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 Research187 (1989)
239-253
NCBI PubMed ID:2663154 Journal NLM ID:0043535 Publisher: Elsevier Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan
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.
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) Comments, role: product of acetolysis
Related record ID(s): 104622, 113862, 115627, 115628, 116245, 130428, 130517, 143579 NCBI Taxonomy refs (TaxIDs):5476 Reference(s) to other database(s): GTC:G13237OG, CCSD:9943, CBank-STR:12456 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
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 Research187 (1989)
239-253
The structure was elucidated in this paper NCBI PubMed ID:2663154 Journal NLM ID:0043535 Publisher: Elsevier Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan
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.
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) Comments, role: product of acetolysis
Related record ID(s): 115626, 115628, 116766, 116767, 130432, 148629 NCBI Taxonomy refs (TaxIDs):5476 Reference(s) to other database(s): GTC:G38228VJ, CCSD:50370, CBank-STR:15535 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
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 Research187 (1989)
239-253
NCBI PubMed ID:2663154 Journal NLM ID:0043535 Publisher: Elsevier Institutions: Second Department of Hygienic Chemistry, Tohoku College of Pharmacy, Sendai, Japan
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.
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) Comments, role: product of acetolysis
Related record ID(s): 115626, 115627, 116767, 130433, 148631, 149845, 216768 NCBI Taxonomy refs (TaxIDs):5476 Reference(s) to other database(s): GTC:G90842AG, CCSD:50507, CBank-STR:17069 Show glycosyltransferases
There are 3 chemically distinct structures. Please, select:
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