Induction of stress protein synthesis in Histoplasma capsulatum by heat, low pH and hydrogen peroxide.

It is well known that some micro-organisms synthesize proteins when stressed by heat or other factors. The function of these proteins is not yet clear, but some of them are believed to be related to resistance against a hostile environment. Histoplasma capsulatum is an intracellular pathogenic fungus that multiplies inside macrophages and resists macrophage microbicidal mechanisms. To study the defense mechanisms of H. capsulatum and mimic the hostile environment the fungus may encounter during infection, we investigated protein synthesis by H. capsulatum (isolate G217B) when stressed by heat (40 degrees C), low pH (pH 4), or oxidative products (H2O2) using [35S]-methionine labelling. Analysis of cytosol proteins by SDS-PAGE and fluorography disclosed that H. capsulatum increased synthesis of six constitutive proteins and decreased synthesis of six proteins when stressed at 40 degrees C. When stressed by pH 4 or H2O2, H. capsulatum increased the synthesis of eight and five constitutive proteins, respectively, and decreased the synthesis of three proteins. Estimation of superoxide dismutase (SOD) and catalase enzymatic activity in cytosols from stressed H. capsulatum did not reveal an increase of these enzymatic activities compared to cytosols from non-stressed H. capsulatum. These results suggest that H. capsulatum increases the synthesis of some constitutive proteins when stressed by heat, low pH or H2O2, which might relate to pathogenicity, and are thus worthy of further study. These induced proteins are apparently different from SOD or catalase.