Identification and immunochemical characterization of a germ tube specific antigen of Candida albicans

Germ tube specific fractions of the dimorphic pathogenic fungus Candida albicans were fractionated according to their ability to link fibrinogen. These fibrinogen binding factors were used as immunogens to prepare monoclonal antibodies (mAbs) with BALB/c mice. Among the resulting mAbs, one (mAb 3D9....

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Published in:FEMS immunology and medical microbiology 1993-08, Vol.7 (2), p.175-186
Main Authors: Marot‐Leblond, Agnès, Robert, Raymond, Aubry, Jacques, Ezcurra, Pilar, Senet, Jean‐Marcel
Format: Article
Language:English
Subjects:
Animals
Antibodies, immunoglobulins
Antibodies, Monoclonal - isolation & purification
Antigen
Antigens, Fungal - immunology
Antigens, Fungal - isolation & purification
Biological and medical sciences
Candida albicans
Candida albicans - growth & development
Candida albicans - immunology
Cell wall
Female
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Germ tube
Humans
Immunoblotting
Mice
Mice, Inbred BALB C
Molecular immunology
Monoclonal antibodies
Monoclonal antibody
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Summary:Germ tube specific fractions of the dimorphic pathogenic fungus Candida albicans were fractionated according to their ability to link fibrinogen. These fibrinogen binding factors were used as immunogens to prepare monoclonal antibodies (mAbs) with BALB/c mice. Among the resulting mAbs, one (mAb 3D9.3) was shown by indirect immunofluorescence to be specific to the surface of the mycelial phase of the C. albicans species. No labelling of the cell wall of any other Candida species was observed. This morphological shape specificity was confirmed by immunoblotting where a polydispersed high molecular mass component was identified. The molecular mass varied with the extraction procedure used; over 210 kDa with EDTA‐2ME treatment, and ranging from 110 to 220 kDa after Zymolyase digestion. This phase‐specific epitope was sensitive to proteolysis with pronase E, proteinase K and trypsin, but not to periodate treatment. Further purification of this material would allow further development of new serodiagnostic assays that might be more specific for invasive disease than currently available tests.
ISSN:0928-8244
1574-695X
DOI:10.1111/j.1574-695X.1993.tb00397.x