Production and characterization of monoclonal antibodies against secretory proteinase of Candida albicans CBS 2730.
We describe the production and characterization of three murine monoclonal antibodies (M1-M3) which are directed against different epitopes of the secretory aspartic proteinase of Candida albicans CBS 2730. All antibodies belonged to the IgM class, and they recognized denatured enzyme. Only antibody M1 was capable to react with the active proteinase. Differential reactivity was also observed with a large fragment of the proteinase of C. albicans. All antibodies recognized the corresponding proteinase of C. tropicalis 293 both in the active, and in the denatured state. Denatured porcine pepsin was also recognized by all three antibodies. However, active pepsin was recognized only by antibodies M1 and M2. The antibodies did not inhibit enzymatic activity, and they were not suited for immunofluorescence detection of proteinase on fungal cells. However, employing Western blot analysis, proteinase antigen was detected by antibody M 1 in the serum of a patient suffering from candidal pneumonia. The circulating proteinase antigen was found to be bound to patient's IgM. Implications for the use of monoclonal antibodies in the serodiagnosis of candidosis, and first experiences with other monoclonal anti-proteinase antibodies are discussed.
Borg
M
M
Institute of Hygiene, University of Göttingen, Federal Republic of Germany.
Watters
D
D
Reich
B
B
Rüchel
R
R
D000911:Antibodies, Monoclonal / Q000302:isolation & purification; D000936:Antigen-Antibody Complex; D002176:Candida albicans / Q000201:enzymology*; D007124:Immunoenzyme Techniques; D007075:Immunoglobulin M; D010447:Peptide Hydrolases / Q000032:analysis* / Q000276:immunology
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D007075:Immunoglobulin M; D010447:Peptide Hydrolases