1887

Abstract

Summary

The induction of heat-shock proteins has been postulated to play a role not only in thermo-adaptation, but also in phase transition of the dimorphic fungi. In this study, we used yeast and mycelial forms of the thermally dimorphic fungus to evaluate the effect of temperature on the induction of the heat-shock response. We also evaluated protein synthesis by caused by exposure to low pH and HO. Analysis of protein synthesis by SDS-PAGE disclosed that mycelia increased synthesis of all major constitutive proteins when stressed at 37°C and increased synthesis of three non-constitutive proteins of 134, 82 and 28 kDa at 40°C. Yeasts incubated at 40°C showed decreased synthesis of five constitutive proteins (136, 98, 62, 57 and 54 kDa) and the appearance of three new proteins (134, 82 and 28 kDa). There was a decrease in the synthesis of all major constitutive proteins except for three proteins of 141, 136 and 16 kDa when yeast cells were incubated at 25°C. When stressed by low pH and HO, yeast increased synthesis of one (134 kDa) and five (134, 104, 82, 52 and 40 kDa) non-constitutive proteins, respectively. mycelia and yeast forms disclosed the same profile of protein synthesis when stressed at temperatures that trigger phase transition (37°C for mycelia; 25°C for yeast). The same profile of protein synthesis by both forms occurred when the fungi were incubated at 40°C and was similar to that of yeast cells stressed by low pH or HO, but different from the patterns produced by mycelia incubated at 37°C or yeast at 25°C. These results suggest that synthesis of stress proteins by mycelia and yeast forms at 40°C, low pH or exposed to HO was associated with adaptation to hostile environments. In contrast, the overall increased and decreased synthesis of major constitutive proteins by mycelia and yeast forms at 37°C and 25°C was associated with phase transition. It is unlikely that the heat-shock proteins produced in these experiments are important in the maintenance of the morphology of yeast or mycelia at their usual temperatures of growth.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-40-2-124
1994-02-01
2024-04-18
Loading full text...

Full text loading...

/deliver/fulltext/jmm/40/2/medmicro-40-2-124.html?itemId=/content/journal/jmm/10.1099/00222615-40-2-124&mimeType=html&fmt=ahah

References

  1. Restrepo A. The ecology of Paracoccidioides brasiliensis a puzzle still unsolved. Sabouraudia 1985; 23:323–334
    [Google Scholar]
  2. Medoff G, Painter A, Kobayashi GS. Mycelial- to yeast-phase transitions of the dimorphic fungi Blastomyces dermatitidis and Paraoccidioides brasiliensis . J Bacteriol 1987; 169:4055–4060
    [Google Scholar]
  3. Lathigra RB, Butcher PD, Garbe TR, Young DB. Heat shock proteins as virulence factors of pathogens. Curr Top Microbiol Immunol 1991; 167:125–143
    [Google Scholar]
  4. Sokolovic Z, Goebel W. Synthesis of listeriolysin in Listeria monocytogenes under heat shock conditions. Infect Immun 1989; 57:295–298
    [Google Scholar]
  5. Bienz M, Pelham HRB. Mechanisms of heat-shock gene activation in higher eukaryotes. Adv Genet 1987; 24:31–72
    [Google Scholar]
  6. Bond U, Schlesinger MJ. Heat-shock proteins and development. Adv Genet 1987; 24:1–29
    [Google Scholar]
  7. Akins RA, Lambowitz AM. General method for cloning Neurospora crassa nuclear genes by complementation of mutants. Mol Cell Biol 1985; 5:2272–2278
    [Google Scholar]
  8. Burdon RH. Heat shock and the heat shock proteins. Bioch J 1986; 240:313–324
    [Google Scholar]
  9. Zeuthen ML, Howard DH. Thermotolerance and the heatshock response in Candida albicans . J Gen Microbiol 1989; 135:2509–2518
    [Google Scholar]
  10. Plesofsky-Vig N, Brambl R. Heat shock response in Neurospora crassa protein synthesis and induced thermotolerance. J Bacteriol 1985; 162:1083–1091
    [Google Scholar]
  11. Kamei K, Brummer E, Clemons KV, Stevens DA. Induction of stress protein synthesis in Histoplasma capsulatum by heat, low pH and hydrogen peroxide. J Med Vet Mycol 1992; 30:385–393
    [Google Scholar]
  12. Matthews RC. Candida albicans HSP 90: link between protective and auto immunity. J Med Microbiol 1992; 36:367–370
    [Google Scholar]
  13. San-Blas F, San-Blas G. Bioquimica y dimorfismo en Paracoccidioides brasiliensis . Del Negro G, Lacaz CS, Fiorillo AM. (eds) Paracoccidioidomicose Sao Paulo: Sarvier-Edusp; 198235–57
    [Google Scholar]
  14. Clemons KV, Feldman D, Stevens DA. Influence of oestradiol on protein expression and methionine utilization during morphogenesis of Paracoccidioides brasiliensis . J Gen Microbiol 1989; 135:1607–1617
    [Google Scholar]
  15. Gottesman S. Bacterial regulation : global regulatory networks. Annu Rev Genet 1984; 18:415–441
    [Google Scholar]
  16. Ferreira-da-Cruz MF, Galväo-Castro B, Daniel-Ribeiro C. Isolation and antigenicity of a 45-kilodalton Paracoccidioides brasiliensis immunodominant antigen. Infect Immun 1992; 60:2667–2671
    [Google Scholar]
  17. Puccia R, Travassos LR. 43-kilodalton glycoprotein from Paracoccidioides brasiliensis immunochemical reactions with sera from patients with paracoccidiodomycosis, histo-plasmosis, or Jorge Lobo’s disease. J Clin Microbiol 1991; 29:1610–1615
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-40-2-124
Loading
/content/journal/jmm/10.1099/00222615-40-2-124
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error