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HSP 90, yeasts and Corynebacterium jeikeium
1Department of Medical Microbiology, Manchester University Medical School, UK.
Epidemiology and Infection
|October 1, 1991
Summary
Seroconversion to a Heat Shock Protein (HSP) 90 breakdown product indicates recovery from disseminated candidosis. Researchers identified key epitopes on HSP 90, aiding in understanding its role in Candida albicans infections.
Area of Science:
- Medical Mycology
- Immunology
- Molecular Biology
Background:
- Disseminated candidosis recovery correlates with seroconversion to a specific Heat Shock Protein (HSP) 90 fragment.
- Heat Shock Proteins (HSP) play crucial roles in cellular stress responses and are implicated in various infections.
Purpose of the Study:
- To delineate immunodominant epitopes of Candida albicans HSP 90.
- To investigate the presence and expression of HSP 90 in different Candida albicans phases and related species.
Main Methods:
- Cloning, sequencing, and epitope mapping of Candida albicans HSP 90.
- Utilizing monoclonal and polyclonal antibodies for protein detection.
- Comparative analysis of HSP 90 expression across different fungal and bacterial species.
Main Results:
- Identified immunodominant epitopes: LKVIRKNIVKKMIE and STDEPAGESA.
- Confirmed HSP 90 production in both yeast and mycelial phases of all tested C. albicans strains.
- Detected homologous proteins in Saccharomyces cerevisiae, Candida parapsilosis, and Corynebacterium jeikeium, but not Torulopsis glabrata.
- Provided evidence for two distinct HSP 90 forms in C. albicans: one constitutive and one heat-inducible.
Conclusions:
- The identified HSP 90 epitopes are valuable targets for immunological studies related to candidosis.
- HSP 90 is conserved across several microbial species, suggesting a fundamental biological role.
- Differential expression of HSP 90 in C. albicans highlights its adaptability to environmental stress.