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Structure type: oligomer
Compound class: mannan, disaccharide
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 2663
  Venisse A, Berjeaud JM, Chaurand P, Gilleron M, Puzo G "Structural features of lipoarabinomannan from Mycobacterium bovis BCG. Determination of molecular mass by laser desorption mass spectrometry" - Journal of Biological Chemistry 268 (1993) 12401-12411
  

  It was recently shown that mycobacterial lipoarabinomannan (LAM) can be classified into two types (Chatterjee, D., Lowell, K., Rivoire B., McNeil M. R., and Brennan, P. J. (1992) J. Biol. Chem. 267, 6234-6239) according to the presence or absence of mannosyl residues (Manp) located at the nonreducing end of the oligoarabinosyl side chains. These two types of LAM were found in a pathogenic Mycobacterium tuberculosis strain and in an avirulent M. tuberculosis strain, respectively, suggesting that LAM with Manp characterizes virulent and "disease-inducing strains." We now report the structure of the LAM from Mycobacterium bovis Bacille Calmette-Guérin (BCG) strain Pasteur, largely used throughout the world as vaccine against tuberculosis. Using an up-to-date analytical approach, we found that the LAM of M. bovis BCG belongs to the class of LAMs capped with Manp. By means of two-dimensional homonuclear and heteronuclear scalar coupling NMR analysis and methylation data, the sugar spin system assignments were partially established, revealing that the LAM contained two types of terminal Manp and 2-O-linked Manp. From the following four-step process: (i) partial hydrolysis of deacylated LAM (dLAM), (ii) oligosaccharide derivatization with aminobenzoic ethyl ester, (iii) HPLC purification, (iv) FAB/MS-MS analysis; it was shown that the dimannosyl unit α-D-Manp-(1→2)-α-D-Manp is the major residue capping the termini of the arabinan of the LAM. In this report, LAM molecular mass determination was established using matrix-assisted UV-laser desorption/ionization mass spectrometry which reveals that the LAM molecular mass is around 17.4 kDa. The similarity of the LAM structures between M. bovis BCG and M. tuberculosis H37Rv is discussed in regard to their function in the immunopathology of mycobacterial infection.

  NCBI PubMed ID: 8509380
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Centre National de la Recherche Scientifique, Département Glycoconjugués et Biomembranes, Toulouse, France
  Methods: 1H NMR, FAB-MS/MS, LD-MS
  
   
  
  Mycobacterium bovis BCG
  CSDB ID 136630 (all data & tools)
• Article ID: 6481
  Kobayashi H, Takahashi SI, Shibata N, Miyauchi M, Ishida M, Sato J, Maeda K, Suzuki S "Structural modification of cell wall mannans of Candida albicans serotype A strains grown in yeast extract-Sabouraud liquid medium under acidic conditions" - Infection and Immunity 62 (1994) 968-973
  

  The cell wall mannans of two Candida albicans serotype A strains, NIH A-207 and J-1012 (abbreviated as A and J strains, respectively), cultured in yeast extract-Sabouraud liquid medium at pH 2.0, contained neither a phosphate group nor a β-1,2-linked mannopyranose unit (H. Kobayashi, P. Giummelly, S. Takahashi, M. Ishida, J. Sato, M. Takaku, Y. Nishidate, N. Shibata, Y. Okawa, and S. Suzuki, Biochem. Biophys. Res. Commun. 175:1003-1009, 1991). In this study, the mannans obtained from A and J strains grown in pH 2.0 medium (abbreviated as mannans A2 and J2, respectively) exhibited quite different reactivities against rabbit anti-C. albicans and anti-Saccharomyces cerevisiae sera compared with those of mannans from the corresponding strains cultured in conventional medium at pH 5.9 (abbreviated as mannans A and J, respectively). Namely, mannans A2 and J2 lost reactivity against the former serum but reacted with the latter serum to a higher extent than mannans A and J. In order to account for these difference in more detail, mannans A2 and J2 were subjected to acetolysis. Elution profiles of the acetolysates were completely different from those of acetolysates obtained from mannans A and J reported in our previous papers. The 1H nuclear magnetic resonance spectra of the oligosaccharides from mannans A2 and J2 obtained by this procedure indicate that the side chains are composed of α-linked mannopyranose units densely linked to the α-1,6-linked backbone. The long side chains containing one α-1,3-linked mannopyranose unit are markedly increased.

  NCBI PubMed ID: 8112871
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
  Methods: 1H NMR, acetolysis, hot-water extraction, short-term precipitation, quantitative precipitin assay
  
   
  
  Candida albicans A NIH A-207, Candida albicans A NIH J-1012
  CSDB ID 130518 (all data & tools)
• Article ID: 7334
  Nakajima T, Yoshida M, Nakamura M, Hiura N, Matsuda K "Structure of the cell wall proteogalactomannan from Neurospora crassa: II. Structural analysis of the polysaccharide part" - Journal of Biochemistry 96(4) (1984) 1013-1020
  

  The native proteoheteroglycan (PHG) from mycelia of Neurospora crassa contains two kinds of carbohydrate chains differing structure. The oligosaccharides containing mannose and galactofuransoe are attached by O-glycosidic linkages to serine or threonine residues in the protein (J. Biochem. 96, 1005-1011, 1984). The second kind of carbohydrate chain is a polysaccharide containing mannose and galactofuranose as the main sugar components. The results of structural studies with methylation and NMR analyses on the native PHG and some of its specifically degraded products obtained on partial acid hydrolysis and acetolysis indicate that the polysaccharide moiety of the PHG has an (αl-6) linked mannan backbone with mainly (αl-2) linked side chains, each of which consists of 2 to 5 mannose units, and most of the mannosyl side chains bear β-galactofuranosyl residues linked to the 2 positions of the mannosyl nonreducing terminals. The galactofuranose residues are linked with each other by (β1-5) bonds.

  amino acid, Galactomannan, proteoglycan, Neurospora crassa

  NCBI PubMed ID: 6240491
  Publication DOI: 10.1093/oxfordjournals.jbchem.a134917
  Journal NLM ID: 0376600
  Publisher: Japanese Biochemical Society
  Institutions: Department of Agricultural Chemistry, Tohoku University, Sendai, Japan
  Methods: gel filtration, 13C NMR, 1H NMR, methylation, GC, amino acid analysis, enzymatic digestion, extraction, optical rotation measurement, acetylation, acetolysis, reduction, phenol-sulfuric acid assay, Lowry method
  
   
  
  Neurospora crassa
  CSDB ID 44129 (all data & tools)
• Article ID: 7666
  Takahashi S, Kudoh A, Okawa Y, Shibata N "Significant differences in the cell-wall mannans from three Candida glabrata strains correlate with antifungal drug sensitivity" - FEBS Journal 279(10) (2012) 1844-1856
  

  Candida glabrata is often the second or third most common cause of candidiasis after Candida albicans. C. glabrata infections are difficult to treat, often resistant to many azole antifungal agents and are associated with a high mortality rate in compromised patients. We determined the antigenic structure of the cell-wall mannoproteins from three C. glabrata strains, NBRC 0005, NBRC 0622 and NBRC 103857. 1H NMR and methylation analyses of the acetolysis products of these mannoproteins showed a significant difference in the amount of the β-1,2-linked mannose residue and side-chain structure. The C. glabrata NBRC 103857 strain contained up to the triose side chains and the nonreducing terminal of the triose was predominantly the β-1,2-linked mannose residue. By contrast, the mannans of the two former strains possessed up to the tetraose side chains and the amount of the β-1,2-linked mannose residue was very low. Larger oligosaccharides than tetraose in the acetolysis products of these mannans were identified as incomplete cleavage fragments by analyzing methylation, 1H NMR spectra and the α1-2,3 mannosidase degradation reaction. Resistance to the antifungal drugs itraconazole and micafungin was significantly different in these strains. Interestingly, the NBRC 103857 strain, which involved a large amount of the β-1,2-linked mannose residues, exhibited significant sensitivity to these antifungal drugs.

  oligosaccharide, polysaccharide, NMR spectroscopy, azole resistance, cell-wall mannan

  NCBI PubMed ID: 22404982
  Publication DOI: 10.1111/j.1742-4658.2012.08564.x
  Journal NLM ID: 101229646
  Publisher: Blackwell Publishing
  Correspondence: nshibata@tohoku-pharm.ac.jp
  Institutions: Department of Infection and Host Defense, Tohoku Pharmaceutical University, Sendai, Japan
  Methods: 1H NMR, methylation, GC-MS, acid hydrolysis, biological assays, enzymatic digestion, extraction, acetylation, acetolysis, reduction, cell growth, DQF-COSY
  
   
  
  Candida glabrata NBRC 0622
  CSDB ID 45860 (all data & tools)
• Article ID: 7759
  Kobayashi H, Shibata N, Osaka T, Miyagawa Y, Ohkubo Y, Suzuki S "Structural study of cell wall mannan of a Candida albicans (serotype A) strain" - Phytochemistry 31(4) (1992) 1147-1153
  

  The structure of the mannan of Candida albicans NIH A-207 strain (serotype A) was investigated by adopting mild acetolysis followed by enzymolysis with an Arthrobacter GJM-1 exo-alpha-mannosidase. The resultant oligosaccharides, from pentaose to octaose (where manp = D-mannopyranose), were identified as manp β (1-2)manp alpha (1-2)manp alpha (1-2)manp alpha (1-2)manp, manp β (1-2)manp β (1-2)manp alpha (1-2)manp alpha (1-2)- manp alpha (1-2)manp, manp β (1-2)manp β (1-2)manp β (1-2)manp alpha (1-2)manp alpha (1--2)manp alpha (1-2)manp and manp β (1-2)manp β (1-2)manp β (1-2)manp β (1-2)manp alpha (1-2)manp alpha (1-2)manp alpha (1-2)manp, respectively. Analyses of alpha-linked oligosaccharides obtained by acetolysis under conventional conditions gave the same oligosaccharides, from biose to heptaose, as those obtained from the mannans of C. albicans NIH B-792 (serotype B) and J-1012 (serotype A, formerly serotype C).

  mannan, cell wall polysaccharide, Candida albicans, fungus, Manno-oligosaccharides, acetolysis, β-(1-2)-linkage

  NCBI PubMed ID: 1368047
  Publication DOI: 10.1016/0031-9422(92)80250-i
  Journal NLM ID: 0151434
  Publisher: Elsevier
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai Aoba-ku, Miyagi, Japan, Department of Radiopharmacy, Tohoku College of Pharmacy, Sendai Aoba-ku, Miyagi, Japan
  Methods: 1H NMR, FAB-MS, acid hydrolysis, enzymatic digestion, acetolysis, protein detection, phenol-sulfuric acid assay, hydrolysis, phosphate measurement, antibody precipitation
  
   
  
  Candida albicans NIH A-207
  CSDB ID 44962 (all data & tools)
• Article ID: 7837
  Baron M, Iacomini M, Fantata E.S., Gorin P.A.J. "Galactomannan, lichenan and isolichenan from the polysaccharide-rich lichen Newropogon aurantiaco-ater" - Chemical and Pharmaceutical Bulletin 30(9) (1991) 3125-3126
  

  Newropogon aurantiaco-ater contains 56% of polysaccharide, from which lichenan (26%) was isolated in very large amounts, along with isolichenan (4%) and a galactomannan (1 %). The galactomannan consists mainly of a (1→6)-Iinked α-DManp main-chain partly substituted at 0-2 with α-D-Galp units, the virtual absence of β-D-Galp units being unusual in a lichen galactomannan. Arabinitol (3%) is also present.

  carbohydrates, arabinitol, Galactomannan, lichen, isolichenan, Newropogon aurantiaco-ater, lichenan

  Publication DOI: 10.1016/S0031-9422(00)98266-9
  Journal NLM ID: 0377775
  Publisher: Pharmaceutical Society Of Japan
  Institutions: Departamentos de Bioquimica e Biologia Celular, Universidade Federal do Paraná, Curitiba, Brasil
  Methods: 13C NMR, 1H NMR, partial acid hydrolysis, GC-MS, GC, Smith degradation, paper chromatography, electrophoresis, extraction, optical rotation measurement, methylation analysis, HPGPC, phenol-sulfuric acid assay
  
   
  
  Neuropogon aurantiaco-ater
  CSDB ID 47120 (all data & tools)
• Article ID: 8227
  Kudoh A, Okawa Y, Shibata N "Significant structural change in both O- and N-linked carbohydrate moieties of the antigenic galactomannan from Aspergillus fumigatus grown under different culture conditions" - Glycobiology 25(1) (2015) 74-87
  

  Invasive aspergillosis is an important cause of morbidity and mortality in immunocompromised patients. Diagnosis of this infection frequently employs detection of the circulating galactomannan in the patient serum using enzyme immunoassay (EIA), a highly sensitive and specific system. Although there are many structural studies of the galactomannan of Aspergillus fumigatus, some inconsistencies are present in these results. In this study, to clarify the relationship between the growth conditions and structure of the galactomannans, we cultured A. fumigatus using two distinct yeast/fungal cultivation media, i.e. the yeast extract-peptone-dextrose (YPD) medium and yeast nitrogen base (YNB) medium. Galactomannans prepared from the resulting culture supernatants were structurally characterized by 1H and 13C nuclear magnetic resonance, methylation analysis, acetolysis and α-mannosidase degradation. These assays revealed that the galactomannan from the YPD cultivation had short β-1,5-linked galactofuranose (Galf) oligosaccharide chains in both the O- and N-linked carbohydrate moieties, while the galactomannan from the YNB cultivation incorporated long Galf oligosaccharide chains. The galactomannans derived from the two culture conditions significantly differed in reactivity based on the EIA diagnostic system. We also demonstrated the presence of a novel Galf-containing branched oligosaccharide in the O-linked moiety

  NMR, antigen, oligosaccharide, Galactomannan, Aspergillus

  NCBI PubMed ID: 25187160
  Publication DOI: 10.1093/glycob/cwu091
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: nshibata@tohoku-pharm.ac.jp
  Institutions: Department of Infection and Host Defense, Tohoku Pharmaceutical University, Sendai, Japan, The Sendai Open Hospital, Sendai, Japan
  Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, enzyme immunoassay, acid hydrolysis, alkaline hydrolysis, enzymatic digestion, acetylation, acetolysis, methylation analysis, reduction, column chromatography, gel permeation chromatography, cell growth, dialysis, enzymatic assay, precipitation, evaporation, DEPT
  
   
  
  Aspergillus fumigatus NBRC 33022
  CSDB ID 48306 (all data & tools)
• Article ID: 8228
  Lee DJ, Bahn YS, Kim HJ, Chung SY, Kang HA "Unraveling the novel structure and biosynthetic pathway of O-linked glycans in the Golgi apparatus of the human pathogenic yeast Cryptococcus neoformans" - Journal of Biological Chemistry 290(3) (2015) 1861-1873
  

  Cryptococcus neoformans is an encapsulated basidiomycete causing cryptococcosis in immunocompromised humans. The cell surface mannoproteins of C. neoformans were reported to stimulate the host T-cell response and to be involved in fungal pathogenicity; however, their O-glycan structure is uncharacterized. In this study, we performed a detailed structural analysis of the O-glycans attached to cryptococcal mannoproteins using HPLC combined with exoglycosidase treatment and showed that the major C. neoformans O-glycans were short manno-oligosaccharides that were connected mostly by α1,2-linkages but connected by an α1,6-linkage at the third mannose residue. Comparison of the O-glycan profiles from wild-type and uxs1Δ mutant strains strongly supports the presence of minor O-glycans carrying a xylose residue. Further analyses of C. neoformans mutant strains identified three mannosyltransferase genes involved in O-glycan extensions in the Golgi. C. neoformans KTR3, the only homolog of the Saccharomyces cerevisiae KRE2/MNT1 family genes, was shown to encode an α1,2-mannosyltransferase responsible for the addition of the second mannose residue via an α1,2-linkage to the major O-glycans. C. neoformans HOC1 and HOC3, homologs of the Saccharomyces cerevisiae OCH1 family genes, were shown to encode α1,6-mannosyltransferases that can transfer the third mannose residue, via an α1,6-linkage, to minor O-glycans containing xylose and to major O-glycans without xylose, respectively. Moreover, the C. neoformans ktr3Δ mutant strain, which displayed increased sensitivity to SDS, high salt, and high temperature, showed attenuated virulence in a mouse model of cryptococcosis, suggesting that the extended structure of O-glycans is required for cell integrity and full pathogenicity of C. neoformans

  cell wall, glycosyltransferase, glycoprotein, Glycomics, mannosyltransferases, fungi, Cryptococcus neoformans, glycan analysis, O-mannosylation

  NCBI PubMed ID: 25477510
  Publication DOI: 10.1074/jbc.M114.607705
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: Kang HA
  Institutions: College of Pharmacy, Chung-Ang University, Seoul, South Korea, Department of Life Science, Center for Fungal Pathogenesis, Yonsei University, Seoul, South Korea, Department of Biotechnology, Center for Fungal Pathogenesis, Yonsei University, Seoul, South Korea
  Methods: PCR, DNA techniques, biological assays, HPLC, enzymatic digestion, hydrazinolysis, cell growth, dialysis, mutagenesis, derivatization, evaporation, centrifugation, staining
  
   
  
  Cryptococcus neoformans var. grubii H99, Cryptococcus neoformans var. grubii H99 (Δhoc2 mutant), Cryptococcus neoformans var. grubii H99 (Δhoc4 mutant), Cryptococcus neoformans var. grubii H99 (Δhoc1 mutant), Cryptococcus neoformans var. grubii H99 (Δhoc3 mutant), Cryptococcus neoformans var. grubii H99 (Δhoc1::HOC1 mutant), Cryptococcus neoformans var. grubii H99 (Δhoc3::HOC3 mutant)
  CSDB ID 48326 (all data & tools)
• Article ID: 8342
  Bystricky P, Machová E, Bystricky S "NMR comparison of hyphal and yeast Candida albicans serotype B mannans" - European Biophysics Journal: EBJ 47(5) (2018) 591-596
  

  A change from a globular to a filamentous hyphal form is an important feature in the pathogenicity of yeasts. Such a dimorphism while infecting a host organism is thought to be also accompanied in the case of Candida albicans spp. by a structural rearrangement of surface mannan antigen. The presented work brings new insights into the molecular structural changes of mannan C. albicans serotype B based on NMR experimental data. 1H and 13C signal identification of the anomeric region and the assignment of their linkage type is presented here. 2D deconvolution of the HSQC spectra facilitated accurate integration of all anomeric cross-peaks. Analysis of the differences in the integrals led to the proposal that C. albicans serotype B hyphal mannan side chains have the shortened structural moieties: Manα1-2Manα1- and Manα1-3 [Manα1-6] Manα1-2Manα1-. These represent the dominant structures important for construction of a saccharide-based prospective anti-candida vaccine.

  NMR, mannan, Candida albicans, yeast, Hyphae, serotype A, serotype B

  NCBI PubMed ID: 29654475
  Publication DOI: 10.1007/s00249-018-1298-y
  Journal NLM ID: 8409413
  Publisher: Berlin; New York: Springer International
  Correspondence: peter.bystricky@jfmed.uniba.sk
  Institutions: Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovakia, Division of Neurosciences, Biomedical Center Martin, Jessenius Faculty of Medicine in Martin, Comenius University in Bratislava, Martin, Slovakia
  Methods: 1H NMR, dialysis, precipitation, DQF-COSY, centrifugation, HSQC, H2BC
  
   
  
  Candida albicans CCY 29-3-103 B
  CSDB ID 48551 (all data & tools)