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1. Compound ID: 13097
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a-D-Manp3Me-(1-2)-{{{-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-}}}a-D-Manp-(1-3)-a-D-Manp-(1-3)-a-D-Manp |
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Structure type: oligomer
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_134620,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141795,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_241100,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 5188
Micoli F, Costantino P, Adamo R "Potential targets for next generation anti-microbial glycoconjugate vaccines" -
FEMS Microbiology Reviews 42(3) (2018) 388-423
Cell surface carbohydrates have been proven optimal targets for vaccine development. Conjugation of polysaccharides to a carrier protein triggers a T-cell dependent immune response to the glycan moiety. Licensed glycoconjugate vaccines are produced by chemical conjugation of capsular polysaccharides to prevent meningitis caused by meningococcus, pneumococcus and Haemophilus influenzae type b. However, other classes of carbohydrates (O-antigens, exopolysaccharides, wall/teichoic acids) represent attractive targets for developing vaccines.Recent analysis from WHO/CHO underpins alarming concern towards antibiotic resistant bacteria, such as the so called ESKAPE pathogens (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa and Enterobacter spp.) and additional pathogens such as Clostridium difficile and Group A Streptococcus. Fungal infections are also becoming increasingly invasive for immunocompromised patients or hospitalized individuals. Other emergencies could derive from bacteria which spread during environmental calamities (Vibrio cholerae) or with potential as bioterrorism weapons (Burkholderia pseudomallei and mallei, Francisella tularensis). Vaccination could aid reducing the use of broad spectrum antibiotics and provide protection by herd immunity also to individuals who are not vaccinated.This review analyses structural and functional differences of the polysaccharides exposed on the surface of emerging pathogenic bacteria, combined with medical need and technological feasibility of corresponding glycoconjugate vaccines.
carbohydrates, glycoconjugates, vaccines, glycoengineering, antimicrobial resistance
NCBI PubMed ID: 29547971Publication DOI: 10.1093/femsre/fuy011Journal NLM ID: 8902526Publisher: Oxford University Press
Correspondence: Roberto Adamo
Institutions: GSK Vaccines Institute for Global Health (GVGH), Via Fiorentina 1, 53100 Siena
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2. Compound ID: 16401
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-D-Man |
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Structure type: oligomer
Trivial name: mannopentaose, mannohexaose
Compound class: mannan, D-mannan
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141795,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 6370
Funayama M, Nishikawa A, Shinoda T, Suzuki M, Fukazawa Y "Antigenic relationship between Candida parapsilosis and Candida albicans serotype B" -
Microbiology and Immunology 28 (1984) 1359-1371
We examined the antigenic relationship between Candida parapsilosis and C. albicans serotype B with respect to antigenic factors 13 and 13b, specific for the former species and common to both species, respectively. Acetolysis of C. albicans serotype B cell-wall mannan gave six oligosaccharides. Their chemical structure was determined by 1H-nuclear magnetic resonance (NMR) spectroscopy, methylation analysis, and partial acid hydrolysis. The structure of the hexasaccharide derived from C. albicans serotype B mannan was α-D-Manp-(1-2)-α-D-Manp-(1-3)-α-D-Manp-(1- 2)-α-D-Manp-(1-2)- α-D-Manp-(1-2)-D-Man (M6) which is identical to that from C. parapsilosis mannan. Inhibition of two precipitin reaction systems (anti-C. albicans serotype B serum and anti-C. parapsilosis serum to the respective homologous mannan), by oligosaccharides from homologous and heterologous mannans indicated that M6 from either C. albicans serotype B or C. parapsilosis was the most effective inhibitor. Moreover inhibition of the agglutination reaction between factor serum containing anti-factors 13 and 13b and C. albicans serotype B or C. parapsilosis cells by oligosaccharides from both mannans also indicated that the M6s were the most effective inhibitors. These results suggest that the M6s derived from the two species are identical in their chemical structure, although the structures of the whole mannans of the two species are not identical as demonstrated by gel diffusion precipitation patterns, and that M6s may be involved in the specificities of antigenic factors 13 and 13b. The amount of M6 is larger in C. parapsilosis cell-wall mannan, suggesting that high repeating frequency of M6 fragment may induce the antibody specific for C. parapsilosis.
NCBI PubMed ID: 6085394Journal NLM ID: 7703966Publisher: Japanese Society For Bacteriology
- Article ID: 6431
Kobayashi H, Takaku M, Nishidate Y, Takahashi SI, Takikawa M, Shibata N, Suzuki S "Structure of the D-mannan of the pathogenic yeast, Candida stellatoidea ATCC 20408 (Type II) strain, in comparison with that of C. stellatoidea ATCC 36232 (Type I) strain" -
Carbohydrate Research 231 (1992) 105-116
Acid treatment of the cell-wall D-mannas of Candida stellatoidea strains ATCC 36232 (Type I, A3 strain) and ATCC 20408 (Type II, A2 strain) gave (1----2)-linked β-D-manno-oligosaccharides (dp 2-5), whereas treatment with alkali gave the (1----2)-linked α-D-mannobiose. Conventional acetolysis of the acid- and alkali-treated D-mannan of the A3 strain gave oligosaccharides consisting of (1----2)- and (1----3)-linked α-D-mannopyranose residues, similar to those of Candida albicans serotype B strain. Mild acetolysis of the acid- and alkali-treated D-mannan of the A2 strain gave higher oligosaccharides that were digested by the Arthrobacter GJM-1 strain exo-α-D-mannosidase. The results of 1H- and 13C-NMR analyses indicated this D-mannan to contain branches with the following structures: β-D-Manp-(1----2)-α-D-Manp-(1----2)-α-D-Manp++ +-(1----2)-α-D-Manp- (1----2)-D-Man, β-D-Manp-(1----2)-β-D-Manp-(1----2)-α-D-Manp -(1----2)- α-D-Manp-(1----2)-D-Man, and β-D-Manp-(1----2)-β-D-Manp-(1----2)-β-D-Manp-(1----2)-α-D-Manp-(1----2)-α-D-Manp-(1- ---2)-α-D-Manp- (1----2)-D-Man, in common with the D-mannans of C. albicans serotype A strains.
NCBI PubMed ID: 1394307Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Japan
- Article ID: 6452
Kobayashi H, Shibata N, Mitobe H, Ohkubo Y, Suzuki S "Structural study of phosphomannan of yeast-form cells of Candida albicans J-1012 strain with special reference to application of mild acetolysis" -
Archives of Biochemistry and Biophysics 272 (1989) 364-375
Structural analysis of the phosphomannan isolated from yeast-form cells of a pathogenic yeast, Candida albicans J-1012 strain, was conducted. Treatment of this phosphomannan (Fr. J) with 10 mM HCl at 100 degrees C for 60 min gave a mixture of β-1,2-linked manno-oligosaccharides, from tetraose to biose plus mannose, and an acid-stable mannan moiety (Fr. J-a), which was then acetolyzed by means of an acetolysis medium, 100:100:1 (v/v) mixture of (CH3CO)2O, CH3COOH, and H2SO4, at 40 degrees C for 36 h in order to avoid cleavage of the β-1,2 linkage. The resultant manno-oligosaccharide mixture was fractionated on a column of Bio-Gel P-2 to yield insufficiently resolved manno-oligosaccharide fractions higher than pentaose and lower manno-oligosaccharides ranging from tetraose to biose plus mannose. The higher manno-oligosaccharide fraction was then digested with the Arthrobacter GJM-1 α-mannosidase in order to cleave the enzyme-susceptible α-1,2 and α-1,3 linkages, leaving manno-oligosaccharides containing the β-1,2 linkage at their nonreducing terminal sites, Manp β 1----2Manp α 1----2Manp α 1----2Manp α 1----2Man, Manp β 1----2Manp β 1----2Manp α 1----2Manp α 1---- 2Manp α 1----2Man, and Manp β 1----2Manp β 1----2Manp β 1----2Manp α 1---- 2Manp α 1----2Manp α 1----2Man. However, the result of acetolysis of Fr. J-a by means of a 10:10:1 (v/v) mixture of (CH3CO)2O, CH3COOH, and H2SO4 at 40 degrees C for 13 h was significantly different from that obtained by the mild acetolysis method; i.e., the amount of mannose was apparently larger than that formed by the mild acetolysis method. In summary, a chemical structure for Fr. J as a highly branched mannan containing 14 different branching moieties was proposed.
NCBI PubMed ID: 2665649Journal NLM ID: 0372430Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
Methods: acetolysis
- Article ID: 6453
Kobayashi H, Shibata N, Nakada M, Chaki S, Mizugami K, Ohkubo Y, Suzuki S "Structural study of cell wall phosphomannan of Candida albicans NIH B-792 (serotype B) strain, with special reference to 1H and 13C NMR analyses of acid-labile oligomannosyl residues" -
Archives of Biochemistry and Biophysics 278 (1990) 195-204
Chemical structures of manno-oligosaccharides, from biose to heptaose, released from the phosphomannan of Candida albicans NIH B-792 strain (serotype B) by mild acid hydrolysis were investigated. The results of 1H NMR, 13C NMR, and fast atom bombardment mass spectrometry analyses confirmed that these manno-oligosaccharides belong to a homologous β-1,2-linked series. Although chemical shifts of 1H NMR patterns of these oligosaccharides were considerably too complicated to be assigned, their 13C NMR patterns were sufficiently simple to be interpreted, exhibiting a regular increase of downfield shift of ppm values of the C-1 atom from each mannopyranose residue in proportion to their molecular weights. In order to determine the whole chemical structure of the parent phosphomannan, the acid-stable domain was subjected to acetolysis and then enzymolysis with the Arthrobacter GJM-1 α-mannosidase and the resultant manno-oligosaccharides were investigated for their chemical structures by 1H NMR spectroscopy. The results of a precipitin-inhibition test using the β-1,2-linked manno-oligosaccharides, from biose to hexaose, in comparison with the corresponding isomers containing α-1,2 linkage with small amounts of α-1,3 linkage, indicated that the haptens possessing the former linkage exhibited much higher inhibitory effects than the corresponding isomers containing the latter linkages did. Based on the present findings, a chemical structure of the phosphomannan of this C. albicans strain was proposed.
NCBI PubMed ID: 2181936Journal NLM ID: 0372430Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
Methods: 13C NMR, 1H NMR, FAB-MS, enzymatic digestion, acetolysis, HCl hydrolysis, precipitation assay, methylation assay, precipitin-inhibition test
- Article ID: 6478
Kobayashi H, Shibata N, Suzuki S "Evidence for oligomannosyl residues containing both b-1,2 and a-1,2 linkages as a serotype A-specific epitope(s) in mannans of Candida albicans" -
Infection and Immunity 60 (1992) 2106-2109
In order to identify the branches containing both β-1,2 and α-1,2 linkages as the serotype A-specific epitope(s) in the mannans of Candida albicans, serotype A strains with oligosaccharides constituting the β-1,2 linkage, the α-1,2 linkage, and both the β-1,2 and the α-1,2 linkages were prepared from the mannans of C. albicans serotype A strains (NIH A-207 and J-1012) and tested for their inhibitory effects in the precipitin and slide agglutination assays. The results indicated that two oligosaccharides containing both β-1,2 and α-1,2 linkages, Manp β-1-2Manp α 1-2Manp α 1-2Manp α 1-2Man and Manp β-1-2Manp β-1-2Manp α 1-2Manp α 1-2Manp α 1-2Man, served as epitopes participating in the serotype A specificity of C. albicans strains.
NCBI PubMed ID: 1373405Journal NLM ID: 0246127Publisher: American Society for Microbiology
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
Methods: enzymatic digestion, acetolysis, partial acid degradation
- 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: 8112871Journal NLM ID: 0246127Publisher: 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
- Article ID: 6529
Kobayashi H, Kojimahara T, Takahashi K, Takikawa M, Takahashi SI, Shibata N, Okawa Y, Suzuki S "Structural determination of D-mannans of pathogenic yeasts Candida stellatoidea Type I strains: TIMM 0310 and ATCC 11006 compared to IFO 1397" -
Carbohydrate Research 214 (1991) 131-145
The structures of the cell-wall D-mannans of pathogenic yeasts of Candida stellatoidea Type I strains, IFO 1397, TIMM 0310, and ATCC 11006, were investigated by mild acid and, alkaline hydrolysis, by digestion with the Arthrobacter GJM-1 strain exo-α-D-mannosidase, and by acetolysis. The modified D-mannans and their degradation products were studied by 1H- and 13C-n.m.r. analyses. D-Manno-oligosaccharides released by acid treatment from the parent D-mannans were identified as the homologous β-(1----2)-linked D-manno-oligosaccharides from biose to hexaose, whereas those obtained by alkaline degradation were the homologous α-(1----2)-linked D-mannobiose and D-mannotriose. The acid- and alkali-modified D-mannans lacking 1H-n.m.r. signals above 4.900 p.p.m. [corresponding to β-(1----2)-linked D-mannopyranose units] were acetolyzed with 10:10:1 (v/v) Ac2O-AcOH-H2SO4, and the resultant D-manno-oligosaccharides were also analyzed. It was found that the longest branches of these D-mannans, corresponding to hexaosyl residues, had the following structures: α-D-manp-(1----3)-α-D-manp-(1----2)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man and α-D-manp-(1----2)-α-D-manp-(1----3)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man. These results indicate that the D-mannans of C. stellatoidea Type I strains possess structures in common with the D-mannans of Candida albicans serotype B strain (see ref. 4) containing phosphate-bound β-(1----2)-linked oligo-D-mannosyl residues.
NCBI PubMed ID: 1954627Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan, Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan.
Methods: gel filtration, 13C NMR, 1H NMR, enzymatic digestion, acetolysis, slide-agglutination reaction, acid and alkaline hydrolysis
- Article ID: 6620
Hearn VM, Cole GT, Susuki S "Fungal antigens" -
Book: Structure of antigens (1993) Vol. 8, 211-260
Book NLM ID: 9110063Publisher: Boca Raton: CRC Press
Editors: Van Regenmortel MHV
- Article ID: 6622
Suzuki S "Immunochemical study on mannan, the antigenic polysaccharide of pathogenic yeasts in man of genus Candida" -
Yakugaku Zasshi = Journal of the Pharmaceutical Society of Japan [Japanese] 115 (1995) 280-294
This article accounts for the development of immunochemical studies on the antigenic polysaccharide, mannan, a major antigen of pathogenic yeast in man, genus Candida, in order to determine the chemical structures dominating the serological specificities of the parent cells as follows. 1. The serological classification system of 7 medically important Candida species by detecting 10 antigenic factors, 1, 4, 5, 6, 8, 9, 11, 13, 13b, and 34 the corresponding antisera, established by Tsuchiya and his coworkers is documented. 2. The structural studies of Candida mannans until early 1980s, which did not include any evidence for the presence of β-1,2-linked Man unit, the common constituent of antigenic factors, 5, and 6, are also reviewed. 3. The process of structural identification of antigenic factor 5 residing in the mannans of C. albicans, C. tropicalis, and C. stellatoidea, in the phosphate-bound form of β-1,2 linked mannooligosaccharides, is summarized. 4. The results of structural identification of antigenic factors 4 and 6 in the mannans of the acid-stable domains of C. albicans are summarized as follows: In order to isolate oligosaccharides containing β-1,2 and α-1,6 linkages, a modified acetolysis method under mild conditions was established. By means of this procedure, oligosaccharides corresponding to antigenic factors 4 and 6 were successfully isolated, and their structures determined, subsequently. 5. Furthermore, effects of the alteration of cultivation conditions, carbon source, pH and temperature, on the chemical structure of mannans, especially of decrease and/or loss of densities of antigenic factors, 4, 5 and 6, are documented, because of the significance of these findings as basic concepts for in situ assay of Candida cells by antibody-staining technique in patients' foci.
NCBI PubMed ID: 7541458Journal NLM ID: 0413613Publisher: Tokyo: Nihon Yakugakkai
Institutions: Tohoku College of Pharmacy, Sendai, Japan
- Article ID: 6655
Funayama M, Nishikawa A, Shinoda T, Fukazawa Y "Immunochemical determinant of Candida parapsilosis" -
Carbohydrate Research 117 (1983) 229-239
Acetolysis of Candida parapsilosis cell-wall D-mannan, obtained by alkali extraction and purified as a copper complex, gave six oligosaccharides by Bio-Gel P-2 filtration. Their chemical structure was examined by 1H-n.m.r. spectroscopy, methylation analysis, and partial acid hydrolysis. The structures of the penta- and hexa-saccharide were α-D-manp-(1 leads to 3)-α-D-manp-(1 leads to 2)-α-D-manp-(1 leads to 2)-α-D-manp-(1 leads to 2)-D-Man (M5) and α-D-manp-(1 leads to 2)-α-D-manp-(1 leads to 3)-α-D-manp-(1 leads to 2)-α-D-manp-(1 leads to 2)-α-D-manp-(1 leads to 2)-D-Man (M6), respectively. Inhibition of the oligosaccharides with anti-C. parapsilosis serum and homologous D-mannan indicated that although M5 and M6 exhibited strong inhibitory-activity, M6 was the more effective inhibitor, and suggested that M6 may be the immunodominant or may be responsible for the specificity of C. parapsilosis mannan in the precipitin-reaction system, or both.
NCBI PubMed ID: 6192914Journal NLM ID: 0043535Publisher: Elsevier
Methods: gel filtration, 1H NMR, partial acid hydrolysis, acetylation, acetolysis, methylation analysis, precipitin reaction, optical rotation determination, inhibition reaction
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3. Compound ID: 16638
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp |
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Structure type: oligomer
Trivial name: mannohexaose
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141795,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 6446
Shibata N, Kojima C, Satoh Y, Satoh R, Suzuki A, Kobayashi H, Suzuki S "Structural study of a cell-wall mannan of Saccharomyces kluyveri IFO 1685 strain. Presence of a branched side chain and β-1,2 linkage" -
European Journal of Biochemistry 217 (1993) 1-12
Acetolysis of the cell-wall mannan of Saccharomyces kluyveri under mild conditions, gave fragments with 1-6 mannose residues. The structures of mannopentaose and mannohexaose were determined to be [Formula; see text] respectively, by two-dimensional homonuclear Hartmann-Hahn spectroscopy and a sequential NMR assignment method that combines 1H-13C correlated spectroscopy, relayed coherence transfer spectroscopy, 1H-detected heteronuclear multiple-bond connectivity and methylation analysis. The H1 proton chemical shift of a neighboring α-1,2-linked mannose unit of the 3-O-substituted structure was shifted upfield by the addition of a mannose unit to the adjacent 3-O-substituted unit by an α-1,6 linkage. The characteristic H1--H2-correlated cross-peak of the α-1,3-linked mannose unit substituted by a β-1,2 linkage, β 1-->2Man α 1-->3, in the mannan of S. kluyveri, as also found by two-dimensional homonuclear Hartmann-Hahn spectroscopy in the mannan of Candida guilliermondii, a pathogenic yeast in man.
NCBI PubMed ID: 8223546Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan
Methods: gel filtration, 13C NMR, 1H NMR, enzymatic digestion, acetolysis, methylation analysis
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4. Compound ID: 16713
|
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-D-Man |
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Structure type: oligomer
Trivial name: mannan
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- 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: 8112871Journal NLM ID: 0246127Publisher: 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
- Article ID: 6529
Kobayashi H, Kojimahara T, Takahashi K, Takikawa M, Takahashi SI, Shibata N, Okawa Y, Suzuki S "Structural determination of D-mannans of pathogenic yeasts Candida stellatoidea Type I strains: TIMM 0310 and ATCC 11006 compared to IFO 1397" -
Carbohydrate Research 214 (1991) 131-145
The structures of the cell-wall D-mannans of pathogenic yeasts of Candida stellatoidea Type I strains, IFO 1397, TIMM 0310, and ATCC 11006, were investigated by mild acid and, alkaline hydrolysis, by digestion with the Arthrobacter GJM-1 strain exo-α-D-mannosidase, and by acetolysis. The modified D-mannans and their degradation products were studied by 1H- and 13C-n.m.r. analyses. D-Manno-oligosaccharides released by acid treatment from the parent D-mannans were identified as the homologous β-(1----2)-linked D-manno-oligosaccharides from biose to hexaose, whereas those obtained by alkaline degradation were the homologous α-(1----2)-linked D-mannobiose and D-mannotriose. The acid- and alkali-modified D-mannans lacking 1H-n.m.r. signals above 4.900 p.p.m. [corresponding to β-(1----2)-linked D-mannopyranose units] were acetolyzed with 10:10:1 (v/v) Ac2O-AcOH-H2SO4, and the resultant D-manno-oligosaccharides were also analyzed. It was found that the longest branches of these D-mannans, corresponding to hexaosyl residues, had the following structures: α-D-manp-(1----3)-α-D-manp-(1----2)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man and α-D-manp-(1----2)-α-D-manp-(1----3)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man. These results indicate that the D-mannans of C. stellatoidea Type I strains possess structures in common with the D-mannans of Candida albicans serotype B strain (see ref. 4) containing phosphate-bound β-(1----2)-linked oligo-D-mannosyl residues.
NCBI PubMed ID: 1954627Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan, Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan.
Methods: gel filtration, 13C NMR, 1H NMR, enzymatic digestion, acetolysis, slide-agglutination reaction, acid and alkaline hydrolysis
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5. Compound ID: 16755
|
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
|
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
| |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | |
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | |
| | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | |
| | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | |
| | | | | |
a-D-Manp-(1-2)-+ | | | | | |
| | | | | | |
-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1- |
Show graphically |
Structure type: polymer biological repeating unit
Compound class: N-glycan, O-linked glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,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_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_164174,IEDB_164175,IEDB_164176,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
The structure is contained in the following publication(s):
- Article ID: 6529
Kobayashi H, Kojimahara T, Takahashi K, Takikawa M, Takahashi SI, Shibata N, Okawa Y, Suzuki S "Structural determination of D-mannans of pathogenic yeasts Candida stellatoidea Type I strains: TIMM 0310 and ATCC 11006 compared to IFO 1397" -
Carbohydrate Research 214 (1991) 131-145
The structures of the cell-wall D-mannans of pathogenic yeasts of Candida stellatoidea Type I strains, IFO 1397, TIMM 0310, and ATCC 11006, were investigated by mild acid and, alkaline hydrolysis, by digestion with the Arthrobacter GJM-1 strain exo-α-D-mannosidase, and by acetolysis. The modified D-mannans and their degradation products were studied by 1H- and 13C-n.m.r. analyses. D-Manno-oligosaccharides released by acid treatment from the parent D-mannans were identified as the homologous β-(1----2)-linked D-manno-oligosaccharides from biose to hexaose, whereas those obtained by alkaline degradation were the homologous α-(1----2)-linked D-mannobiose and D-mannotriose. The acid- and alkali-modified D-mannans lacking 1H-n.m.r. signals above 4.900 p.p.m. [corresponding to β-(1----2)-linked D-mannopyranose units] were acetolyzed with 10:10:1 (v/v) Ac2O-AcOH-H2SO4, and the resultant D-manno-oligosaccharides were also analyzed. It was found that the longest branches of these D-mannans, corresponding to hexaosyl residues, had the following structures: α-D-manp-(1----3)-α-D-manp-(1----2)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man and α-D-manp-(1----2)-α-D-manp-(1----3)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man. These results indicate that the D-mannans of C. stellatoidea Type I strains possess structures in common with the D-mannans of Candida albicans serotype B strain (see ref. 4) containing phosphate-bound β-(1----2)-linked oligo-D-mannosyl residues.
NCBI PubMed ID: 1954627Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan, Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan.
Methods: gel filtration, 13C NMR, 1H NMR, enzymatic digestion, acetolysis, slide-agglutination reaction, acid and alkaline hydrolysis
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6. Compound ID: 16759
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
|
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | |
| | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | |
| | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | |
| | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | |
| | | | | |
a-D-Manp-(1-2)-+ | | | | | |
| | | | | | |
-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1- |
Show graphically |
Structure type: polymer biological repeating unit
Compound class: N-glycan, O-linked glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,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_152206,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_164174,IEDB_164175,IEDB_164176,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
The structure is contained in the following publication(s):
- Article ID: 6529
Kobayashi H, Kojimahara T, Takahashi K, Takikawa M, Takahashi SI, Shibata N, Okawa Y, Suzuki S "Structural determination of D-mannans of pathogenic yeasts Candida stellatoidea Type I strains: TIMM 0310 and ATCC 11006 compared to IFO 1397" -
Carbohydrate Research 214 (1991) 131-145
The structures of the cell-wall D-mannans of pathogenic yeasts of Candida stellatoidea Type I strains, IFO 1397, TIMM 0310, and ATCC 11006, were investigated by mild acid and, alkaline hydrolysis, by digestion with the Arthrobacter GJM-1 strain exo-α-D-mannosidase, and by acetolysis. The modified D-mannans and their degradation products were studied by 1H- and 13C-n.m.r. analyses. D-Manno-oligosaccharides released by acid treatment from the parent D-mannans were identified as the homologous β-(1----2)-linked D-manno-oligosaccharides from biose to hexaose, whereas those obtained by alkaline degradation were the homologous α-(1----2)-linked D-mannobiose and D-mannotriose. The acid- and alkali-modified D-mannans lacking 1H-n.m.r. signals above 4.900 p.p.m. [corresponding to β-(1----2)-linked D-mannopyranose units] were acetolyzed with 10:10:1 (v/v) Ac2O-AcOH-H2SO4, and the resultant D-manno-oligosaccharides were also analyzed. It was found that the longest branches of these D-mannans, corresponding to hexaosyl residues, had the following structures: α-D-manp-(1----3)-α-D-manp-(1----2)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man and α-D-manp-(1----2)-α-D-manp-(1----3)-α-D-manp+ ++-(1----2)-α-D-manp- (1----2)-α-D-manp-(1----2)-D-Man. These results indicate that the D-mannans of C. stellatoidea Type I strains possess structures in common with the D-mannans of Candida albicans serotype B strain (see ref. 4) containing phosphate-bound β-(1----2)-linked oligo-D-mannosyl residues.
NCBI PubMed ID: 1954627Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan, Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan.
Methods: gel filtration, 13C NMR, 1H NMR, enzymatic digestion, acetolysis, slide-agglutination reaction, acid and alkaline hydrolysis
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7. Compound ID: 16846
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a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-D-Man |
Show graphically |
Structure type: oligomer
Compound class: factor 4 antigen
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73
The structure is contained in the following publication(s):
- Article ID: 6622
Suzuki S "Immunochemical study on mannan, the antigenic polysaccharide of pathogenic yeasts in man of genus Candida" -
Yakugaku Zasshi = Journal of the Pharmaceutical Society of Japan [Japanese] 115 (1995) 280-294
This article accounts for the development of immunochemical studies on the antigenic polysaccharide, mannan, a major antigen of pathogenic yeast in man, genus Candida, in order to determine the chemical structures dominating the serological specificities of the parent cells as follows. 1. The serological classification system of 7 medically important Candida species by detecting 10 antigenic factors, 1, 4, 5, 6, 8, 9, 11, 13, 13b, and 34 the corresponding antisera, established by Tsuchiya and his coworkers is documented. 2. The structural studies of Candida mannans until early 1980s, which did not include any evidence for the presence of β-1,2-linked Man unit, the common constituent of antigenic factors, 5, and 6, are also reviewed. 3. The process of structural identification of antigenic factor 5 residing in the mannans of C. albicans, C. tropicalis, and C. stellatoidea, in the phosphate-bound form of β-1,2 linked mannooligosaccharides, is summarized. 4. The results of structural identification of antigenic factors 4 and 6 in the mannans of the acid-stable domains of C. albicans are summarized as follows: In order to isolate oligosaccharides containing β-1,2 and α-1,6 linkages, a modified acetolysis method under mild conditions was established. By means of this procedure, oligosaccharides corresponding to antigenic factors 4 and 6 were successfully isolated, and their structures determined, subsequently. 5. Furthermore, effects of the alteration of cultivation conditions, carbon source, pH and temperature, on the chemical structure of mannans, especially of decrease and/or loss of densities of antigenic factors, 4, 5 and 6, are documented, because of the significance of these findings as basic concepts for in situ assay of Candida cells by antibody-staining technique in patients' foci.
NCBI PubMed ID: 7541458Journal NLM ID: 0413613Publisher: Tokyo: Nihon Yakugakkai
Institutions: Tohoku College of Pharmacy, Sendai, Japan
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8. Compound ID: 16958
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | |
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | |
| | | |
a-D-Manp-(1-2)-+ | | | |
| | | | |
{{{-b-D-Manp-(1-2)-}}}/n=1-7/-b-D-Manp-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | |
| | | | |
{{{-a-D-Manp-(1-2)-}}}/n=7/-a-D-Manp-(1-2)-+ | | | | |
| | | | | |
{{{-a-D-Manp-(1-2)-}}}/n=5/-a-D-Manp-(1-2)-+ | | | | | |
| | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-{{{-a-D-Manp-(1-2)-}}}/n=5/-a-D-Manp-(1-2)-+ | | | | | | |
| | | | | | | |
{{{-a-D-Manp-(1-2)-}}}/n=5/-a-D-Manp-(1-2)-+ | | | | | | | |
| | | | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-{{{-a-D-Manp-(1-2)-}}}/n=5/-a-D-Manp-(1-2)-+ | | | | | | | | |
| | | | | | | | | |
{{{-a-D-Manp-(1-2)-}}}/n=5/-a-D-Manp-(1-2)-+ | | | | | | | | | |
| | | | | | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | | | | | | |
| | | | | | | | | | | |
{{{-a-D-Manp-(1-6)-a-D-Manp-(1-6)-+ | | | | | | | | | |
| | | | | | | | | | |
a-D-Manp-(1-6)-+ | | | | | | | | a-D-Manp-(1-2)-+ | | |
| | | | | | | | | | | | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-{{{-a-D-Manp-(1-2)-}}}/n=5/-a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-}}}a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-D-Manp-(1-4)-D-GlcpNAc-(1-4)-D-GlcpNAc-(1--/protein/ |
Show graphically |
Structure type: oligomer
Aglycon: protein
Trivial name: mannan
Contained glycoepitopes: IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,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_143632,IEDB_144983,IEDB_144995,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_1539315,IEDB_164174,IEDB_164175,IEDB_164176,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,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 6680
Jouault T, Delaunoy C, Sendid B, Ajana F, Poulain D "Differential humoral response against alpha- and beta-linked mannose residues associated with tissue invasion by Candida albicans" -
Clinical and Diagnostic Laboratory Immunology 4(3) (1997) 328-333
Candida albicans mannan is the major cell wall antigen that elicits antibodies considered to be of little diagnostic value. It comprises epitopes corresponding to sequences of alpha- and beta-1,2-linked mannose residues. Both types of oligomannosidic epitopes may also be present on the glycosidic portions of other C. albicans molecules, i.e., mannoproteins (MP) (either structural or enzymatic) and glycolipids. The human humoral responses against beta-1,2- and alpha-linked oligomannosides were investigated by C. albicans Western blotting by considering the elective distribution of beta-1,2-oligomannosidic epitopes over a 14- to 18-kDa phospholipomannan (PLM) and the presence of alpha-mannosidic epitopes over heavily glycosylated MP. Western blotting of 51 control sera confirmed the presence of antibodies against C. albicans as a commensal member of the indigenous microflora; an immunoglobulin G (IgG) reactivity linked to enzyme-linked immunosorbent assay mannan signals was found for both PLM (beta-1,2-Man residues) and MP (alpha-Man residues). Despite strong reactivities against mannan and MP, IgG from 21 hospitalized patients with mycological evidence of deep-tissue invasion by C. albicans very significantly failed to react or reacted only faintly with PLM. This downregulation of anti-beta-1,2-oligomannosidic epitopes, associated with tissue invasion by C. albicans, was confirmed in 3 of 4 AIDS patients with extended oroesophageal candidosis. The application of a dissociation procedure proved that the absence of PLM reactivity was not due to the presence of immune complexes. These data provide the first evidence for a qualitative modification of the human antimannan antibody response associated with the C. albicans commensal-pathogenic transition.
NCBI PubMed ID: 9144372Journal NLM ID: 9421292Publisher: Washington, DC: American Society for Microbiology
Correspondence: 101473.2356@CompuServe.COM
Institutions: Unité INSERM 42, Domaine du CERTIA, Villeneuve d'Ascq, France
Methods: serological methods, ELIZA
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9. Compound ID: 17114
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a-D-Manp-(1-2)-+
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/Variants 0/-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
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b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
| |
b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | |
| | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | |
| | | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | |
| | | | |
b-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | |
| | | | | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | |
| | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | | |
| | | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | | | |
| | | | | | | | |
a-D-Manp-(1-2)-+ | | | | | | | | |
| | | | | | | | | |
-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-
/Variants 0/ is:
a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)-- |
Show graphically |
Structure type: structural motif or average structure
Aglycon: inner core (ID 40648)
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_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
The structure is contained in the following publication(s):
- Article ID: 6731
Martínez JP, Gil ML, López-Ribot JL, Chaffin WL "Serologic response to cell wall mannoproteins and proteins of Candida albicans" -
Clinical Microbiology Reviews 11 (1998) 121-141
The cell wall of Candida albicans not only is the structure in which many biological functions essential for the fungal cells reside but also is a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both the carbohydrate and protein moieties are able to trigger immune responses. Although cell-mediated immunity is often considered to be the most important line of defense against candidiasis, cell wall protein and glycoprotein components also elicit a potent humoral response from the host that may include some protective antibodies. Proteins and glycoproteins exposed at the most external layers of the wall structure are involved in several types of interactions of fungal cells with the exocellular environment. Thus, coating of fungal cells with host antibodies has the potential to influence profoundly the host-parasite interaction by affecting antibody-mediated functions such as opsonin-enhanced phagocytosis and blocking the binding activity of fungal adhesins for host ligands. In this review, the various members of the protein and glycoprotein fraction of the C. albicans cell wall that elicit an antibody response in vivo are examined. Although a number of proteins have been shown to stimulate an antibody response, for some of these species the response is not universal. On the other hand, some of the studies demonstrate that certain cell wall antigens and anti-cell wall antibodies may be the basis for developing specific and sensitive serologic tests for the diagnosis of candidasis, particularly the disseminated form. In addition, recent studies have focused on the potential for antibodies to cell wall protein determinants to protect the host against infection. Hence, a better understanding of the humoral response to cell wall antigens of C. albicans may provide the basis for the development of (i) effective procedures for the serodiagnosis of disseminated candidiasis and (ii) novel prophylactic (vaccination) and therapeutic strategies for the management of this type of infection.
Journal NLM ID: 8807282WWW link: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC121378/Publisher: Washington, DC: American Society for Microbiology
Correspondence: jose.pedro.martinez@uv.es
Institutions: Departamento de Microbiología y Ecología, Facultad de Farmacia, Universitat de València, Valencia, Spain, Division of Infectious Diseases, Department of Medicine, The University of Texas Health Sciences Center at San Antonio, San Antonio, Texas, USA, Department of Microbiology and Immunology, Texas Tech University Health Sciences Center, Lubbock, Texas, USA
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10. Compound ID: 17115
|
a-D-Manp-(1-2)-+
|
/Variants 0/-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
|
a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
| |
a-D-Manp-(1-6)-+ | |
| | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | |
| | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | |
| | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | |
| | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | |
| | | | | |
a-D-Manp-(1-2)-+ | | | | | |
| | | | | | |
-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-
/Variants 0/ is:
a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)-- |
Show graphically |
Structure type: structural motif or average structure
Aglycon: inner core (ID 40648)
Contained glycoepitopes: IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,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_143632,IEDB_144983,IEDB_144995,IEDB_144996,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,SB_73
The structure is contained in the following publication(s):
- Article ID: 6731
Martínez JP, Gil ML, López-Ribot JL, Chaffin WL "Serologic response to cell wall mannoproteins and proteins of Candida albicans" -
Clinical Microbiology Reviews 11 (1998) 121-141
The cell wall of Candida albicans not only is the structure in which many biological functions essential for the fungal cells reside but also is a significant source of candidal antigens. The major cell wall components that elicit a response from the host immune system are proteins and glycoproteins, the latter being predominantly mannoproteins. Both the carbohydrate and protein moieties are able to trigger immune responses. Although cell-mediated immunity is often considered to be the most important line of defense against candidiasis, cell wall protein and glycoprotein components also elicit a potent humoral response from the host that may include some protective antibodies. Proteins and glycoproteins exposed at the most external layers of the wall structure are involved in several types of interactions of fungal cells with the exocellular environment. Thus, coating of fungal cells with host antibodies has the potential to influence profoundly the host-parasite interaction by affecting antibody-mediated functions such as opsonin-enhanced phagocytosis and blocking the binding activity of fungal adhesins for host ligands. In this review, the various members of the protein and glycoprotein fraction of the C. albicans cell wall that elicit an antibody response in vivo are examined. Although a number of proteins have been shown to stimulate an antibody response, for some of these species the response is not universal. On the other hand, some of the studies demonstrate that certain cell wall antigens and anti-cell wall antibodies may be the basis for developing specific and sensitive serologic tests for the diagnosis of candidasis, particularly the disseminated form. In addition, recent studies have focused on the potential for antibodies to cell wall protein determinants to protect the host against infection. Hence, a better understanding of the humoral response to cell wall antigens of C. albicans may provide the basis for the development of (i) effective procedures for the serodiagnosis of disseminated candidiasis and (ii) novel prophylactic (vaccination) and therapeutic strategies for the management of this type of infection.
Journal NLM ID: 8807282WWW link: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC121378/Publisher: Washington, DC: American Society for Microbiology
Correspondence: jose.pedro.martinez@uv.es
Institutions: Departamento de Microbiología y Ecología, Facultad de Farmacia, Universitat de València, Valencia, Spain, Division of Infectious Diseases, Department of Medicine, The University of Texas Health Sciences Center at San Antonio, San Antonio, Texas, USA, Department of Microbiology and Immunology, Texas Tech University Health Sciences Center, Lubbock, Texas, USA
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11. Compound ID: 17190
|
Galf-(1-?)-Galf-(1-?)-Galf-(1-?)-b-Galf-(1-5)-Galf-(1-?)-+
|
Man-(1-?)-Man-(1-?)-a-Man-(1-2)-a-Man-(1-2)-a-Man-(1-2)-+ |
| |
Galf-(1-?)-Galf-(1-?)-Galf-(1-?)-b-Galf-(1-5)-Galf-(1-?)-a-Man-(1-6)-a-Man-(1-2)-a-Man-(1-2)-Man-(1-6)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+
|
b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-b-GlcN-(1-4)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ |
| |
Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ | |
| | |
Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-6)-+ | |
| | |
Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ | | |
| | | |
Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-6)-+ | | |
| | | |
Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-+ | | | |
| | | | |
Glc-(1-4)-b-Glc-(1-3)-b-Glc-(1-4)-b-Glc-(1-3)-b-Glc-(1-4)-b-Glc-(1-3)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-b-Glc-(1-3)-b-Glc-(1-3)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc-(1-?)-Glc |
Show graphically |
Structure type: structural motif or average structure
Contained glycoepitopes: IEDB_115576,IEDB_128161,IEDB_130701,IEDB_133966,IEDB_134620,IEDB_134621,IEDB_135614,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1394182,IEDB_1397514,IEDB_140116,IEDB_140628,IEDB_140629,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141806,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_144998,IEDB_146664,IEDB_147452,IEDB_147453,IEDB_147454,IEDB_149137,IEDB_149176,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153755,IEDB_153756,IEDB_1539315,IEDB_158538,IEDB_158555,IEDB_161166,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164479,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_232584,IEDB_232585,IEDB_241101,IEDB_420417,IEDB_420418,IEDB_420419,IEDB_420420,IEDB_420421,IEDB_423115,IEDB_558866,IEDB_558867,IEDB_558868,IEDB_558869,IEDB_742521,IEDB_76933,IEDB_857742,IEDB_857743,IEDB_885812,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77
The structure is contained in the following publication(s):
- Article ID: 6749
Fontaine T, Simenel C, Dubreucq G, Adam O, Delepierre M, Lemoine J, Vorgias CE, Diaquin M, Latge JP "Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall" -
Journal of Biological Chemistry 275 (2000) 27594-27607
Physical and biological properties of the fungal cell wall are determined by the composition and arrangement of the structural polysaccharides. Cell wall polymers of fungi are classically divided into two groups depending on their solubility in hot alkali. We have analyzed the alkali-insoluble fraction of the Aspergillus fumigatus cell wall, which is the fraction believed to be responsible for fungal cell wall rigidity. Using enzymatic digestions with recombinant endo-β-1,3-glucanase and chitinase, fractionation by gel filtration, affinity chromatography with immobilized lectins, and high performance liquid chromatography, several fractions that contained specific interpolysaccharide covalent linkages were isolated. Unique features of the A. fumigatuscell wall are (i) the absence of β-1,6-glucan and (ii) the presence of a linear β-1,3/1,4-glucan, never previously described in fungi. Galactomannan, chitin, and β-1,3-glucan were also found in the alkali-insoluble fraction. The β-1,3-glucan is a branched polymer with 4% of β-1,6 branch points. Chitin, galactomannan, and the linear β-1,3/1,4-glucan were covalently linked to the nonreducing end of β-1,3-glucan side chains. As in Saccharomyces cerevisiae, chitin was linked via a β-1,4 linkage to β-1,3-glucan. The data obtained suggested that the branching of β-1,3-glucan is an early event in the construction of the cell wall, resulting in an increase of potential acceptor sites for chitin, galactomannan, and the linear β-1,3/1,4-glucan.
Publication DOI: 10.1074/jbc.M909975199Journal NLM ID: 2985121RWWW link: http://www.jbc.org/content/275/36/27594.abstractPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: tfontain@pasteur.fr
Institutions: Laboratoire des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Résonance Magnétique Nucléaire, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Chimie Biologique, Universitédes Sciences et Technologie de Lille Flandres-Artois 59655 Villeneuve d'Ascq cedex, France, University of Athens, Department of Biology, Division of Biochemistry and Molecular Biology GR-15701, Athens, Greece
Methods: gel filtration, 13C NMR, 1H NMR, GLC-MS, acid hydrolysis, GLC, mild acid hydrolysis, HPAEC, enzymatic digestion, 15N NMR, acetolysis, TOCSY, methylation analysis, DQF-COSY, MALDI-TOF-MS, phenol-sulfuric acid procedure, Johnson procedure, lectin affinity chromatography, gHSQC-TOCSY
- Article ID: 6762
Bernard M, Latge JP "Aspergillus fumigatus cell wall: composition and biosynthesis" -
Medical Mycology 39 (2001) 9-17
Analysis of the cell wall of Aspergillus fumigatus is guided by obvious biological reasons: the cell wall protects the fungus against the aggressive human defense reactions, it harbours most of the fungal antigens and it represents a potential drug target. This review will discuss our current understanding of the structural organization of the polysaccharides constitutive of the cell wall of A. fumigatus [α and β(1,3)-glucans, chitin, galactomannan, and β(1,3),(1,4)-glucan] and of the enzymes (synthases, transglycosidases, and glycosyl hydrolases) responsible for their biosynthesis and remodelling. Comparative analysis of the cell wall of the conidium and mycelium also provides insights on their respective roles during the pathogenic life of this fungal species.
transferase, cell wall, synthase, hydrolase, Aspergillus fumigatus, conidium, mycelium
Publication DOI: 10.1080/mmy.39.1.9.17Journal NLM ID: 9815835Publisher: Oxford: Oxford University Press
Correspondence: jplatge@pasteur.fr
Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France
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12. Compound ID: 17193
|
a-Man-(1-?)-+ b-Galf-(1-?)-+ b-Galf-(1-?)-+
| | |
b-Galf-(1-?)-a-Man-(1-?)-a-Man-(1-?)-a-Man-(1-?)-a-Man-(1-?)-a-Man-(1-?)-a-Man-(1-?)-a-Man-(1-?)-a-Man-(1-?)-b-Glc-(1-3)-b-Glc-(1-3)-b-Glc-(1-3)-b-Glc-(1-3)-b-Glc |
Show graphically |
Structure type: oligomer
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_134620,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_1394182,IEDB_1397514,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142488,IEDB_143632,IEDB_144983,IEDB_146664,IEDB_147454,IEDB_152206,IEDB_153220,IEDB_153543,IEDB_153756,IEDB_153762,IEDB_153763,IEDB_158555,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_190606,IEDB_241100,IEDB_76933,IEDB_983930,IEDB_983931,SB_136,SB_191,SB_192,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_77
The structure is contained in the following publication(s):
- Article ID: 6749
Fontaine T, Simenel C, Dubreucq G, Adam O, Delepierre M, Lemoine J, Vorgias CE, Diaquin M, Latge JP "Molecular organization of the alkali-insoluble fraction of Aspergillus fumigatus cell wall" -
Journal of Biological Chemistry 275 (2000) 27594-27607
Physical and biological properties of the fungal cell wall are determined by the composition and arrangement of the structural polysaccharides. Cell wall polymers of fungi are classically divided into two groups depending on their solubility in hot alkali. We have analyzed the alkali-insoluble fraction of the Aspergillus fumigatus cell wall, which is the fraction believed to be responsible for fungal cell wall rigidity. Using enzymatic digestions with recombinant endo-β-1,3-glucanase and chitinase, fractionation by gel filtration, affinity chromatography with immobilized lectins, and high performance liquid chromatography, several fractions that contained specific interpolysaccharide covalent linkages were isolated. Unique features of the A. fumigatuscell wall are (i) the absence of β-1,6-glucan and (ii) the presence of a linear β-1,3/1,4-glucan, never previously described in fungi. Galactomannan, chitin, and β-1,3-glucan were also found in the alkali-insoluble fraction. The β-1,3-glucan is a branched polymer with 4% of β-1,6 branch points. Chitin, galactomannan, and the linear β-1,3/1,4-glucan were covalently linked to the nonreducing end of β-1,3-glucan side chains. As in Saccharomyces cerevisiae, chitin was linked via a β-1,4 linkage to β-1,3-glucan. The data obtained suggested that the branching of β-1,3-glucan is an early event in the construction of the cell wall, resulting in an increase of potential acceptor sites for chitin, galactomannan, and the linear β-1,3/1,4-glucan.
Publication DOI: 10.1074/jbc.M909975199Journal NLM ID: 2985121RWWW link: http://www.jbc.org/content/275/36/27594.abstractPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: tfontain@pasteur.fr
Institutions: Laboratoire des Aspergillus, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Résonance Magnétique Nucléaire, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris cedex 15, France, Laboratoire de Chimie Biologique, Universitédes Sciences et Technologie de Lille Flandres-Artois 59655 Villeneuve d'Ascq cedex, France, University of Athens, Department of Biology, Division of Biochemistry and Molecular Biology GR-15701, Athens, Greece
Methods: gel filtration, 13C NMR, 1H NMR, GLC-MS, acid hydrolysis, GLC, mild acid hydrolysis, HPAEC, enzymatic digestion, 15N NMR, acetolysis, TOCSY, methylation analysis, DQF-COSY, MALDI-TOF-MS, phenol-sulfuric acid procedure, Johnson procedure, lectin affinity chromatography, gHSQC-TOCSY
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13. Compound ID: 17223
|
a-D-Manp-(1-2)-+
|
/Variants 0/-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+
|
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
| |
b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | |
| | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | |
| | | |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | |
| | | | |
b-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | |
| | | | | |
a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | |
| | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | | |
| | | | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ | | | | | | | |
| | | | | | | | |
a-D-Manp-(1-2)-+ | | | | | | | | |
| | | | | | | | | |
-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-
/Variants 0/ is:
a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)--
OR (exclusively)
b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-b-D-Manp-(1-2)-a-D-Manp-(1--P--6)-- |
Show graphically |
Structure type: structural motif or average structure
Aglycon: ID 40721
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_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
The structure is contained in the following publication(s):
- Article ID: 6763
Cutler JE "N-glycosylation of yeast, with emphasis on Candida albicans" -
Medical Mycology 39 (2001) 75-86
Fungal cell wall N-linked glycans have been studied most extensively in Saccharomyces cerevisiae and in Candida albicans. The glycans are located on the fungal cell surface in the form of phosphomannoprotein complexes and the amount of glycosylation is influenced both by genetics and environmental factors. The glycans, which are comprised mostly of mannan, are important in fungal-host interactions, as they make first contact with the immune system. Initial N-linked glycosylation events take place in the endoplasmic reticulum and are conserved throughout all eukaryotes, but yeasts are capable of additional glycosylation that may result in a glycan comprised of more than 200 mannose units. In C. albicans, the glycan can be delineated into an inner mannan core, which is similar to mammalian glycoproteins, an α-linked mannan backbone with α-oligomannosyl side chains, and β(1,2)-oligomannosides which are phosphodiester linked to the α-mannan. Both the β-oligomannosides, which make up the acid-labile part of the phosphomannan complex, and α-oligomannosides, which make up the acid-stable part of the complex, serve as adhesins in the attachment of C. albicans yeast cells to host splenic and lymph node macrophages. The β-oligomannosides can induce release of tumour necrosis factor (TNF)-α, and antibodies specific to certain β-oligomannosides enhance host resistance to various forms of candidiasis. The importance of the N-linked glycans in fungal-host interactions provides rationale for further studies, which may well lead to effective immunotherapeutic strategies for prevention and, possibly, treatment of disease.
antibodies, vaccines, cell walls, fungi, N-glycans, mannoproteins, phosphomannoproteins
Publication DOI: 10.1080/mmy.39.1.75.86Journal NLM ID: 9815835Publisher: Oxford: Oxford University Press
Correspondence: jcutler@montana.edu
Institutions: Department of Microbiology, Montana State University, Bozeman 59717, USA.
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14. Compound ID: 17904
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/Variants 0/-+
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?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-a-D-Manp-(1-0)-?%P-6)-?%a-D-Manp-(1-2)-?%a-D-Manp-(1-2)-+
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-6)-a-D-Manp-(1-
/Variants 0/ is:
a-D-Manp-(1-6)-+
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?%a-D-Manp-(1-2)-a-D-Manp-(1-3)-?%a-D-Manp-(1-2)-
OR (exclusively)
?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-?%b-D-Manp-(1-2)-?%a-D-Manp-(1-2)- |
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Structure type: structural motif or average structure
Aglycon: inner core
Trivial name: cell wall mannan
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134620,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_143632,IEDB_144983,IEDB_144995,IEDB_144996,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,SB_73
The structure is contained in the following publication(s):
- Article ID: 6993
Koyama T, Makita M, Shibata N, Okawa Y "Influence of oxidative and osmotic stresses on the structure of the cell wall mannan of Candida albicans serotype A" -
Carbohydrate Research 344(16) (2009) 2195-2200
In this study, we investigated the structural changes in the cell wall mannan of Candida albicans serotype A strain cells cultured under various stress conditions, that is, oxidative stress of 3.5 mM H2O2, osmotic stress of 1.5 M NaCl, and heat stress at 37 °C, compared with the normal condition of 30 °C in yeast extract-added Sabouraud liquid medium (YSLM). Based on the 1H nuclear magnetic resonance (NMR) and fluorophore-assisted carbohydrate electrophoresis (FACE) analyses of the mannans, we showed that the proportion of the terminal β-1,2-linked mannose side chain unit in the mannan increased in the cell proliferation process under both the normal condition and the oxidative stress condition. The osmotic stress induced a slight decrease in the proportion of the β-1,2-linked mannose unit in the acid-labile fraction. The heat stress induced a significant decrease in the proportions of the β-1,2-linked mannose unit in both the acid-labile and acid-stable fractions. Based on these results, we propose that C. albicans significantly changes the mannan structures under various stress conditions and that sufficient attention to the cultural conditions is needed to perform an accurate diagnosis of candidiasis.
structure, Candida albicans, β-1, oxidative stress, Osmotic stress, Cell wall mannan, 2-Linked mannose
NCBI PubMed ID: 19765692Publication DOI: 10.1016/j.carres.2009.08.002Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: okawa@tohoku-pharm.ac.jp (Yoshio Okawa)
Institutions: Department of Infection and Host Defense, Tohoku Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan
Methods: 13C NMR, 1H NMR, composition analysis, FACE, extraction, acid degradation
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15. Compound ID: 17913
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a-D-Manp-(1-6)-+
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?%a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp |
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Structure type: oligomer
Trivial name: mannan
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_134620,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153220,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73
The structure is contained in the following publication(s):
- Article ID: 6997
Karelin AA, Tsvetkov YE, Paulovičová L, Bystricky S, Paulovičová E, Nifantiev NE "Synthesis of 3,6-branched oligomannoside fragments of the mannan from Candida albicans cell wall corresponding to the antigenic factor 4" -
Carbohydrate Research 345(10) (2010) 1283-1290
3-Aminopropyl glycosides of 3,6-branched penta- and hexamannoside fragments of the cell wall mannan from Candida albicans, corresponding to the antigenic factor 4, have been synthesized. Subsequent coupling of both oligosaccharides with BSA using the squarate procedure provided corresponding neoglycoconjugates.
synthesis, mannan, Candida albicans, neoglycoconjugates, Antigenic factor 4, Oligomannosides
NCBI PubMed ID: 20096401Publication DOI: 10.1016/j.carres.2009Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: nen@ioc.ac.ru (Nikolay E. Nifantiev)
Institutions: Laboratory of Glycoconjugate Chemistry, N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Centre of Excellence GLYCOMED, Department of Immunochemistry of Glycoconjugates, Institute of Chemistry, Center for Glycomics, Slovak Academy of Sciences, Bratislava, Slovakia
Methods: 13C NMR, 1H NMR, TLC, MALDI-TOF MS, GPC, HR-ESI-MS
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Next 15 structure(s)
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