Show legend Show as text

Structure type: oligomer
Compound class: blood-group A antigen
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_133966,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164479,IEDB_164480,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6400
  Shibata N, Fukasawa S, Kobayashi H, Tojo M, Yonezu T, Ambo A, Ohkubo Y, Suzuki S "Structural analysis of phospho-D-mannan-protein complexes isolated from yeast and mold form cells of Candida albicans NIH A-207 serotype A strain" - Carbohydrate Research 187 (1989) 239-253
  

  The immunochemical properties between phospho-D-mannan-protein complexes of yeast (Y) and mycelial (M) forms of Candida albicans NIH A-207 (serotype A) strain were compared. Hydrolysis of the Y-form complex gave a mixture of β-(1----2)-linked D-mannooligosaccharides consisting mainly of tri- and tetra-ose, whereas the M-form complex gave preponderantly D-mannose. The antiserum against Y-form cells exhibited a lower reactivity with the M-form than with the Y-form complex, whereas the antiserum to M-form cells could not distinguish significantly between both complexes. Moreover, these acid-modified complexes showed lower antibody-precipitating effect than each corresponding intact complex against antisera of Y- and M-form cells. Digestion of the acid-modified Y- and M-form complexes with the Arthrobacter GJM-1 strain α-D-mannosidase yielded 35- and 40-% degradation products, respectively. Acetolysis of each modified complex under mild conditions gave the same D-mannohexaose, 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. Because the complexes of Y- and M-form cells of C. albicans NIH B-792 (serotype B) strain did not give any hexaose fraction containing β-(1----2) linkages, the presence of this hexaose can be regarded as one of the dominant characteristics of the serotype-A specificity of C. albicans spp.

  NCBI PubMed ID: 2663154
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan
  Methods: 1H NMR, GLC, acetolysis, hot water extraction, fractional precipitation, HCl hydrolysis, antibody-precipitation assay, precipitin-inhibition assay, α-D-mannosidase treatment, methylation analysis (Hakomori method)
  
   
  
  Candida albicans A NIH A-207
  CSDB ID 115627 (all data & tools)
• 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: 1394307
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Japan
  
   
  
  Candida stellatoidea I A3 ATCC 36232, Candida stellatoidea II A2 ATCC 20408
  CSDB ID 116767 (all data & tools)
• 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: 1373405
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
  Methods: enzymatic digestion, acetolysis, partial acid degradation
  
   
  
  Candida albicans A NIH A-207, Candida albicans A NIH J-1012
  CSDB ID 130432 (all data & tools)
• Article ID: 6620
  Hearn VM, Cole GT, Susuki S "Fungal antigens" - Book: Structure of antigens (1993) Vol. 8, 211-260
  
  Book NLM ID: 9110063
  Publisher: Boca Raton: CRC Press
  Editors: Van Regenmortel MHV
  
   
  
  Candida albicans B
  CSDB ID 148629 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: factor 6 antigen
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_76933,IEDB_858578,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6400
  Shibata N, Fukasawa S, Kobayashi H, Tojo M, Yonezu T, Ambo A, Ohkubo Y, Suzuki S "Structural analysis of phospho-D-mannan-protein complexes isolated from yeast and mold form cells of Candida albicans NIH A-207 serotype A strain" - Carbohydrate Research 187 (1989) 239-253
  

  The immunochemical properties between phospho-D-mannan-protein complexes of yeast (Y) and mycelial (M) forms of Candida albicans NIH A-207 (serotype A) strain were compared. Hydrolysis of the Y-form complex gave a mixture of β-(1----2)-linked D-mannooligosaccharides consisting mainly of tri- and tetra-ose, whereas the M-form complex gave preponderantly D-mannose. The antiserum against Y-form cells exhibited a lower reactivity with the M-form than with the Y-form complex, whereas the antiserum to M-form cells could not distinguish significantly between both complexes. Moreover, these acid-modified complexes showed lower antibody-precipitating effect than each corresponding intact complex against antisera of Y- and M-form cells. Digestion of the acid-modified Y- and M-form complexes with the Arthrobacter GJM-1 strain α-D-mannosidase yielded 35- and 40-% degradation products, respectively. Acetolysis of each modified complex under mild conditions gave the same D-mannohexaose, 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. Because the complexes of Y- and M-form cells of C. albicans NIH B-792 (serotype B) strain did not give any hexaose fraction containing β-(1----2) linkages, the presence of this hexaose can be regarded as one of the dominant characteristics of the serotype-A specificity of C. albicans spp.

  NCBI PubMed ID: 2663154
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan
  Methods: 1H NMR, GLC, acetolysis, hot water extraction, fractional precipitation, HCl hydrolysis, antibody-precipitation assay, precipitin-inhibition assay, α-D-mannosidase treatment, methylation analysis (Hakomori method)
  
   
  
  Candida albicans A NIH A-207
  CSDB ID 115628 (all data & tools)
• 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: 1394307
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Japan
  
   
  
  Candida stellatoidea I A3 ATCC 36232, Candida stellatoidea II A2 ATCC 20408
  CSDB ID 216768 (all data & tools)
• 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: 1373405
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
  Methods: enzymatic digestion, acetolysis, partial acid degradation
  
   
  
  Candida albicans A NIH A-207, Candida albicans A NIH J-1012
  CSDB ID 130433 (all data & tools)
• Article ID: 6620
  Hearn VM, Cole GT, Susuki S "Fungal antigens" - Book: Structure of antigens (1993) Vol. 8, 211-260
  
  Book NLM ID: 9110063
  Publisher: Boca Raton: CRC Press
  Editors: Van Regenmortel MHV
  
   
  
  Candida albicans B
  CSDB ID 148631 (all data & tools)
• 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: 7541458
  Journal NLM ID: 0413613
  Publisher: Tokyo: Nihon Yakugakkai
  Institutions: Tohoku College of Pharmacy, Sendai, Japan
  
   
  
  Candida albicans A, Candida glabrata, Candida tropicalis
  CSDB ID 149845 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: mannan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_133966,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164479,IEDB_164480,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• 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: 8223546
  Journal NLM ID: 0107600
  Publisher: 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
  
   
  
  Candida albicans A J-1012
  CSDB ID 124309 (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 44971 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: antigen
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_133966,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164479,IEDB_164480,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6480
  Kobayashi H, Matsuda K, Ikeda T, Suzuki M, Takahashi SI, Suzuki A, Shibata N, Suzuki S "Structures of cell wall mannans of pathogenic Candida tropicalis IFO 0199 and IFO 1647 yeast strains" - Infection and Immunity 62 (1994) 615-622
  

  We conducted a structural analysis of the cell wall mannans isolated from two Candida tropicalis strains, IFO 0199 and IFO 1647, exhibiting strong agglutinabilities against anti-Candida factor sera 5 and 6. The products released from these mannans by acid treatment were identified as the oligosaccharides, from biose to pentaose, consisting solely of β-1,2-linked mannopyranose units corresponding to common epitopes of Candida albicans serotypes A and B (factor 5). Mild acetolysis of acid- and alkali-treated mannans produced large amounts of hexaose and heptaose, Man rho β-1-2Man rho β-1-2Man rho α 1-2Man rho α 1-2Man rho α 1-2Man and Man rho β-1-2Man rho β-1-2Man rho β-1-2Man rho α 1-2 Man rho α 1-2Man, corresponding to the C. albicans serotype A-specific epitopes (factor 6). However, the homologous pentaose, Man rho β-1-2Man rho α 1-2 Man, was not generated by this procedure. The oligosaccharides (biose to hexaose) obtained from the mannans by conventional acetolysis were composed exclusively of α-1,2-linked mannopyranose units. Therefore, the mannans of C. tropicalis IFO 0199 and IFO 1647 do not have the α-1,3-linked mannopyranose units previously observed in the mannans of C. albicans and Candida stellatoidea. The results of this study and previous findings indicate that the similarity of the antigenicities of three Candida species, C. albicans serotype A, C. stellatoidea type II, and C. tropicalis, reside in the β-1,2 and α-1,2 linkages containing oligomannosyl side chain (factor 6) in the cell wall mannan.

  NCBI PubMed ID: 7507898
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
  Methods: 1H NMR, acid hydrolysis, enzymatic digestion, acetolysis, slide agglutination reaction
  
   
  
  Candida tropicalis IFO 0199, Candida tropicalis IFO 1647
  CSDB ID 130511 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: antigen
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_76933,IEDB_858578,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6480
  Kobayashi H, Matsuda K, Ikeda T, Suzuki M, Takahashi SI, Suzuki A, Shibata N, Suzuki S "Structures of cell wall mannans of pathogenic Candida tropicalis IFO 0199 and IFO 1647 yeast strains" - Infection and Immunity 62 (1994) 615-622
  

  We conducted a structural analysis of the cell wall mannans isolated from two Candida tropicalis strains, IFO 0199 and IFO 1647, exhibiting strong agglutinabilities against anti-Candida factor sera 5 and 6. The products released from these mannans by acid treatment were identified as the oligosaccharides, from biose to pentaose, consisting solely of β-1,2-linked mannopyranose units corresponding to common epitopes of Candida albicans serotypes A and B (factor 5). Mild acetolysis of acid- and alkali-treated mannans produced large amounts of hexaose and heptaose, Man rho β-1-2Man rho β-1-2Man rho α 1-2Man rho α 1-2Man rho α 1-2Man and Man rho β-1-2Man rho β-1-2Man rho β-1-2Man rho α 1-2 Man rho α 1-2Man, corresponding to the C. albicans serotype A-specific epitopes (factor 6). However, the homologous pentaose, Man rho β-1-2Man rho α 1-2 Man, was not generated by this procedure. The oligosaccharides (biose to hexaose) obtained from the mannans by conventional acetolysis were composed exclusively of α-1,2-linked mannopyranose units. Therefore, the mannans of C. tropicalis IFO 0199 and IFO 1647 do not have the α-1,3-linked mannopyranose units previously observed in the mannans of C. albicans and Candida stellatoidea. The results of this study and previous findings indicate that the similarity of the antigenicities of three Candida species, C. albicans serotype A, C. stellatoidea type II, and C. tropicalis, reside in the β-1,2 and α-1,2 linkages containing oligomannosyl side chain (factor 6) in the cell wall mannan.

  NCBI PubMed ID: 7507898
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Miyagi, Japan
  Methods: 1H NMR, acid hydrolysis, enzymatic digestion, acetolysis, slide agglutination reaction
  
   
  
  Candida tropicalis IFO 0199, Candida tropicalis IFO 1647
  CSDB ID 130512 (all data & tools)

Show legend Show as text

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

• 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: 8807282
  WWW 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
  
   
  
  Candida albicans A
  CSDB ID 40462 (all data & tools)

Show legend Show as text

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

• 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.M909975199
  Journal NLM ID: 2985121R
  WWW link: http://www.jbc.org/content/275/36/27594.abstract
  Publisher: 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
  
   
  
  Aspergillus fumigatus CBS 144-89
  CSDB ID 40488 (all data & tools)
• 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.39.1.9.17
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: jplatge@pasteur.fr
  Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France
  
   
  
  Aspergillus fumigatus
  CSDB ID 40511 (all data & tools)

Show legend Show as text

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

• 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.39.1.75.86
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: jcutler@montana.edu
  Institutions: Department of Microbiology, Montana State University, Bozeman 59717, USA.
  
   
  
  Candida albicans
  CSDB ID 40512 (all data & tools)

Show legend Show as text

Structure type: homopolymer
Trivial name: mannan
Compound class: EPS
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164177,IEDB_164479,IEDB_164480,IEDB_173895,IEDB_76920,IEDB_76933,IEDB_858578,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6821
  Methacanon P, Madla S, Kirtikara K, Prasitsil M "Structural elucidation of bioactive fungi-derived polymers" - Carbohydrate Polymers 60(2) (2005) 199-203
  

  Chemical composition and molecular structure of exopolysaccharides (EPS) from three strains of fungi, Akanthomyces pistillariiformis BCC2694, Cordyceps dipterigena BCC2073, and Phytocordyceps sp. BCC2744, which can promote the production of IL-8 (a cytokine enhancing wound healing), were elucidated. The results from HPLC after acid hydrolysis revealed that the EPS were mainly composed of glucose indicating the presence of glucan. Galactose, mannose and arabinose were also found as minor monosaccharides. In addition, the protein content in the EPS was determined to be approximately 6–7% with the exception of Phytocordyceps sp. BCC2744 (21%). To identify the linkages between the monosaccharides and the molecular structure of the EPS, methylation followed by reductive cleavage and 13C-NMR analyses were performed. They were shown to be composed of a (1→3)-β-D-glucan backbone substituted at O-6 with side chains of (1→6)-β-D-glucopyranosyl units. The highest branching structure was shown in the EPS from A. pistillariiformis BCC2694, followed by C. dipterigena BCC2073 and Phytocordyceps sp. BCC2744, respectively. Apart from the highly branched at O-6 of (1→3)-β-D-glucan, (1→2) mannan and (1→3) galactan were also found in C. dipterigena BCC2073.

  methylation analysis, Monosaccharide composition, fungal polysaccharides

  Publication DOI: 10.1016/j.carbpol.2004.12.006
  Journal NLM ID: 8307156
  Publisher: Elsevier
  Correspondence: pawadeem@mtec.or.th
  Institutions: National Metal and Materials Technology Center, 114 Thailand Science Park, Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand, National Center for Genetic Engineering and Biotechnology, 113 Thailand Science Park, Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand
  Methods: 13C NMR, methylation, GC-MS, sugar analysis, acid hydrolysis, GC, HPLC, GPC, reductive cleavage
  
   
  
  Cordyceps dipterigena BCC2073
  CSDB ID 41264 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->3) Ser/Thr-protein
Trivial name: O-glycan
Compound class: glycoprotein
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_133966,IEDB_136104,IEDB_137485,IEDB_1394182,IEDB_140116,IEDB_141830,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_152206,IEDB_1539315,IEDB_164479,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6953
  Goto M "Protein O-Glycosylation in Fungi: Diverse Structures and Multiple Functions" - Bioscience, Biotechnology, and Biochemistry 71(6) (2007) 1415-1427
  

  Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation has roles in modulating the function of secretory proteins by enhancing the stability and solubility of the proteins, by affording protection from protease degradation, and by acting as a sorting determinant in yeasts. In filamentous fungi, protein O-glycosylation contributes to proper maintenance of fungal morphology, hyphal development, and differentiation. This review describes recent studies of the structure and function of protein O-glycosylation in industrially and medically important fungi.

  O-glycosylation, Aspergillus, protein O-mannosyltransferase

  NCBI PubMed ID: 17587671
  Publication DOI: 10.1271/bbb.70080
  Journal NLM ID: 9205717
  Publisher: Japan Society for Bioscience, Biotechnology, and Agrochemistry
  Correspondence: m_goto@agr.kyushu-u.ac.jp
  Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Japan
  
   
  
  Pichia pastoris
  CSDB ID 42028 (all data & tools)

Show legend Show as text

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

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

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

  cell wall, glycosylation

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

Show legend Show as text

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

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

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

  cell wall, glycosylation

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

Show legend Show as text

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

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

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

  cell wall, glycosylation

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

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

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

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

  cell wall, glycosylation

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

Show legend Show as text

Structure type: fragment of a bigger structure
Aglycon: ID 43619; link: a1-6 to aDMan(1-3)bDMan fragment in aglycon
Compound class: N-glycan
Contained glycoepitopes: IEDB_128161,IEDB_130701,IEDB_131173,IEDB_133966,IEDB_133967,IEDB_134618,IEDB_134621,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141111,IEDB_141793,IEDB_141795,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_141832,IEDB_141833,IEDB_141834,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144994,IEDB_144995,IEDB_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_76920,IEDB_76933,IEDB_857732,IEDB_857735,IEDB_858578,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72

• Article ID: 7138
  Sheth CC, Hall R, Lewis L, Brown AJ, Odds FC, Erwig LP, Gow NA "Glycosylation status of the C. albicans cell wall affects the efficiency of neutrophil phagocytosis and killing but not cytokine signaling" - Medical Mycology 49(5) (2011) 513-524
  

  The cell wall of the opportunistic human fungal pathogen, Candida albicans is a complex, layered network of rigid structural polysaccharides composed of β-glucans and chitin that is covered with a fibrillar matrix of highly glycosylated mannoproteins. Polymorphonuclear cells (PMNs, neutrophils) are the most prevalent circulating phagocytic leukocyte in peripheral blood and they are pivotal in the clearance of invading fungal cells from tissues. The importance of cell-wall mannans for the recognition and uptake of C. albicans by human PMNs was therefore investigated. N- and O-glycosylation-deficient mutants were attenuated in binding and phagocytosis by PMNs and this was associated with reduced killing of C. albicans yeast cells. No differences were found in the production of the respiratory burst enzyme myeloperoxidase (MPO) and the neutrophil chemokine IL-8 in PMNs exposed to control and glycosylation-deficient C. albicans strains. Thus, the significant decrease in killing of glycan-deficient C. albicans strains by PMNs is a consequence of a marked reduction in phagocytosis rather than changes in the release of inflammatory mediators by PMNs.

  glycosylation, innate immunity, C. albicans, PMN

  NCBI PubMed ID: 21254968
  Publication DOI: 10.3109/13693786.2010.551425
  Journal NLM ID: 9815835
  Publisher: Oxford: Oxford University Press
  Correspondence: Gow NA
  Institutions: The Aberdeen Fungal Group, School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK
  Methods: DNA techniques, flow cytometry analysis, FACS assay
  
   
  
  Candida albicans NGY152
  CSDB ID 43634 (all data & tools)