Phase transition and stage-specific protein synthesis in the dimorphic fungus Paracoccidioides brasiliensis

Silva, Silvana P. da; Felipe, Maria Sueli Soares; Pereira, Maristela; Azevedo, M. O.; Soares, Célia Maria de Almeida

doi:10.1016/s0147-5975(06)80002-2

Cited by 35 publications

(38 citation statements)

References 11 publications

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“…This is an active approach to survive in a changing environment, which simply shift their thallic organization to adapt and thrive in the new conditions. Dimorphism is studied in many fungi, Histoplasma capsulatum [5], blastomyces dermatitidis, and Sporothrix schenckii [6], Ceratocystis ulmi [7], Paracoccidioides brasiliensis [8], Candida albicans [9], Penicillium marneffei [10], Rhizopus oryzae ATCC 20344 [11]. Mucor dimorphism has interested microbiologists since the time of Pasteur [12].…”

Section: Introductionmentioning

confidence: 99%

Effect of Extracellular Factors on Growth and Dimorphism of Rhizopus oryzae with Multiple Enzyme Synthesizing Ability

2011

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Rhizopus oryzae PR7 MTCC 9642 was a dimorphic fungus that showed a regular 90 days cycle of filament (mycelium) to pellet (yeast) transformation through a distinct bottom dwelling intermediate state and the pellets never revert back to filamentous form. Apart from the normal cycle, high temperature (37°C and above) and extreme pH also induced the yeast formation. Among the ions tested, calcium and chloride ions were found to restore the filamentous morphology, even in extreme pH and temperature. Cysteine HCl also played noteworthy role in maintaining mycelial growth even at adverse condition. Immobilized spores showed the appearance of intermediate form instead of typical yeast form even at high temperature. The strain could produce a number of extracellular hydrolytic enzymes like cellulolytic, xylanolytic, pectinolytic and amylolytic enzymes. The pellet and mycelial forms were found to be a better producer of cellulaselignocellulase enzymes and amylolytic enzymes respectively, which might be correlated with their infectivity. Increase in inoculum size, agitation during cultivation, change in carbon and nitrogen source failed to induce mycelial growth in extreme conditions, which might be explained as irreversible change of configuration of protein responsible for mycelial development.

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Section: Introductionmentioning

confidence: 99%

Effect of Extracellular Factors on Growth and Dimorphism of Rhizopus oryzae with Multiple Enzyme Synthesizing Ability

2011

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“…grow as a multicellular saprobic mycelium in the environment and as a unicellular pathogenic yeast in vivo (32,33). During in vitro growth under experimental conditions, phase transitions are triggered when the incubation temperature is shifted from ambient to mammalian body temperature or in the reverse direction (34). The conversion of the inhaled airborne propagules to the yeast form occurs primarily within the lungs (35)(36)(37), and this transition is essential for the establishment of infection (38).…”

Section: Paracoccidioidomycosismentioning

confidence: 99%

Heat Shock Proteins in Histoplasma and Paracoccidioides

Cleare

Zamith-Miranda

Nosanchuk

2017

Clin Vaccine Immunol

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Heat shock proteins (Hsps) are highly conserved biomolecules that are constitutively expressed and generally upregulated in response to various stress conditions (biotic and abiotic). Hsps have diverse functions, categorizations, and classifications. Their adaptive expression in fungi indicates their significance in these diverse species, particularly in dimorphic pathogens. Histoplasma capsulatum and Paracoccidioides species are dimorphic fungi that are the causative agents of histoplasmosis and paracoccidioidomycosis, respectively. This minireview focuses on the pathobiology of Hsps, with particular emphasis on their roles in the morphogenesis and virulence of Histoplasma and Paracoccidioides and the potential roles of active and passive immunization against Hsps in protection against infection with these fungi.

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“…Early work from our laboratory using metabolically labelled cells has led to a group of heat-induced proteins (Silva et al, 1994). Our group also isolated and characterized the genes encoding the heat-induced proteins 70 and 60 (Silva et al, 1999;Salem-Izaac et al, 2001).…”

Section: Introductionmentioning

confidence: 97%