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Structure type: oligomer
Compound class: antigen
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_164480,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72

• Article ID: 6460
  Maruyama Y, Nakajima T, Ichishima E "A 1,2-a-D-mannosidase from a Bacillus sp.: purification, characterization, and mode of action" - Carbohydrate Research 251 (1994) 89-98
  

  A 1,2-α-D-mannosidase was purified to homogeneity from the culture supernatant of Bacillus sp. M-90, which was isolated from soil by enrichment culture on baker's yeast mannan. The purified enzyme had M(r) 380,000 Da, and was comprised of two apparently identical 190,000 Da subunits. It had a neutral optimum pH (7.0) and an isoelectric point of 3.6. The enzyme was highly specific for α-1,2-linked D-mannose oligosaccharides. An N-linked high-mannose type oligosaccharide, Man9GlcNAc2, was a good substrate, yielding Man5GlcNAc2, and the α-1,2-linked side chains of Saccharomyces cerevisiae mannan were also specifically hydrolyzed by the enzyme. p-Nitrophenyl α-D-mannopyranoside and 1,2-α-D-mannobiitol were not hydrolyzed at all. Calcium ion, 1-deoxyman-nojirimycin, and swainsonine had no effect on the enzyme, but the activity was completely inhibited by EDTA. The mode of action on α-1,2-linked mannotetraose indicated that the enzyme is an exo-1,2-α-D-mannanase.

  NCBI PubMed ID: 8149382
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai-shi, Japan
  Methods: 1H NMR, SDS-PAGE, HPLC, enzyme assay, enzymatic digestion, gel electrofocusing
  
   
  
  Saccharomyces cerevisiae
  CSDB ID 217564 (all data & tools)
• 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 280515 (all data & tools)