted hypha formation/pseudohyphal formation at 24 h, resulting in minimal proinflammatory cytokine production and cell damage. Further, the α-1,6-mannose backbone of the N-linked outer chain (corresponding to a Δmnn9 mutant) may be required for epithelial adhesion, while the α-1,2-mannose component of phospholipomannan (corresponding to a Δmit1 mutant) may contribute to epithelial cell damage. β-Glucan appeared to play no role in adhesion, epithelial activation, or cell damage. In summary, N- and O-mannosylation defects affect the ability of C. albicans to induce proinflammatory cytokines and damage in oral epithelial cells, but this may be due to indirect effects on fungal pathogenicity rather than mannose residues being direct activators of the MAPK/MKP1/c-Fos hypha-mediated immune response.

  cell wall, glycosylation

  NCBI PubMed ID: 21930756
  Publication DOI: 10.1128/IAI.05591-11
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: julian.naglik@kcl.ac.uk
  Institutions: Department of Oral Immunology, King’s College London Dental Institute, King’s College London, London, UK, Department of Molecular and Cell Biology, Institute of Medical Sciences, Foresterhill, University of Aberdeen, Aberdeen, UK, INSERM U, Pôle Recherche, Lille, France
  Methods: Western blotting, cytokine assay, cell growth, adherence assay, differential interference contrast microscopy, cell damage assay
  
   
  
  Candida albicans CA14 (Δbmt2 mutant)
  CSDB ID 42298 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: ID 45022 (core)
Compound class: N-mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_474450,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7120
  Murciano C, Moyes DL, Runglall M, Islam A, Mille C, Fradin C, Poulain D, Gow NA, Naglik JR "Candida albicans cell wall glycosylation may be indirectly required for activation of epithelial cell proinflammatory responses" - Infection and Immunity 79(12) (2011) 4902-4911
  

  Oral epithelial cells discriminate between the yeast and hyphal forms of Candida albicans via the mitogen-activated protein kinase (MAPK) signaling pathway. This occurs through phosphorylation of the MAPK phosphatase MKP1 and activation of the c-Fos transcription factor by the hyphal form. Given that fungal cell wall polysaccharides are critical in host recognition and immune activation in myeloid cells, we sought to determine whether β-glucan and N- or O-glycosylation was important in activating the MAPK/MKP1/c-Fos hypha-mediated response mechanism and proinflammatory cytokines in oral epithelial cells. Using a series of β-glucan and N- and O-mannan mutants, we found that N-mannosylation (via Δoch1 and Δpmr1 mutants) and O-mannosylation (via Δpmt1 and Δmnt1 Δmnt2 mutants), but not phosphomannan (via a Δmnn4 mutant) or β-1,2 mannosylation (via Δbmt1 to Δbmt6 mutants), were required for MKP1/c-Fos activation, proinflammatory cytokine production, and cell damage induction. However, the N- and O-mannan mutants showed reduced adhesion or lack of initial hypha formation at 2 h, resulting in little MKP1/c-Fos activation, or restricted hypha formation/pseudohyphal formation at 24 h, resulting in minimal proinflammatory cytokine production and cell damage. Further, the α-1,6-mannose backbone of the N-linked outer chain (corresponding to a Δmnn9 mutant) may be required for epithelial adhesion, while the α-1,2-mannose component of phospholipomannan (corresponding to a Δmit1 mutant) may contribute to epithelial cell damage. β-Glucan appeared to play no role in adhesion, epithelial activation, or cell damage. In summary, N- and O-mannosylation defects affect the ability of C. albicans to induce proinflammatory cytokines and damage in oral epithelial cells, but this may be due to indirect effects on fungal pathogenicity rather than mannose residues being direct activators of the MAPK/MKP1/c-Fos hypha-mediated immune response.

  cell wall, glycosylation

  NCBI PubMed ID: 21930756
  Publication DOI: 10.1128/IAI.05591-11
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: julian.naglik@kcl.ac.uk
  Institutions: Department of Oral Immunology, King’s College London Dental Institute, King’s College London, London, UK, Department of Molecular and Cell Biology, Institute of Medical Sciences, Foresterhill, University of Aberdeen, Aberdeen, UK, INSERM U, Pôle Recherche, Lille, France
  Methods: Western blotting, cytokine assay, cell growth, adherence assay, differential interference contrast microscopy, cell damage assay
  
   
  
  Candida albicans CA14 (Δbmt4 mutant)
  CSDB ID 45026 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: ID 45022 (core)
Compound class: N-mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7120
  Murciano C, Moyes DL, Runglall M, Islam A, Mille C, Fradin C, Poulain D, Gow NA, Naglik JR "Candida albicans cell wall glycosylation may be indirectly required for activation of epithelial cell proinflammatory responses" - Infection and Immunity 79(12) (2011) 4902-4911
  

  Oral epithelial cells discriminate between the yeast and hyphal forms of Candida albicans via the mitogen-activated protein kinase (MAPK) signaling pathway. This occurs through phosphorylation of the MAPK phosphatase MKP1 and activation of the c-Fos transcription factor by the hyphal form. Given that fungal cell wall polysaccharides are critical in host recognition and immune activation in myeloid cells, we sought to determine whether β-glucan and N- or O-glycosylation was important in activating the MAPK/MKP1/c-Fos hypha-mediated response mechanism and proinflammatory cytokines in oral epithelial cells. Using a series of β-glucan and N- and O-mannan mutants, we found that N-mannosylation (via Δoch1 and Δpmr1 mutants) and O-mannosylation (via Δpmt1 and Δmnt1 Δmnt2 mutants), but not phosphomannan (via a Δmnn4 mutant) or β-1,2 mannosylation (via Δbmt1 to Δbmt6 mutants), were required for MKP1/c-Fos activation, proinflammatory cytokine production, and cell damage induction. However, the N- and O-mannan mutants showed reduced adhesion or lack of initial hypha formation at 2 h, resulting in little MKP1/c-Fos activation, or restricted hypha formation/pseudohyphal formation at 24 h, resulting in minimal proinflammatory cytokine production and cell damage. Further, the α-1,6-mannose backbone of the N-linked outer chain (corresponding to a Δmnn9 mutant) may be required for epithelial adhesion, while the α-1,2-mannose component of phospholipomannan (corresponding to a Δmit1 mutant) may contribute to epithelial cell damage. β-Glucan appeared to play no role in adhesion, epithelial activation, or cell damage. In summary, N- and O-mannosylation defects affect the ability of C. albicans to induce proinflammatory cytokines and damage in oral epithelial cells, but this may be due to indirect effects on fungal pathogenicity rather than mannose residues being direct activators of the MAPK/MKP1/c-Fos hypha-mediated immune response.

  cell wall, glycosylation

  NCBI PubMed ID: 21930756
  Publication DOI: 10.1128/IAI.05591-11
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: julian.naglik@kcl.ac.uk
  Institutions: Department of Oral Immunology, King’s College London Dental Institute, King’s College London, London, UK, Department of Molecular and Cell Biology, Institute of Medical Sciences, Foresterhill, University of Aberdeen, Aberdeen, UK, INSERM U, Pôle Recherche, Lille, France
  Methods: Western blotting, cytokine assay, cell growth, adherence assay, differential interference contrast microscopy, cell damage assay
  
   
  
  Candida albicans CA14 (Δmnn4 mutant)
  CSDB ID 42246 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; 23000
Trivial name: tramesan
Compound class: EPS, polysaccharide
Contained glycoepitopes: IEDB_115576,IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_135614,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141806,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144998,IEDB_146664,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_158538,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_241100,IEDB_241101,IEDB_76920,IEDB_76933,IEDB_858578,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77

• Article ID: 7476
  Scarpari M, Reverberi M, Parroni A, Scala V, Fanelli C, Pietricola C, Zjalic S, Maresca V, Tafuri A, Ricciardi MR, Licchetta R, Mirabilii S, Sveronis A, Cescutti P, Rizzo R "Tramesan, a novel polysaccharide from Trametes versicolor. Structural characterization and biological effects" - PLoS One 12 (2017) e0171412
  

  Mushrooms represent a formidable source of bioactive compounds. Some of these may be considered as biological response modifiers; these include compounds with a specific biological function: antibiotics (e.g. plectasin), immune system stimulator (e,g, lentinan), antitumor agents (e.g. krestin, PSK) and hypolipidemic agents (e.g. lovastatin) inter alia. In this study, we focused on the Chinese medicinal mushroom "yun zhi", Trametes versicolor, traditionally used for (cit.) "replenish essence and qi (vital energy)". Previous studies indicated the potential activity of extracts from culture filtrate of asexual mycelia of T. versicolor in controlling the growth and secondary metabolism (e.g. mycotoxins) of plant pathogenic fungi. The quest of active principles produced by T. versicolor, allowed us characterising an exo-polysaccharide released in its culture filtrate and naming it Tramesan. Herein we evaluate the biological activity of Tramesan in different organisms: plants, mammals and plant pathogenic fungi. We suggest that the bioactivity of Tramesan relies mostly on its ability to act as pro antioxidant molecule regardless the biological system on which it was applied.

  NCBI PubMed ID: 28829786
  Publication DOI: 10.1371/journal.pone.0171412
  Journal NLM ID: 101285081
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: massimo.reverberi@uniroma1.it
  Institutions: Sapienza University, Department of Environmental Biology, Rome, Italy, Research Unit for Plant Pathology, Council for Agricultural Research and Economics, Rome, Italy, Department of Ecology, Agronomy and Aquaculture, University of Zadar, Rome, Italy, Department of Clinical and Molecular Medicine, Hematology, ''Sant’Andrea'' University Hospital Sapienza, University of Rome, Rome, Italy, Department of the Life Sciences, University of Trieste, Trieste, Italy
  Methods: 13C NMR, 1H NMR, methylation, GLC-MS, ESI-MS, GLC, de-O-acetylation, reduction with NaBD4, triflic acid solvolysis, TOCSY, COSY, NOESY, HSQC, HP-SEC
  
   
  
  Trametes versicolor C
  CSDB ID 43024 (all data & tools)
• Article ID: 9149
  Scala V, Pietricola C, Farina V, Beccaccioli M, Zjalic S, Quaranta F, Fornara M, Zaccaria M, Momeni B, Reverberi M, Iori A "Tramesan elicits durum wheat defense against the septoria disease complex" - Biomolecules 10(4) (2020) ID 608
  

  The Septoria Leaf Blotch Complex (SLBC), caused by the two ascomycetes Zymoseptoria tritici and Parastagonospora nodorum, can reduce wheat global yearly yield by up to 50%. In the last decade, SLBC incidence has increased in Italy; notably, durum wheat has proven to be more susceptible than common wheat. Field fungicide treatment can efficiently control these pathogens, but it leads to the emergence of resistant strains and adversely affects human and animal health and the environment. Our previous studies indicated that active compounds produced by Trametes versicolor can restrict the growth of mycotoxigenic fungi and the biosynthesis of their secondary metabolites (e.g., mycotoxins). Specifically, we identified Tramesan: a 23 kDa α-heteropolysaccharide secreted by T. versicolor that acts as a pro-antioxidant molecule in animal cells, fungi, and plants. Foliar-spray of Tramesan (3.3 μM) on SLBC-susceptible durum wheat cultivars, before inoculation of causal agents of Stagonospora Nodorum Blotch (SNB) and Septoria Tritici Blotch (STB), significantly decreased disease incidence both in controlled conditions (SNB: -99%, STB: -75%) and field assays (SNB: -25%, STB: -30%). We conducted these tests were conducted under controlled conditions as well as in field. We showed that Tramesan increased the levels of jasmonic acid (JA), a plant defense-related hormone. Tramesan also increased the early expression (24 hours after inoculation - hai) of plant defense genes such as PR4 for SNB infected plants, and RBOH, PR1, and PR9 for STB infected plants. These results suggest that Tramesan protects wheat by eliciting plant defenses, since it has no direct fungicidal activity. In field experiments, the yield of durum wheat plants treated with Tramesan was similar to that of healthy untreated plots. These results encourage the use of Tramesan to protect durum wheat against SLBC.

  mushrooms, wheat, plant defense, Antioxidant, septoria disease complex, biostimulant

  NCBI PubMed ID: 32295231
  Publication DOI: 10.3390/biom10040608
  Journal NLM ID: 101596414
  Publisher: Basel, Switzerland: MDPI
  Correspondence: Scala V ; Pietricola C ; Farina V ; Beccaccioli M ; Zjalic S ; Quaranta F ; Fornara M ; Iori A ; Zaccaria M ; Momeni B ; Reverberi M
  Institutions: Consiglio per la Ricerca in Agricoltura e l'Analisi dell'Economia Agraria, Centro di Ricerca Difesa e Certificazione, Roma, Italy, Università Sapienza, Dip. Biologia Ambientale, Roma, Italy, Department of Ecology, Agronomy and Aquaculture, University of Zadar, Zadar, Croatia, Consiglio per la Ricerca in Agricoltura e l'Analisi dell'Economia Agraria, Centro di ricerca Ingegneria e Trasformazioni agroalimentari, Roma, Italy, Department of Biology, Boston College, Chestnut Hill, USA
  Methods: biological assays, HPLC, extraction, RT-PCR, cell growth, LC-MS/MS, gene expression, DNA extraction, centrifugation, filtration
  
   
  
  Trametes versicolor
  CSDB ID 50924 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; 23000
Trivial name: tramesan
Compound class: EPS, polysaccharide
Contained glycoepitopes: IEDB_115576,IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_140628,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144998,IEDB_146664,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_232584,IEDB_241100,IEDB_76920,IEDB_76933,IEDB_858578,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77

• Article ID: 7476
  Scarpari M, Reverberi M, Parroni A, Scala V, Fanelli C, Pietricola C, Zjalic S, Maresca V, Tafuri A, Ricciardi MR, Licchetta R, Mirabilii S, Sveronis A, Cescutti P, Rizzo R "Tramesan, a novel polysaccharide from Trametes versicolor. Structural characterization and biological effects" - PLoS One 12 (2017) e0171412
  

  Mushrooms represent a formidable source of bioactive compounds. Some of these may be considered as biological response modifiers; these include compounds with a specific biological function: antibiotics (e.g. plectasin), immune system stimulator (e,g, lentinan), antitumor agents (e.g. krestin, PSK) and hypolipidemic agents (e.g. lovastatin) inter alia. In this study, we focused on the Chinese medicinal mushroom "yun zhi", Trametes versicolor, traditionally used for (cit.) "replenish essence and qi (vital energy)". Previous studies indicated the potential activity of extracts from culture filtrate of asexual mycelia of T. versicolor in controlling the growth and secondary metabolism (e.g. mycotoxins) of plant pathogenic fungi. The quest of active principles produced by T. versicolor, allowed us characterising an exo-polysaccharide released in its culture filtrate and naming it Tramesan. Herein we evaluate the biological activity of Tramesan in different organisms: plants, mammals and plant pathogenic fungi. We suggest that the bioactivity of Tramesan relies mostly on its ability to act as pro antioxidant molecule regardless the biological system on which it was applied.

  NCBI PubMed ID: 28829786
  Publication DOI: 10.1371/journal.pone.0171412
  Journal NLM ID: 101285081
  Publisher: San Francisco, CA: Public Library of Science
  Correspondence: massimo.reverberi@uniroma1.it
  Institutions: Sapienza University, Department of Environmental Biology, Rome, Italy, Research Unit for Plant Pathology, Council for Agricultural Research and Economics, Rome, Italy, Department of Ecology, Agronomy and Aquaculture, University of Zadar, Rome, Italy, Department of Clinical and Molecular Medicine, Hematology, ''Sant’Andrea'' University Hospital Sapienza, University of Rome, Rome, Italy, Department of the Life Sciences, University of Trieste, Trieste, Italy
  Methods: 13C NMR, 1H NMR, methylation, GLC-MS, ESI-MS, GLC, de-O-acetylation, reduction with NaBD4, triflic acid solvolysis, TOCSY, COSY, NOESY, HSQC, HP-SEC
  
   
  
  Trametes versicolor C
  CSDB ID 43207 (all data & tools)
• Article ID: 9149
  Scala V, Pietricola C, Farina V, Beccaccioli M, Zjalic S, Quaranta F, Fornara M, Zaccaria M, Momeni B, Reverberi M, Iori A "Tramesan elicits durum wheat defense against the septoria disease complex" - Biomolecules 10(4) (2020) ID 608
  

  The Septoria Leaf Blotch Complex (SLBC), caused by the two ascomycetes Zymoseptoria tritici and Parastagonospora nodorum, can reduce wheat global yearly yield by up to 50%. In the last decade, SLBC incidence has increased in Italy; notably, durum wheat has proven to be more susceptible than common wheat. Field fungicide treatment can efficiently control these pathogens, but it leads to the emergence of resistant strains and adversely affects human and animal health and the environment. Our previous studies indicated that active compounds produced by Trametes versicolor can restrict the growth of mycotoxigenic fungi and the biosynthesis of their secondary metabolites (e.g., mycotoxins). Specifically, we identified Tramesan: a 23 kDa α-heteropolysaccharide secreted by T. versicolor that acts as a pro-antioxidant molecule in animal cells, fungi, and plants. Foliar-spray of Tramesan (3.3 μM) on SLBC-susceptible durum wheat cultivars, before inoculation of causal agents of Stagonospora Nodorum Blotch (SNB) and Septoria Tritici Blotch (STB), significantly decreased disease incidence both in controlled conditions (SNB: -99%, STB: -75%) and field assays (SNB: -25%, STB: -30%). We conducted these tests were conducted under controlled conditions as well as in field. We showed that Tramesan increased the levels of jasmonic acid (JA), a plant defense-related hormone. Tramesan also increased the early expression (24 hours after inoculation - hai) of plant defense genes such as PR4 for SNB infected plants, and RBOH, PR1, and PR9 for STB infected plants. These results suggest that Tramesan protects wheat by eliciting plant defenses, since it has no direct fungicidal activity. In field experiments, the yield of durum wheat plants treated with Tramesan was similar to that of healthy untreated plots. These results encourage the use of Tramesan to protect durum wheat against SLBC.

  mushrooms, wheat, plant defense, Antioxidant, septoria disease complex, biostimulant

  NCBI PubMed ID: 32295231
  Publication DOI: 10.3390/biom10040608
  Journal NLM ID: 101596414
  Publisher: Basel, Switzerland: MDPI
  Correspondence: Scala V ; Pietricola C ; Farina V ; Beccaccioli M ; Zjalic S ; Quaranta F ; Fornara M ; Iori A ; Zaccaria M ; Momeni B ; Reverberi M
  Institutions: Consiglio per la Ricerca in Agricoltura e l'Analisi dell'Economia Agraria, Centro di Ricerca Difesa e Certificazione, Roma, Italy, Università Sapienza, Dip. Biologia Ambientale, Roma, Italy, Department of Ecology, Agronomy and Aquaculture, University of Zadar, Zadar, Croatia, Consiglio per la Ricerca in Agricoltura e l'Analisi dell'Economia Agraria, Centro di ricerca Ingegneria e Trasformazioni agroalimentari, Roma, Italy, Department of Biology, Boston College, Chestnut Hill, USA
  Methods: biological assays, HPLC, extraction, RT-PCR, cell growth, LC-MS/MS, gene expression, DNA extraction, centrifugation, filtration
  
   
  
  Trametes versicolor
  CSDB ID 50925 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: (->4)ID 45771-peptide
Compound class: glycopeptide, mannan
Contained glycoepitopes: IEDB_130701,IEDB_133966,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_144995,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73

• Article ID: 7654
  Shibata N, Kobayashi H, Suzuki S "Immunochemistry of pathogenic yeast, Candida species, focusing on mannan" - Proceedings of the Japan Academy. Series B, Physical and Biological Sciences 88(6) (2012) 250-265
  

  This review describes recent findings based on structural and immunochemical analyses of the cell wall mannan of Candida albicans, and other medically important Candida species. Mannan has been shown to consist of α-1,2-, α-1,3-, α-1,6-, and β-1,2-linked mannopyranose units with few phosphate groups. Each Candida species has a unique mannan structure biosynthesized by sequential collaboration between species-specific mannosyltransferases. In particular, the β-1,2-linked mannose units have been shown to comprise a characteristic oligomannosyl side chain that is strongly antigenic. For these pathogenic Candida species, cell-surface mannan was also found to participate in the adhesion to the epithelial cells, recognition by innate immune receptors and development of pathogenicity. Therefore, clarification of the precise chemical structure of Candida mannan is indispensable for understanding the mechanism of pathogenicity, and for development of new antifungal drugs and immunotherapeutic procedures.

  pathogenicity, mannan, 1H NMR, Candida, Mannosyltransferase, Dectin-2

  NCBI PubMed ID: 22728440
  Publication DOI: 10.2183/pjab.88.250
  Journal NLM ID: 9318162
  Publisher: Japan Academy
  Correspondence: suzusige@seagreen.ocn.ne.jp
  Institutions: Sendai Research Institute for Mycology, Miyagi, Japan, Department of Infection and Host Defense, Tohoku Pharmaceutical University, Miyagi, Japan, Department of Microbiology, Nagasaki International University, Nagasaki, Japan, Tohoku Pharmaceutical University, Miyagi, Japan
  
   
  
  Candida guilliermondii
  CSDB ID 45768 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: (->4)ID 45997-protein
Compound class: N-glycan, mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_474450,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73

• Article ID: 7665
  Takahara K, Arita T, Tokieda S, Shibata N, Okawa Y, Tateno H, Hirabayashi J, Inaba K "Difference in fine specificity to polysaccharides of Candida albicans mannoprotein between mouse SIGNR1 and human DC-SIGN" - Infection and Immunity 80(5) (2012) 1699-1706
  

  C-type lectin SIGNR1 directly recognizes Candida albicans and zymosan and has been considered to share properties of polysaccharide recognition with human DC-SIGN (hDC-SIGN). However, the precise specificity of SIGNR1 and the difference from that of hDC-SIGN remain to be elucidated. We prepared soluble forms of SIGNR1 and hDC-SIGN and conducted experiments to examine their respective specificities. Soluble SIGNR1 (sSIGNR1) bound several types of live C. albicans clinical isolate strains in an EDTA-sensitive manner. Inhibition analyses of sSIGNR1 binding by glycans from various yeast strains demonstrated that SIGNR1 preferentially recognizes N-glycan α-mannose side chains in Candida mannoproteins, as reported in hDC-SIGN. Unlike shDC-SIGN, however, sSIGNR1 recognized not only Saccharomyces cerevisiae, but also C. albicans J-1012 glycan, even after α-mannosidase treatment that leaves only β1,2-mannose-capped α-mannose side chains. In addition, glycomicroarray analyses showed that sSIGNR1 binds mannans from C. albicans and S. cerevisiae but does not recognize Lewis(a/b/x/y) antigen polysaccharides as in shDC-SIGN. Consistent with these results, RAW264.7 cells expressing hDC-SIGN in which the carbohydrate recognition domain (CRD) was replaced with that of SIGNR1 (RAW-chimera) produced comparable amounts of interleukin 10 (IL-10) in response to glycans from C. albicans and S. cerevisiae, but those expressing hDC-SIGN produced less IL-10 in response to S. cerevisiae than C. albicans. Furthermore, RAW-hDC-SIGN cells remarkably reduced IL-10 production after α-mannosidase treatment compared with RAW-chimera cells. These results indicate that SIGNR1 recognizes C. albicans/yeast through a specificity partly distinct from that of its homologue hDC-SIGN.

  lectin, Candida albicans, DC-SIGN, mannoprotein

  NCBI PubMed ID: 22331432
  Publication DOI: 10.1128/IAI.06308-11
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: Inaba K
  Institutions: Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan, CREST, Kyoto University, Kyoto, Japan, Department of Infection and Host Defense, Tohoku Pharmaceutical University, Komatsushima, Japan, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), AIST Tsukuba Central Umezono, Ibaraki, Japan
  Methods: DNA techniques, ELISA, biological assays, enzymatic digestion, extraction, cell growth, Fehling treatment
  
   
  
  Candida albicans A J-1012
  CSDB ID 45846 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: (->4)ID 45997-protein
Compound class: N-glycan, mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7665
  Takahara K, Arita T, Tokieda S, Shibata N, Okawa Y, Tateno H, Hirabayashi J, Inaba K "Difference in fine specificity to polysaccharides of Candida albicans mannoprotein between mouse SIGNR1 and human DC-SIGN" - Infection and Immunity 80(5) (2012) 1699-1706
  

  C-type lectin SIGNR1 directly recognizes Candida albicans and zymosan and has been considered to share properties of polysaccharide recognition with human DC-SIGN (hDC-SIGN). However, the precise specificity of SIGNR1 and the difference from that of hDC-SIGN remain to be elucidated. We prepared soluble forms of SIGNR1 and hDC-SIGN and conducted experiments to examine their respective specificities. Soluble SIGNR1 (sSIGNR1) bound several types of live C. albicans clinical isolate strains in an EDTA-sensitive manner. Inhibition analyses of sSIGNR1 binding by glycans from various yeast strains demonstrated that SIGNR1 preferentially recognizes N-glycan α-mannose side chains in Candida mannoproteins, as reported in hDC-SIGN. Unlike shDC-SIGN, however, sSIGNR1 recognized not only Saccharomyces cerevisiae, but also C. albicans J-1012 glycan, even after α-mannosidase treatment that leaves only β1,2-mannose-capped α-mannose side chains. In addition, glycomicroarray analyses showed that sSIGNR1 binds mannans from C. albicans and S. cerevisiae but does not recognize Lewis(a/b/x/y) antigen polysaccharides as in shDC-SIGN. Consistent with these results, RAW264.7 cells expressing hDC-SIGN in which the carbohydrate recognition domain (CRD) was replaced with that of SIGNR1 (RAW-chimera) produced comparable amounts of interleukin 10 (IL-10) in response to glycans from C. albicans and S. cerevisiae, but those expressing hDC-SIGN produced less IL-10 in response to S. cerevisiae than C. albicans. Furthermore, RAW-hDC-SIGN cells remarkably reduced IL-10 production after α-mannosidase treatment compared with RAW-chimera cells. These results indicate that SIGNR1 recognizes C. albicans/yeast through a specificity partly distinct from that of its homologue hDC-SIGN.

  lectin, Candida albicans, DC-SIGN, mannoprotein

  NCBI PubMed ID: 22331432
  Publication DOI: 10.1128/IAI.06308-11
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: Inaba K
  Institutions: Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan, CREST, Kyoto University, Kyoto, Japan, Department of Infection and Host Defense, Tohoku Pharmaceutical University, Komatsushima, Japan, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), AIST Tsukuba Central Umezono, Ibaraki, Japan
  Methods: DNA techniques, ELISA, biological assays, enzymatic digestion, extraction, cell growth, Fehling treatment
  
   
  
  Candida albicans A J-1012
  CSDB ID 45847 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Aglycon: Man8GlcNAc2 inner core-xLAsn
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_143632,IEDB_144983,IEDB_144995,IEDB_146674,IEDB_152206,IEDB_153220,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_173895,IEDB_174840,IEDB_76920,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73

• Article ID: 7829
  Kohatsu L, Hsu DK, Jegalian AG, Liu FT, Baum LG "Galectin-3 induces death of Candida species expressing specific β-1,2-linked mannans" - Journal of Immunology 177(7) (2006) 4718-4726
  

  Lectins play a critical role in host protection against infection. The galectin family of lectins recognizes saccharide ligands on a variety of microbial pathogens, including viruses, bacteria, and parasites. Galectin-3, a galectin expressed by macrophages, dendritic cells, and epithelial cells, binds bacterial and parasitic pathogens including Leishmania major, Trypanosoma cruzi, and Neisseria gonorrhoeae. However, there have been no reports of galectins having direct effects on microbial viability. We found that galectin-3 bound only to Candida albicans species that bear β-1,2-linked oligomannans on the cell surface, but did not bind Saccharomyces cerevisiae that lacks β-1,2-linked oligomannans. Surprisingly, binding directly induced death of Candida species containing specific β-1,2-linked oligomannosides. Thus, galectin-3 can act as a pattern recognition receptor that recognizes a unique pathogen-specific oligosaccharide sequence. This is the first description of antimicrobial activity for a member of the galectin family of mammalian lectins; unlike other lectins of the innate immune system that promote opsonization and phagocytosis, galectin-3 has direct fungicidal activity against opportunistic fungal pathogens.

  galectin, Mannans

  NCBI PubMed ID: 16982911
  Publication DOI: 10.4049/jimmunol.177.7.4718
  Journal NLM ID: 2985117R
  Publisher: Bethesda, MD: American Association of Immunologists
  Correspondence: Baum LG
  Institutions: Department of Pathology and Laboratory Medicine, Jonsson Comprehensive Cancer Center, School of Medicine, University of California, Los Angeles, USA, Department of Dermatology, School of Medicine, University of California Davis, Sacramento, USA
  Methods: cell growth, flow cytometry, biological assay
  
   
  
  Candida albicans A ATCC 10231, Candida albicans B ATCC 60193, Candida glabrata ATCC 2001, Saccharomyces cerevisiae BY4741a
  CSDB ID 45536 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->4) Asn (protein)
Trivial name: N-glycan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_429156,IEDB_474450,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857734,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77

• Article ID: 7879
  Fradin C, Bernardes ES, Jouault T "Candida albicans phospholipomannan: a sweet spot for controlling host response/inflammation" - Seminars in Immunopathology 37(2) (2015) 123-30
  

  Fungal cell walls contain several types of glycans, which play important roles in the pathogenesis of fungal infection and host immune response. Among them, glycosphingolipids have attracted much attention lately since they contribute actively to the fungi development and fungal-induced pathogenesis. Although glycosphingolipids are present in pathogenic and non-pathogenic fungi, pathogenic strains exhibit distinct glycan structures on their sphingolipids, which contribute to the regulatory processes engaged in inflammatory response. In Candida albicans, phospholipomannan (PLM) represents a prototype of these sphingolipids. Through its glycan and lipid moieties, PLM induces activation of host signaling pathways involved in the initial recognition of fungi, causing immune system disorder and persistent fungal disease. In this review, first we describe the general aspects of C. albicans sphingolipids synthesis with a special emphasize on PLM synthesis and its insertion into the cell wall. Then, we discuss the role of PLM glycosylation in regulating immune system activation and its contribution to the chronic persistent inflammation found in Candida infections and chronic inflammatory diseases.

  regulation, glycosphingolipids, yeasts, inflammatory response

  NCBI PubMed ID: 25394861
  Publication DOI: 10.1007/s00281-014-0461-5
  Journal NLM ID: 101308769
  Publisher: Berlin: Springer
  Correspondence: Jouault T
  Institutions: INSERM U995, Lille, France, Université de Lille, Lille, France, Institute of Energy and Nuclear Research (IPEN), São Paulo, Brazil, Faculté de Médecine H.Warembourg, Pôle Recherche, Lille, France, Institute of Energy and Nuclear Research IPEN, São Paulo, Brazil, Faculté de Médecine H. Warembourg, Pôle Recherche, Lille, France
  
   
  
  Candida albicans
  CSDB ID 46383 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->4) Asn (protein)
Trivial name: N-glycan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_429156,IEDB_474450,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857734,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77

• Article ID: 7879
  Fradin C, Bernardes ES, Jouault T "Candida albicans phospholipomannan: a sweet spot for controlling host response/inflammation" - Seminars in Immunopathology 37(2) (2015) 123-30
  

  Fungal cell walls contain several types of glycans, which play important roles in the pathogenesis of fungal infection and host immune response. Among them, glycosphingolipids have attracted much attention lately since they contribute actively to the fungi development and fungal-induced pathogenesis. Although glycosphingolipids are present in pathogenic and non-pathogenic fungi, pathogenic strains exhibit distinct glycan structures on their sphingolipids, which contribute to the regulatory processes engaged in inflammatory response. In Candida albicans, phospholipomannan (PLM) represents a prototype of these sphingolipids. Through its glycan and lipid moieties, PLM induces activation of host signaling pathways involved in the initial recognition of fungi, causing immune system disorder and persistent fungal disease. In this review, first we describe the general aspects of C. albicans sphingolipids synthesis with a special emphasize on PLM synthesis and its insertion into the cell wall. Then, we discuss the role of PLM glycosylation in regulating immune system activation and its contribution to the chronic persistent inflammation found in Candida infections and chronic inflammatory diseases.

  regulation, glycosphingolipids, yeasts, inflammatory response

  NCBI PubMed ID: 25394861
  Publication DOI: 10.1007/s00281-014-0461-5
  Journal NLM ID: 101308769
  Publisher: Berlin: Springer
  Correspondence: Jouault T
  Institutions: INSERM U995, Lille, France, Université de Lille, Lille, France, Institute of Energy and Nuclear Research (IPEN), São Paulo, Brazil, Faculté de Médecine H.Warembourg, Pôle Recherche, Lille, France, Institute of Energy and Nuclear Research IPEN, São Paulo, Brazil, Faculté de Médecine H. Warembourg, Pôle Recherche, Lille, France
  
   
  
  Candida albicans
  CSDB ID 46384 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->4) Asn (protein)
Trivial name: N-glycan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_429156,IEDB_474450,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857734,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77

• Article ID: 7879
  Fradin C, Bernardes ES, Jouault T "Candida albicans phospholipomannan: a sweet spot for controlling host response/inflammation" - Seminars in Immunopathology 37(2) (2015) 123-30
  

  Fungal cell walls contain several types of glycans, which play important roles in the pathogenesis of fungal infection and host immune response. Among them, glycosphingolipids have attracted much attention lately since they contribute actively to the fungi development and fungal-induced pathogenesis. Although glycosphingolipids are present in pathogenic and non-pathogenic fungi, pathogenic strains exhibit distinct glycan structures on their sphingolipids, which contribute to the regulatory processes engaged in inflammatory response. In Candida albicans, phospholipomannan (PLM) represents a prototype of these sphingolipids. Through its glycan and lipid moieties, PLM induces activation of host signaling pathways involved in the initial recognition of fungi, causing immune system disorder and persistent fungal disease. In this review, first we describe the general aspects of C. albicans sphingolipids synthesis with a special emphasize on PLM synthesis and its insertion into the cell wall. Then, we discuss the role of PLM glycosylation in regulating immune system activation and its contribution to the chronic persistent inflammation found in Candida infections and chronic inflammatory diseases.

  regulation, glycosphingolipids, yeasts, inflammatory response

  NCBI PubMed ID: 25394861
  Publication DOI: 10.1007/s00281-014-0461-5
  Journal NLM ID: 101308769
  Publisher: Berlin: Springer
  Correspondence: Jouault T
  Institutions: INSERM U995, Lille, France, Université de Lille, Lille, France, Institute of Energy and Nuclear Research (IPEN), São Paulo, Brazil, Faculté de Médecine H.Warembourg, Pôle Recherche, Lille, France, Institute of Energy and Nuclear Research IPEN, São Paulo, Brazil, Faculté de Médecine H. Warembourg, Pôle Recherche, Lille, France
  
   
  
  Candida albicans
  CSDB ID 46385 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->4) Asn (protein)
Trivial name: N-glycan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_174840,IEDB_429156,IEDB_474450,IEDB_76920,IEDB_76933,IEDB_857732,IEDB_857734,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77

• Article ID: 7879
  Fradin C, Bernardes ES, Jouault T "Candida albicans phospholipomannan: a sweet spot for controlling host response/inflammation" - Seminars in Immunopathology 37(2) (2015) 123-30
  

  Fungal cell walls contain several types of glycans, which play important roles in the pathogenesis of fungal infection and host immune response. Among them, glycosphingolipids have attracted much attention lately since they contribute actively to the fungi development and fungal-induced pathogenesis. Although glycosphingolipids are present in pathogenic and non-pathogenic fungi, pathogenic strains exhibit distinct glycan structures on their sphingolipids, which contribute to the regulatory processes engaged in inflammatory response. In Candida albicans, phospholipomannan (PLM) represents a prototype of these sphingolipids. Through its glycan and lipid moieties, PLM induces activation of host signaling pathways involved in the initial recognition of fungi, causing immune system disorder and persistent fungal disease. In this review, first we describe the general aspects of C. albicans sphingolipids synthesis with a special emphasize on PLM synthesis and its insertion into the cell wall. Then, we discuss the role of PLM glycosylation in regulating immune system activation and its contribution to the chronic persistent inflammation found in Candida infections and chronic inflammatory diseases.

  regulation, glycosphingolipids, yeasts, inflammatory response

  NCBI PubMed ID: 25394861
  Publication DOI: 10.1007/s00281-014-0461-5
  Journal NLM ID: 101308769
  Publisher: Berlin: Springer
  Correspondence: Jouault T
  Institutions: INSERM U995, Lille, France, Université de Lille, Lille, France, Institute of Energy and Nuclear Research (IPEN), São Paulo, Brazil, Faculté de Médecine H.Warembourg, Pôle Recherche, Lille, France, Institute of Energy and Nuclear Research IPEN, São Paulo, Brazil, Faculté de Médecine H. Warembourg, Pôle Recherche, Lille, France
  
   
  
  Candida albicans
  CSDB ID 46386 (all data & tools)

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Structure type: oligomer
Aglycon: (->4) Asn (protein)
Trivial name: N-glycan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,IEDB_134621,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144996,IEDB_146674,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_429156,IEDB_474450,IEDB_76933,IEDB_857732,IEDB_857734,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77

• Article ID: 7879
  Fradin C, Bernardes ES, Jouault T "Candida albicans phospholipomannan: a sweet spot for controlling host response/inflammation" - Seminars in Immunopathology 37(2) (2015) 123-30
  

  Fungal cell walls contain several types of glycans, which play important roles in the pathogenesis of fungal infection and host immune response. Among them, glycosphingolipids have attracted much attention lately since they contribute actively to the fungi development and fungal-induced pathogenesis. Although glycosphingolipids are present in pathogenic and non-pathogenic fungi, pathogenic strains exhibit distinct glycan structures on their sphingolipids, which contribute to the regulatory processes engaged in inflammatory response. In Candida albicans, phospholipomannan (PLM) represents a prototype of these sphingolipids. Through its glycan and lipid moieties, PLM induces activation of host signaling pathways involved in the initial recognition of fungi, causing immune system disorder and persistent fungal disease. In this review, first we describe the general aspects of C. albicans sphingolipids synthesis with a special emphasize on PLM synthesis and its insertion into the cell wall. Then, we discuss the role of PLM glycosylation in regulating immune system activation and its contribution to the chronic persistent inflammation found in Candida infections and chronic inflammatory diseases.

  regulation, glycosphingolipids, yeasts, inflammatory response

  NCBI PubMed ID: 25394861
  Publication DOI: 10.1007/s00281-014-0461-5
  Journal NLM ID: 101308769
  Publisher: Berlin: Springer
  Correspondence: Jouault T
  Institutions: INSERM U995, Lille, France, Université de Lille, Lille, France, Institute of Energy and Nuclear Research (IPEN), São Paulo, Brazil, Faculté de Médecine H.Warembourg, Pôle Recherche, Lille, France, Institute of Energy and Nuclear Research IPEN, São Paulo, Brazil, Faculté de Médecine H. Warembourg, Pôle Recherche, Lille, France
  
   
  
  Candida albicans
  CSDB ID 46387 (all data & tools)