Affiliation:
1. School of Biomedical Sciences, Curtin University of Technology, Bentley, Perth, Australia.
Abstract
Reported targets of the specific immune responses to Candida albicans in human candidiasis include a 47-kDa breakdown product of a 90-kDa heat shock protein (HSP 90) (R. Matthews and J. Burnie, FEMS Microbiol. Lett. 60:25-30, 1989) and the 48-kDa enolase (K.M. Franklyn, J.R. Warmington, A.K. Ott, and R.B. Ashman, Immunol. Cell Biol. 68:173-178, 1990). These proteins are immunodominant antigens of C. albicans. Western blotting (immunoblotting) and immunoprecipitation were used to investigate the humoral response in a mouse model of systemic candidiasis. Resolution of systemic candidiasis in CBA/H mice is associated with a high level of antibody reactivity to C. albicans antigens. A significant antibody response against a non-HSP antigen of 96 kDa which was distinct from the C. albicans HSP 90 antigen was detected. Significant antibody reactivity against an HSP of 75 kDa was also detected. We concluded that resolution of C. albicans infections in CBA/H mice was associated with antibodies to an HSP and a non-HSP of 75 and 96 kDa, respectively.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
21 articles.
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