Characterization of Candida antigens by crossed-immunoaffinoelectrophoresis.
The antigens of three Candida albicans strains (3153 A, 3156 B and CBS 1905) and one C. tropicalis strain were studied by means of crossed-immunoaffinoelectrophoresis with the corresponding polyvalent antisera. Most antigens (from 63.8% to 77.7% depending on the strain) were bound to concanavalin A-sepharose and about 20% to blue cibacron-sepharose for all the strains tested. Free concanavalin A, wheat germ lectin-sepharose and Helix pomatia lectin-sepharose revealed differences between C. albicans 3153 A and C. albicans CBS 1905 on the one hand and C. albicans 3156 B and C. tropicalis on the other, since affinity percentages were from 4.2 to 10.2 and from 14.2 to 20.0 respectively. Among 10 previously described species-specific antigens of C. albicans, 4 were never bound and 5 were bound to concanavalin A-sepharose which was considered an unsuitable agent for antigen purification since it retained 77% of C. albicans antigens. One important species-specific antigen was bound to blue cibacron sepharose and the corresponding purification could be undertaken. Similar results were found for 12 species-specific antigens of C. tropicalis. Blue cibacron-sepharose as well as wheat germ lectin or Helix pomatia lectin-sepharose were found suitable agents for purification of some of them.
S M
SM
Bruneau
R M
RM
Guinet
D000915:Antibody Affinity; D000946:Antigens, Fungal / Q000032:analysis*; D002175:Candida / Q000276:immunology*; D002176:Candida albicans / Q000276:immunology*; D000939:Epitopes; D007122:Immunoelectrophoresis / Q000379:methods*; D007123:Immunoelectrophoresis, Two-Dimensional / Q000379:methods*; D037102:Lectins / Q000276:immunology
D000946:Antigens, Fungal; D000939:Epitopes; D037102:Lectins