Expression of Hsp60 and its cell location in Paracoccidioides brasiliensis

Fernandes, Fabrício Freitas; Pitangui, Nayla de Souza; Peron, Gabriela; Valim, Clarissa Xavier Resende; Mazucato, Vivian Marino; Oliveira, Alberto de; Silva, Thiago Aparecido da; Roque-Barreira, Maria-Cristina; Panunto-Castelo, Ademílson

doi:10.1590/s1678-9946202062029

Cited by 2 publications

(3 citation statements)

References 18 publications

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“…The expression patterns of S. schenckii HSP60, named upregulation in yeast-like cells and fungal cells co-incubated with human cells, agreed with previous observations in Aspergillus fumigatus, Aspergillus terreus, Scedosporium apiospemum, C. albicans, Penicillium chrysogenum, P. brasiliensis, and Trichophyton mentagrophytes, where exposure to high temperatures caused an HSP60 temperature-dependent upregulation [38,86].…”

Section: Discussionsupporting

confidence: 89%

“…Members of the Hsp60 family, also called mitochondrial chaperones, assist in the refolding of denatured proteins under stress conditions, as well as in the folding of newly synthesized proteins and as a transporter of proteins targeted to different cellular compartments, and are preferentially found in the mitochondria and cytoplasm [82,83]. In addition to these canonical functions, members of the Hsp60 family of proteins were also reported to be highly immunogenic in different pathogenic organisms, including H. capsulatum [36], P. brasiliensis, and Paracoccidioides lutzii [84,85], and were also localized within the fungal cell wall [38].…”

Section: Discussionmentioning

confidence: 99%

“…Some intracellular proteins are found on the cell surface of pathogenic fungi, such as Candida spp. [32][33][34][35], Histoplasma capsulatum [36,37], Paracoccidioides brasiliensis [38], and Cryptococcus neoformans [39]. These moonlighting proteins usually have housekeeping functions inside the cell [40] but are thought to be transported to the cell wall through nonclassical secretion routes, such as vesicular transport [41] and post-translational translocation, where they can participate as virulence factors [42].…”

Section: Introductionmentioning

confidence: 99%

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The Heat Shock Protein 60 and Pap1 Participate in the Sporothrix schenckii-Host Interaction

García-Carnero

Salinas-Marín

Lozoya-Pérez

et al. 2021

JoF

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Sporothrixschenckii is one of the etiological agents of sporotrichosis, a worldwide-distributed subcutaneous mycosis. Its cell wall contains a glycoconjugate composed of rhamnose, mannose, glucuronic acid, and proteins, named peptidorhamnomannan, which harbors important Sporothrix-specific immunogenic epitopes. Although the peptidorhamnomannan carbohydrate moiety has been extensively studied, thus far, little is known about the protein core. Here, using LC-MS/MS, we analyzed the S.schenckii peptidorhamnomannan peptide fraction and generated mass signals of 325 proteins, most of them likely to be moonlighting proteins. Among the identified proteins, chaperonin GroEL/Hsp60 and the uncharacterized protein Pap1 were selected for further analysis. Both proteins were heterologously expressed in bacteria, and they showed adhesive properties to the extracellular matrix proteins laminin, elastin, fibrinogen, and fibronectin, although Pap1 also was bound to type-I and type-II collagen. The inoculation of concentrations higher than 40 μg of these proteins, separately, increased immune effectors in the hemolymph of Galleriamellonella larvae and protected animals from an S.schenckii lethal challenge. These observations were confirmed when yeast-like cells, pre-incubated with anti-rHsp60 or anti-rPap1 antibodies were used to inoculate larvae. The animals inoculated with pretreated cells showed increased survival rates when compared to the control groups. In conclusion, we report that Hsp60 and Pap1 are part of the cell wall peptidorhamnomannan, can bind extracellular matrix components, and contribute to the S.schenckii virulence. To our knowledge, this is the first report about moonlighting protein in the S.schenckii cell wall with an important role during the pathogen–host interaction.

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Heat Shock Protein 60 and Pap1 Participate in the Sporothrix schenckii-Host Interaction

García-Carnero

Salinas-Marín

Lozoya-Pérez

et al. 2021

JoF

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Insights and Perspectives on the Role of Proteostasis and Heat Shock Proteins in Fungal Infections

Neves-da-Rocha,

Santos-Saboya,

Lopes

et al. 2023

Microorganisms

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Fungi are a diverse group of eukaryotic organisms that infect humans, animals, and plants. To successfully colonize their hosts, pathogenic fungi must continuously adapt to the host’s unique environment, e.g., changes in temperature, pH, and nutrient availability. Appropriate protein folding, assembly, and degradation are essential for maintaining cellular homeostasis and survival under stressful conditions. Therefore, the regulation of proteostasis is crucial for fungal pathogenesis. The heat shock response (HSR) is one of the most important cellular mechanisms for maintaining proteostasis. It is activated by various stresses and regulates the activity of heat shock proteins (HSPs). As molecular chaperones, HSPs participate in the proteostatic network to control cellular protein levels by affecting their conformation, location, and degradation. In recent years, a growing body of evidence has highlighted the crucial yet understudied role of stress response circuits in fungal infections. This review explores the role of protein homeostasis and HSPs in fungal pathogenicity, including their contributions to virulence and host–pathogen interactions, as well as the concerted effects between HSPs and the main proteostasis circuits in the cell. Furthermore, we discuss perspectives in the field and the potential for targeting the components of these circuits to develop novel antifungal therapies.

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Expression of Hsp60 and its cell location in Paracoccidioides brasiliensis

Abstract: This is an open-access article distributed under the terms of the Creative Commons Attribution License.

Cited by 2 publications

References 18 publications

The Heat Shock Protein 60 and Pap1 Participate in the Sporothrix schenckii-Host Interaction

The Heat Shock Protein 60 and Pap1 Participate in the Sporothrix schenckii-Host Interaction

Insights and Perspectives on the Role of Proteostasis and Heat Shock Proteins in Fungal Infections

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