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Structural analysis of phospho-d-mannan-protein complexes isolated from yeast and mold form cells of Candida albicans NIH A-207 serotype a strain

✍ Scribed by Nobuyuki Shibata; Shigeyuki Fukasawa; Hidemitsu Kobayashi; Minehiro Tojo; Toshio Yonezu; Akihiro Ambo; Yasuhito Ohkubo; Shigeo Suzuki


Publisher
Elsevier Science
Year
1989
Tongue
English
Weight
977 KB
Volume
187
Category
Article
ISSN
0008-6215

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✦ Synopsis


The immunochemical properties between phospho-D-mannan-protein complexes of yeast (Y) and mycelial (M) forms of Candida ulbicans NIH A-207 (serotype A) strain were compared. Hydrolysis of the Y-form complex gave a mixture of P-(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 Artkrobacter GJM-1 strain cr-D-mannosidase yielded 35 and 40-% degradation products, respectively. Acetolysis of each modified complex under mild conditions gave the same D-mannohexaose, P-D-Manp-(1+2)+ D-Manp-(l~2)-a-D-Manp-(l~2)-a-DManp-(l~2)-~-D-Ma~-(l~2)-D-Man. Because the complexes of Y-and M-form cells of C. ulbicuns NIH B-792 (serotype B) strain did not give any hexaose fraction containing p-(1+2) linkages, the presence of this hexaose can be regarded as one of the dominant characteristics of the serotype-A specificity of C. ulbicuns spp. /?-LINKAGE-CONTAINING MANNOOLIGOSACCH.4RIDES OF c. albicuns D-MANNAN