Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_423153,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 5627
  Dembitsky VM, Rezanka T "Metabolites produced by nitrogen-fixing Nostoc species" - Folia Microbiologica 50(5) (2005) 363-391
  

  This paper provides a comprehensive overview of metabolites, including lipids and lipid-like compounds, boron-containing macrocycles, arsenolipids, oligopeptides and amino acid derivatives, produced by cyanobacteria of the genus Nostoc

  cyanobacteria, lipids, metabolites, Nostoc

  NCBI PubMed ID: 16475497
  Publication DOI: 10.1007/bf02931419
  Journal NLM ID: 0376757
  Publisher: New York: Springer
  Correspondence: rezanka@biomed.cas.cz
  Institutions: Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech, Department of Organic Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel
  
   
  
  Nostoc commune HB 261
  CSDB ID 47820 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_423153,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 5627
  Dembitsky VM, Rezanka T "Metabolites produced by nitrogen-fixing Nostoc species" - Folia Microbiologica 50(5) (2005) 363-391
  

  This paper provides a comprehensive overview of metabolites, including lipids and lipid-like compounds, boron-containing macrocycles, arsenolipids, oligopeptides and amino acid derivatives, produced by cyanobacteria of the genus Nostoc

  cyanobacteria, lipids, metabolites, Nostoc

  NCBI PubMed ID: 16475497
  Publication DOI: 10.1007/bf02931419
  Journal NLM ID: 0376757
  Publisher: New York: Springer
  Correspondence: rezanka@biomed.cas.cz
  Institutions: Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech, Department of Organic Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel
  
   
  
  Nostoc commune HB 261
  CSDB ID 47821 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: glucuronoxylomannan
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_115576,IEDB_130701,IEDB_1394182,IEDB_140116,IEDB_140630,IEDB_144983,IEDB_145668,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_2270799,IEDB_423153,IEDB_76933,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 6926
  Doering TL "A unique alpha-1,3 mannosyltransferase of the pathogenic fungus Cryptococcus neoformans" - Journal of Bacteriology 181 (1999) 5482-5488
  

  The major virulence factor of the pathogenic fungusCryptococcus neoformans is an extensive polysaccharide capsule which surrounds the cell. Almost 90% of the capsule is composed of a partially acetylated linear α-1,3-linked mannan substituted with D-xylose and D-glucuronic acid. A novel mannosyltransferase with specificity appropriate for a role in the synthesis of this glucuronoxylomannan is active in cryptococcal membranes. This membrane-associated activity transfers mannose in vitro from GDP-mannose to an α-1,3-dimannoside acceptor, forming a second α-1,3 linkage. Product formation by the transferase is dependent on protein, time, temperature, divalent cations, and each substrate. It is not affected by amphomycin or tunicamycin but is inhibited by GDP and mannose-1-phosphate. The described activity is not detectable in the model yeast Saccharomyces cerevisiae, consistent with the absence of a similar polysaccharide structure in that organism. A second mannosyltransferase from C. neoformans membranes adds mannose in α-1,2 linkage to the same dimannoside acceptor. The two activities differ in pH optimum and cation preference. While the α-1,2 transferase does not have specificity appropriate for a role in glucuronoxylomannan synthesis, it may participate in production of mannoprotein components of the capsule. This study suggests two new targets for antifungal drug discovery.

  Journal NLM ID: 2985120R
  WWW link: http://jb.asm.org/content/181/17/5482.long
  Publisher: American Society for Microbiology
  Correspondence: doering@borcim.wustl.edu
  Institutions: Department of Pharmacology, Cornell University Medical College, New York, New York
  Methods: enzymatic digestion, enzymatic assay, radiolabelling
  
   
  
  Cryptococcus neoformans B
  CSDB ID 40487 (all data & tools)

Show legend Show as text

Structure type: suggested polymer biological repeating unit
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_115576,IEDB_130701,IEDB_1394182,IEDB_140116,IEDB_140630,IEDB_144983,IEDB_145668,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_2270799,IEDB_423153,IEDB_76933,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 6961
  Bar-Peled M, Griffith CL, Doering TL "Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis" - Proceedings of the National Academy of Sciences of the USA 21 (2001) 12003-12008
  

  UDP-xylose is a sugar donor required for the synthesis of diverse and important glycan structures in animals, plants, fungi, and bacteria. Xylose-containing glycans are particularly abundant in plants and in the polysaccharide capsule that is the major virulence factor of the pathogenic fungus Cryptococcus neoformans. Biosynthesis of UDP-xylose is mediated by UDP-glucuronic acid decarboxylase, which converts UDP-glucuronic acid to UDP-xylose. Although this enzymatic activity was described over 40 years ago it has never been fully purified, and the gene encoding it has not been identified. We used homology to a bacterial gene, hypothesized to encode a related function, to identify a cryptococcal sequence as putatively encoding a UDP-glucuronic acid decarboxylase. A soluble 47-kDa protein derived from bacteria expressing the C. neoformans gene catalyzed conversion of UDP-glucuronic acid to UDP-xylose, as confirmed by NMR analysis. NADH, UDP, and UDP-xylose inhibit the activity. Close homologs of the cryptococcal gene, which we termed UXS1, appear in genome sequence data from organisms ranging from bacteria to humans.

  Publication DOI: 10.1073/pnas.211229198
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: peled@ccrc.uga.edu
  Institutions: Complex Carbohydrate Research Center and Department of Botany, University of Georgia, Athens, GA 30602, USA, Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA
  Methods: 1H NMR, SDS-PAGE, HPLC, cloning, protein expression, UDP-GlcA decarboxylase assay
  
   
  
  Cryptococcus neoformans B
  CSDB ID 40538 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_134624,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_1394182,IEDB_141794,IEDB_144983,IEDB_145668,IEDB_151528,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_983930,SB_163,SB_165,SB_166,SB_187,SB_195,SB_197,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 6961
  Bar-Peled M, Griffith CL, Doering TL "Functional cloning and characterization of a UDP-glucuronic acid decarboxylase: the pathogenic fungus Cryptococcus neoformans elucidates UDP-xylose synthesis" - Proceedings of the National Academy of Sciences of the USA 21 (2001) 12003-12008
  

  UDP-xylose is a sugar donor required for the synthesis of diverse and important glycan structures in animals, plants, fungi, and bacteria. Xylose-containing glycans are particularly abundant in plants and in the polysaccharide capsule that is the major virulence factor of the pathogenic fungus Cryptococcus neoformans. Biosynthesis of UDP-xylose is mediated by UDP-glucuronic acid decarboxylase, which converts UDP-glucuronic acid to UDP-xylose. Although this enzymatic activity was described over 40 years ago it has never been fully purified, and the gene encoding it has not been identified. We used homology to a bacterial gene, hypothesized to encode a related function, to identify a cryptococcal sequence as putatively encoding a UDP-glucuronic acid decarboxylase. A soluble 47-kDa protein derived from bacteria expressing the C. neoformans gene catalyzed conversion of UDP-glucuronic acid to UDP-xylose, as confirmed by NMR analysis. NADH, UDP, and UDP-xylose inhibit the activity. Close homologs of the cryptococcal gene, which we termed UXS1, appear in genome sequence data from organisms ranging from bacteria to humans.

  Publication DOI: 10.1073/pnas.211229198
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: peled@ccrc.uga.edu
  Institutions: Complex Carbohydrate Research Center and Department of Botany, University of Georgia, Athens, GA 30602, USA, Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, MO 63110, USA
  Methods: 1H NMR, SDS-PAGE, HPLC, cloning, protein expression, UDP-GlcA decarboxylase assay
  
   
  
  Cryptococcus neoformans
  CSDB ID 40794 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) Ser/Thr-protein
Compound class: EPS, O-glycan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_136104,IEDB_1394182,IEDB_140116,IEDB_141793,IEDB_141829,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_76933,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7134
  Schutzbach J, Ankel H, Brockhausen I "Synthesis of cell envelope glycoproteins of Cryptococcus laurentii" - Carbohydrate Research 342(7) (2007) 881-893
  

  Fungi of the genus Cryptococcus are encapsulated basidiomycetes that are ubiquitously found in the environment. These organisms infect both lower and higher animals. Human infections that are common in immune-compromised individuals have proven difficult to cure or even control with currently available antimycotics that are quite often toxic to the host. The virulence of Cryptococcus has been linked primarily to its polysaccharide capsule, but also to cell-bound glycoproteins. In this review, we show that Cryptococcus laurentii is an excellent model for studies of polysaccharide and glycoprotein synthesis in the more pathogenic relative C. neoformans. In particular, we will discuss the structure and biosynthesis of O-linked carbohydrates on cell envelope glycoproteins of C. laurentii. These O-linked structures are synthesized by at least four mannosyltransferases, two galactosyltransferases, and at least one xylosyltransferase that have been characterized. These glycosyltransferases have no known homologues in human tissues. Therefore, enzymes involved in the synthesis of cryptococcal glycoproteins, as well as related enzymes involved in capsule synthesis, are potential targets for the development of specific inhibitors for treatment of cryptococcal disease.

  synthesis, galactosyltransferase, sugar nucleotides, Mannosyltransferase, Cryptococcus neoformans, Cryptococcus laurentii, O-Linked glycoprotein synthesis, Xylosyltransferase, AIDS

  NCBI PubMed ID: 17316583
  Publication DOI: 10.1016/j.carres.2007.01.002
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: Inka.JSBach@kos.net (John Schutzbach)
  Institutions: Department of Medicine and Department of Biochemistry, Queen’s University, Etherington Hall, Kingston, Ontario, Canada, Service de Virologie, Hôpital Saint-Vincent-de-Paul, Faculté de Médecine, Université René Descartes, Paris, France
  
   
  
  Cryptococcus laurentii
  CSDB ID 42039 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: CPS, glucuronoxylomannan (GXM)
Contained glycoepitopes: IEDB_114701,IEDB_115136,IEDB_115576,IEDB_130701,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_140630,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_423153,IEDB_76933,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 7134
  Schutzbach J, Ankel H, Brockhausen I "Synthesis of cell envelope glycoproteins of Cryptococcus laurentii" - Carbohydrate Research 342(7) (2007) 881-893
  

  Fungi of the genus Cryptococcus are encapsulated basidiomycetes that are ubiquitously found in the environment. These organisms infect both lower and higher animals. Human infections that are common in immune-compromised individuals have proven difficult to cure or even control with currently available antimycotics that are quite often toxic to the host. The virulence of Cryptococcus has been linked primarily to its polysaccharide capsule, but also to cell-bound glycoproteins. In this review, we show that Cryptococcus laurentii is an excellent model for studies of polysaccharide and glycoprotein synthesis in the more pathogenic relative C. neoformans. In particular, we will discuss the structure and biosynthesis of O-linked carbohydrates on cell envelope glycoproteins of C. laurentii. These O-linked structures are synthesized by at least four mannosyltransferases, two galactosyltransferases, and at least one xylosyltransferase that have been characterized. These glycosyltransferases have no known homologues in human tissues. Therefore, enzymes involved in the synthesis of cryptococcal glycoproteins, as well as related enzymes involved in capsule synthesis, are potential targets for the development of specific inhibitors for treatment of cryptococcal disease.

  synthesis, galactosyltransferase, sugar nucleotides, Mannosyltransferase, Cryptococcus neoformans, Cryptococcus laurentii, O-Linked glycoprotein synthesis, Xylosyltransferase, AIDS

  NCBI PubMed ID: 17316583
  Publication DOI: 10.1016/j.carres.2007.01.002
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: Inka.JSBach@kos.net (John Schutzbach)
  Institutions: Department of Medicine and Department of Biochemistry, Queen’s University, Etherington Hall, Kingston, Ontario, Canada, Service de Virologie, Hôpital Saint-Vincent-de-Paul, Faculté de Médecine, Université René Descartes, Paris, France
  
   
  
  Cryptococcus flavescens
  CSDB ID 42041 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: glucan
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_130701,IEDB_136045,IEDB_140116,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_149135,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_76933,IEDB_983930,SB_44,SB_67,SB_72,SB_86

• Article ID: 7670
  Wang J, Cao B, Zhao H, Feng J "Emerging roles of Ganoderma lucidum in anti-aging" - Aging and Disease 8(6) (2017) 691-707
  

  Ganoderma lucidum is a white-rot fungus that has been viewed as a traditional Chinese tonic for promoting health and longevity. It has been revealed that several extractions from Ganoderma lucidum, such as Ethanol extract, aqueous extract, mycelia extract, water soluble extract of the culture medium of Ganoderma lucidum mycelia, Ganodermasides A, B, C, D, and some bioactive components of Ganoderma lucidum, including Reishi Polysaccharide Fraction 3, Ganoderma lucidum polysaccharides I, II, III, IV, Ganoderma lucidum peptide, Ganoderma polysaccharide peptide, total G. lucidum triterpenes and Ganoderic acid C1 could exert lifespan elongation or related activities. Although the use of Ganoderma lucidum as an elixir has been around for thousands of years, studies revealing its effect of lifespan extension are only the tip of the iceberg. Besides which, the kinds of extractions or components being comfrimed to be anti-aging are too few compared with the large amounts of Ganoderma lucidum extractions or constituients being discovered. This review aims to lay the ground for fully elucidating the potential mechanisms of Ganoderma lucidum underlying anti-aging effect and its clinical application.

  Antioxidant, immunomodulation, Ganoderma lucidum, anti-aging, anti-neurodegeneration

  NCBI PubMed ID: 29344411
  Publication DOI: 10.14336/AD.2017.0410
  Journal NLM ID: 101540533
  Publisher: California: JKL International
  Correspondence: Feng J ; Zhao H
  Institutions: Department of Neurology, Shengjing Hospital, China Medical University, Shenyang, China, Cerebrovascular Diseases Research Institute, Xuanwu Hospital of Capital Medical University, Beijing, China
  
   
  
  Ganoderma lucidum
  CSDB ID 43107 (all data & tools)

Show legend Show as text

Structure type: monomer
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_114701,IEDB_167188,IEDB_174332

• Article ID: 7749
  Chen HP, Liu JK "Secondary metabolites from higher fungi" - Progress in the Chemistry of Organic Natural Products 106 (2017) 1-201
  

  Secondary metabolites of higher fungi (mushrooms) are an underexplored resource compared to plant-derived secondary metabolites. An increasing interest in mushroom natural products has been noted in recent years. This chapter gives a comprehensive overview of the secondary metabolites from higher fungi, with 765 references highlighting the isolation, structure elucidation, biological activities, chemical syntheses, and biosynthesis of pigments, nitrogen-containing compounds, and terpenoids from mushrooms. Mushroom toxins are also included in each section.In a section on pigments of higher fungi, pigments are classified into four categories, namely, those from the shikimate-chorismate, acetate-malonate, and mevalonate biosynthetic pathways, and pigments containing nitrogen, with 145 references covering the years 2010-2016.In a section on other nitrogen-containing compounds of higher fungi, compounds are categorized primarily into nitrogen heterocycles, nucleosides, non-protein amino acids, cyclic peptides, and sphingolipids, with 65 references covering the years 2010-2016. In turn, in a section describing terpenoids of higher fungi, the sesquiterpenoids and diterpenoids are thoroughly elaborated, spanning the years 2001-2016, and 2009-2016, respectively. The divergent biosynthetic pathways from farnesyl pyrophosphate to sesquiterpenoids are also described. Selected triterpenoids with novel structures and promising biological activities, including lanostanes and ergostanes, are reported from the genus Ganoderma, and the fungi Antrodia cinnamomea and Poria cocos. In addition, cucurbitanes and saponaceolides are also compiled in this section.

  biosynthesis, biological activity, chemical synthesis, mushrooms, secondary metabolites, higher fungi, triterpenoids, diterpenoids, mushroom toxins, nitrogen-containing compounds, pigments, sesquiterpenoids

  NCBI PubMed ID: 28762089
  Publication DOI: 10.1007/978-3-319-59542-9_1
  Journal NLM ID: 101605200
  Publisher: Wien: Springer
  Correspondence: liujikai@mail.scuec.edu.cn
  Institutions: State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming, China, School of Pharmaceutical Sciences, South-Central University for Nationalities, Wuhan, China
  
   
  
  Fomitopsis pinicola
  CSDB ID 44597 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_130701,IEDB_136045,IEDB_140116,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_149135,IEDB_152206,IEDB_152214,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_76933,IEDB_983930,SB_44,SB_67,SB_72,SB_86

• Article ID: 7858
  Wang YY, Khoo KH, Chen ST, Lin CC, Wong CH, Lin CH "Studies on the immuno-modulating and antitumor activities of Ganoderma lucidum (Reishi) polysaccharides: functional and proteomic analyses of a fucose-containing glycoprotein fraction responsible for the activities" - Bioorganic and Medicinal Chemistry 10(4) (2002) 1057-1062
  

  A fucose-containing glycoprotein fraction which stimulates spleen cell proliferation and cytokine expression has been identified from the water-soluble extract of Ganoderma lucidum. Proteomic analysis of mouse spleen cells treated with this glycoprotein fraction showed approximately 50% change of the proteome. Further studies on the activities of this glycoprotein fraction through selective proteolysis and glycosidic cleavage indicate that a fucose containing polysaccharide fraction is responsible for stimulating the expression of cytokines, especially IL-1, IL-2 and INF-gamma.

  polysaccharides, glycoprotein, proliferation, Ganoderma lucidum

  NCBI PubMed ID: 11836115
  Publication DOI: 10.1016/s0968-0896(01)00377-7
  Journal NLM ID: 9413298
  Publisher: Elsevier
  Correspondence: wong@scripps.edu
  Institutions: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, Laboratory of Bioorganic Chemistry, Institute of Chemistry, Academia Sinica, Taipei, Taiwan
  Methods: GC-MS, amino acid analysis, MALDI-TOF MS, biological assays, methanolysis, electrophoresis, enzymatic digestion, extraction, acetylation, gel filtration chromatography, derivatization, anthrone-sulfuric acid assay, MTT
  
   
  
  Ganoderma lucidum
  CSDB ID 45927 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Trivial name: xylomannan
Compound class: xylomannan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_164480,IEDB_167188,IEDB_174332,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72

• Article ID: 7902
  Free SJ "Fungal cell wall organization and biosynthesis" - Advances in Genetics 81 (2013) 33-82
  

  The composition and organization of the cell walls from Saccharomyces cerevisiae, Candida albicans, Aspergillus fumigatus, Schizosaccharomyces pombe, Neurospora crassa, and Cryptococcus neoformans are compared and contrasted. These cell walls contain chitin, chitosan, β-1,3-glucan, β-1,6-glucan, mixed β-1,3-/β-1,4-glucan, α-1,3-glucan, melanin, and glycoproteins as major constituents. A comparison of these cell walls shows that there is a great deal of variability in fungal cell wall composition and organization. However, in all cases, the cell wall components are cross-linked together to generate a cell wall matrix. The biosynthesis and properties of each of the major cell wall components are discussed. The chitin and glucans are synthesized and extruded into the cell wall space by plasma membrane-associated chitin synthases and glucan synthases. The glycoproteins are synthesized by ER-associated ribosomes and pass through the canonical secretory pathway. Over half of the major cell wall proteins are modified by the addition of a glycosylphosphatidylinositol anchor. The cell wall glycoproteins are also modified by the addition of O-linked oligosaccharides, and their N-linked oligosaccharides are extensively modified during their passage through the secretory pathway. These cell wall glycoprotein posttranslational modifications are essential for cross-linking the proteins into the cell wall matrix. Cross-linking the cell wall components together is essential for cell wall integrity. The activities of four groups of cross-linking enzymes are discussed. Cell wall proteins function as cross-linking enzymes, structural elements, adhesins, and environmental stress sensors and protect the cell from environmental changes.

  Candida albicans, Aspergillus fumigatus, Saccharomyces cerevisiae, fungal cell wall, Schizosaccharomyces pombe, Neurospora crassa, cell wall biogenesis, glucan; chitin, Cryptococcus neoformas

  NCBI PubMed ID: 23419716
  Publication DOI: 10.1016/B978-0-12-407677-8.00002-6
  Journal NLM ID: 0370421
  Publisher: San Diego, CA: Academic Press
  Correspondence: free@buffalo.edu
  Institutions: Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA
  Methods: MS, electrophoresis, enzymatic digestion, microscopy
  
   
  
  Cryptococcus neoformans
  CSDB ID 44865 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: MP84 (Cda3) protein
Trivial name: cell wall mannoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_140434,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_144995,IEDB_145668,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_164174,IEDB_164479,IEDB_167188,IEDB_174332,IEDB_241100,IEDB_474450,IEDB_76933,IEDB_857733,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_55,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

• Article ID: 9632
  Lee SB, Mota C, Thak EJ, Kim J, Son YJ, Oh DB, Kang HA "Effects of altered N-glycan structures of Cryptococcus neoformans mannoproteins, MP98 (Cda2) and MP84 (Cda3), on interaction with host cells" - Scientific Reports 13(1) (2023) 1175
  

  Cryptococcus neoformans is an opportunistic human fungal pathogen causing lethal meningoencephalitis. It has several cell wall mannoproteins (MPs) identified as immunoreactive antigens. To investigate the structure and function of N-glycans assembled on cryptococcal cell wall MPs in host cell interactions, we purified MP98 (Cda2) and MP84 (Cda3) expressed in wild-type (WT) and N-glycosylation-defective alg3 mutant (alg3Δ) strains. HPLC and MALDI-TOF analysis of the MP proteins from the WT revealed protein-specific glycan structures with different extents of hypermannosylation and xylose/xylose phosphate addition. In alg3Δ, MP98 and MP84 had truncated core N-glycans, containing mostly five and seven mannoses (M5 and M7 forms), respectively. In vitro adhesion and uptake assays indicated that the altered core N-glycans did not affect adhesion affinities to host cells although the capacity to induce the immune response of bone-marrow derived dendritic cells (BMDCs) decreased. Intriguingly, the removal of all N-glycosylation sites on MP84 increased adhesion to host cells and enhanced the induction of cytokine secretion from BMDCs compared with that on MP84 carrying WT N-glycans. Therefore, the structure-dependent effects of N-glycans suggested their complex roles in modulating the interaction of MPs with host cells to avoid nonspecific adherence to host cells and host immune response hyperactivation.

  structure, N-glycans, Cryptococcus neoformans, cell wall mannoproteins

  NCBI PubMed ID: 36670130
  Publication DOI: 10.1038/s41598-023-27422-9
  Journal NLM ID: 101563288
  Publisher: London: Nature Publishing Group
  Correspondence: H.A. Kang
  Institutions: Department of Life Science, College of Natural Science, Chung-Ang University, Seoul, 156-756, South Korea, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, South Korea, Department of Biosystems and Bioengineering, KRIBB School, University of Science and Technology (UST), Daejeon, 34113, South Korea
  Methods: SDS-PAGE, DNA techniques, Western blotting, MALDI-TOF MS, HPLC, protein detection, cytokine production
  
   
  
  Cryptococcus neoformans
  CSDB ID 41426 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: alg3ΔMP84 (Cda3) protein
Trivial name: cell wall mannoprotein
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_141793,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_145668,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_167188,IEDB_174332,IEDB_241100,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_55,SB_67,SB_72,SB_73,SB_74,SB_85

• Article ID: 9632
  Lee SB, Mota C, Thak EJ, Kim J, Son YJ, Oh DB, Kang HA "Effects of altered N-glycan structures of Cryptococcus neoformans mannoproteins, MP98 (Cda2) and MP84 (Cda3), on interaction with host cells" - Scientific Reports 13(1) (2023) 1175
  

  Cryptococcus neoformans is an opportunistic human fungal pathogen causing lethal meningoencephalitis. It has several cell wall mannoproteins (MPs) identified as immunoreactive antigens. To investigate the structure and function of N-glycans assembled on cryptococcal cell wall MPs in host cell interactions, we purified MP98 (Cda2) and MP84 (Cda3) expressed in wild-type (WT) and N-glycosylation-defective alg3 mutant (alg3Δ) strains. HPLC and MALDI-TOF analysis of the MP proteins from the WT revealed protein-specific glycan structures with different extents of hypermannosylation and xylose/xylose phosphate addition. In alg3Δ, MP98 and MP84 had truncated core N-glycans, containing mostly five and seven mannoses (M5 and M7 forms), respectively. In vitro adhesion and uptake assays indicated that the altered core N-glycans did not affect adhesion affinities to host cells although the capacity to induce the immune response of bone-marrow derived dendritic cells (BMDCs) decreased. Intriguingly, the removal of all N-glycosylation sites on MP84 increased adhesion to host cells and enhanced the induction of cytokine secretion from BMDCs compared with that on MP84 carrying WT N-glycans. Therefore, the structure-dependent effects of N-glycans suggested their complex roles in modulating the interaction of MPs with host cells to avoid nonspecific adherence to host cells and host immune response hyperactivation.

  structure, N-glycans, Cryptococcus neoformans, cell wall mannoproteins

  NCBI PubMed ID: 36670130
  Publication DOI: 10.1038/s41598-023-27422-9
  Journal NLM ID: 101563288
  Publisher: London: Nature Publishing Group
  Correspondence: H.A. Kang
  Institutions: Department of Life Science, College of Natural Science, Chung-Ang University, Seoul, 156-756, South Korea, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, 34141, South Korea, Department of Biosystems and Bioengineering, KRIBB School, University of Science and Technology (UST), Daejeon, 34113, South Korea
  Methods: SDS-PAGE, DNA techniques, Western blotting, MALDI-TOF MS, HPLC, protein detection, cytokine production
  
   
  
  Cryptococcus neoformans alg3Δ
  CSDB ID 41427 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_115136,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_1394181,IEDB_140630,IEDB_141794,IEDB_142489,IEDB_144562,IEDB_149135,IEDB_151528,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_225177,IEDB_423153,IEDB_885823,SB_7,SB_86

• Article ID: 10073
  Stevenson TT, Darvill AG, Albersheim P "Structure of plant cell walls XXIII. Structural features of the plant cell-wall polysaccharide rhamnogalacturonan-II" - Carbohydrate Research 182 (1988) 207-226
  

  Rhamnogalacturonan-II (RG-II), isolated from the cell walls of suspension-cultured sycamore cells, has been further characterized. End-group analysis of RG-II showed that the polysaccharide contains about 30 glycosyl residues. Some 28 residues have been found as constituents of well characterized oligosaccharide fragments of RG-II. RG-II was treated with lithium metal dissolved in ethylenediamine to degrade the glycosyluronic acid residues. The major product was isolated, characterized, and shown to be the triglycosylalditol α-Xyl-(1→3)-α-Fuc-(1→4)-β-Rha-(1→31)-apiitol. This tetrasaccharide fragment of RG-II has three residues in common with a previously characterized heptasaccharide that had been derived from RG-II by partial hydrolysis with acid. RG-II was found to contain a large number of branched galactosyluronic acid residues that have not yet been identified as components of oligosaccharide fragments, although they are undoubtedly part of an octa(galactosyluronic acid) fragment generated by partial acid hydrolysis. The results of sequential partial acid hydrolysis provided evidence that, in RG-II, the extremely acid-labile 3-deoxy-d-manno-2-octulosonic-acid and 3-deoxy-d-lyxo-2-heptulosaric acid residues are attached to O-3 of 3,4-linked galactosyluronic acid residues, and that the mildly acid-labile apiofuranosyl residues are attached to O-2 of 2,4-linked galactosyluronic acid residues. These and previously published data suggested that RG-II has a highly branched structure, arranged around an α-(1→4)-linked galactosyluronic acid backbone.

  Publication DOI: 10.1016/0008-6215(88)84004-7
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Complex Carbohydrate Research Center and Department of Biochemistry, University of Georgia, Russell Research Center of the United States Department of Agriculture, Athens, Georgia, U.S.A.
  Methods: 1H NMR, gel filtration, FAB-MS, partial acid hydrolysis, GC-MS, acid hydrolysis
  
   
  
  Acer pseudoplatanus
  CSDB ID 115517 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115015,IEDB_130699,IEDB_136045,IEDB_1394181,IEDB_142489,IEDB_144562,IEDB_149135,IEDB_152214,IEDB_174333,IEDB_225177,IEDB_885823,SB_86

• Article ID: 10073
  Stevenson TT, Darvill AG, Albersheim P "Structure of plant cell walls XXIII. Structural features of the plant cell-wall polysaccharide rhamnogalacturonan-II" - Carbohydrate Research 182 (1988) 207-226
  

  Rhamnogalacturonan-II (RG-II), isolated from the cell walls of suspension-cultured sycamore cells, has been further characterized. End-group analysis of RG-II showed that the polysaccharide contains about 30 glycosyl residues. Some 28 residues have been found as constituents of well characterized oligosaccharide fragments of RG-II. RG-II was treated with lithium metal dissolved in ethylenediamine to degrade the glycosyluronic acid residues. The major product was isolated, characterized, and shown to be the triglycosylalditol α-Xyl-(1→3)-α-Fuc-(1→4)-β-Rha-(1→31)-apiitol. This tetrasaccharide fragment of RG-II has three residues in common with a previously characterized heptasaccharide that had been derived from RG-II by partial hydrolysis with acid. RG-II was found to contain a large number of branched galactosyluronic acid residues that have not yet been identified as components of oligosaccharide fragments, although they are undoubtedly part of an octa(galactosyluronic acid) fragment generated by partial acid hydrolysis. The results of sequential partial acid hydrolysis provided evidence that, in RG-II, the extremely acid-labile 3-deoxy-d-manno-2-octulosonic-acid and 3-deoxy-d-lyxo-2-heptulosaric acid residues are attached to O-3 of 3,4-linked galactosyluronic acid residues, and that the mildly acid-labile apiofuranosyl residues are attached to O-2 of 2,4-linked galactosyluronic acid residues. These and previously published data suggested that RG-II has a highly branched structure, arranged around an α-(1→4)-linked galactosyluronic acid backbone.

  Publication DOI: 10.1016/0008-6215(88)84004-7
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Complex Carbohydrate Research Center and Department of Biochemistry, University of Georgia, Russell Research Center of the United States Department of Agriculture, Athens, Georgia, U.S.A.
  Methods: 1H NMR, gel filtration, FAB-MS, partial acid hydrolysis, GC-MS, acid hydrolysis
  
   
  
  Acer pseudoplatanus
  CSDB ID 215517 (all data & tools)