Stress proteins in fungal diseases.
MATTHEWS, R. C. *; MARESCA, B. ; BURNIE, J. P. *; CARDONA, A. [S]; CARRATU, L. +; CONTI, S. [P]; DEEPE, G. S. **; FLOREZ, A. M. [S]; FRANCESCHELLI, S. +; GARCIA, E. [S]; GARGANO, L. S. +; KOBAYASHI, G. S. ++; McEWEN, J. G. [S]; ORTIZ, B. L. [S]; OVIEDO, A. M. [S]; POLONELLI, L. [P]; PONTON, J. ; RESTREPO, A. [S]; STORLAZZI, A. +
[Abstract] Medical Mycology. 36 Supplement 1:45-51, August 1998.

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Heat shock proteins (hsps) are ubiquitous families of proteins, found in all organisms studied so far. They are highly conserved across the species barrier and serve fundamental functions in cell physiology. The term 'heat shock' was adopted because of the early observation of the heat-inducible nature of these proteins, although, as it is now realized that they can be induced by a variety of stressful stimuli, it is probably more appropriate to call them 'stress proteins'. The nomenclature of many hsps, for example hsp90, hsp70 and hsp60, reflects the approximate molecular mass of hsps within each of these families. For many bacterial and parasitic infections, hsps were first recognized as immunodominant antigens on immunoblots of extracts from the organism probed with immune sera, or in T-cell proliferation assays. They have now been identified in a range of fungal pathogens, again often linked to an immune response. In this symposium, we review the association of hsps with humoral immunity to candidosis and aspergillosis, cellular immunity to histoplasmosis, and the identification of hsp70 in another dimorphic fungus, Paracoccidioides brasiliensis. Finally, the crucial role of the membrane in setting the temperature of the heat shock response in yeasts is discussed.

(C) 1998 Blackwell Science Ltd.