Heat shock protein 88 and Aspergillus infection

Abstract

Immunoblotting was used to dissect the antibody responses in the sera of 50 patients with proven invasive aspergillosis, 28 patients with suspected invasive aspergillosis, 35 patients with allergic bronchopulmonary aspergillosis, and 10 patients with an aspergilloma. This demonstrated the immunodominance of antigenic bands at 88, 84, 51, and 40 kDa. Monoclonal antibodies against the heat shock protein 90 complexes of Candida albicans and the water mold Achlya ambisexualis identified these four antigenic bands as homologous proteins. Similar antigens have been described in humans, mice, Saccharomyces cerevisiae, chickens, and Drosophila species. The antibody against A. ambisexualis has previously been shown to cross-react with antigens belonging to the human heat shock protein 90 complex. Aspergillus heat shock protein 90 was extracted from the sera of patients with invasive aspergillosis by affinity chromatography. This was done with both a rabbit hyperimmune antiserum raised against an extract of Aspergillus fumigatus NCPF 2109 and a monoclonal antibody against the heat shock protein 90 of C. albicans. In vivo expression of the antigen was demonstrated in an aspergilloma surgically removed from a patient. The role of the antigen as an allergen in allergic bronchopulmonary aspergillosis is also discussed.