Characterization of a chaperone ClpB homologue of<i>Paracoccidioides brasiliensis</i>

Jesuino, Rosália Santos Amorim; Azevedo, M. O.; Felipe, Maria Sueli Soares; Pereira, Maristela; Soares, Célia Maria de Almeida

doi:10.1002/yea.888

Cited by 13 publications

(13 citation statements)

References 48 publications

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“…An hsp100 homologue, termed ClpB, was identified by screening a λ Dash II genomic library with a PCR fragment of 660 bp representing the chitinase gene of Coccidioides immitis . It was 46% identical to the S. cerevisiae homologue and was detected in the yeast phase (Jesuino et al , 2002).…”

Section: Hsps and Pathogenic Fungimentioning

confidence: 95%

Fungal heat-shock proteins in human disease

Burnie¹,

Carter²,

Hodgetts³

et al. 2006

FEMS Microbiol Rev

135

108

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Heat-shock proteins (hsps) have been identified as molecular chaperones conserved between microbes and man and grouped by their molecular mass and high degree of amino acid homology. This article reviews the major hsps of Saccharomyces cerevisiae, their interactions with trehalose, the effect of fermentation and the role of the heat-shock factor. Information derived from this model, as well as from Neurospora crassa and Achlya ambisexualis, helps in understanding the importance of hsps in the pathogenic fungi, Candida albicans, Cryptococcus neoformans, Aspergillus spp., Histoplasma capsulatum, Paracoccidioides brasiliensis, Trichophyton rubrum, Phycomyces blakesleeanus, Fusarium oxysporum, Coccidioides immitis and Pneumocystis jiroveci. This has been matched with proteomic and genomic information examining hsp expression in response to noxious stimuli. Fungal hsp90 has been identified as a target for immunotherapy by a genetically recombinant antibody. The concept of combining this antibody fragment with an antifungal drug for treating life-threatening fungal infection and the potential interactions with human and microbial hsp90 and nitric oxide is discussed.

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Section: Hsps and Pathogenic Fungimentioning

confidence: 95%

Fungal heat-shock proteins in human disease

Burnie¹,

Carter²,

Hodgetts³

et al. 2006

FEMS Microbiol Rev

135

108

View full text Add to dashboard Cite

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“…3C). The amount of RNA was standardized against the ribosomal protein L35 (GenBank AY057112), whose levels were shown to not vary in phases of P. brasiliensis (Jesuino et al, 2002). The regulation of the GAPDH homologue and the cognate transcript was analyzed during the P. brasiliensis differentiation process.…”

Section: Developmental Regulation Of the Pbgapdh Gene And The Cognatementioning

confidence: 99%

The glyceraldehyde-3-phosphate dehydrogenase homologue is differentially regulated in phases of Paracoccidioides brasiliensis: molecular and phylogenetic analysis

Barbosa

Passos

Felipe

et al. 2004

Fungal Genetics and Biology

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“…As other chaperones of the ER, the expression of cnx 1 by S. cerevisiae was induced when cells were subjected to a variety of stress types causing the accumulation of unfolded and aggregated proteins in the ER, such as heat shock protein (Partaledis and Berlin, 1993). In this context, it is proposed that, during heat stress conditions, the accumulation of denatured or aggregated proteins is responsible for the loss of cell viability, reinforcing the importance of molecular chaperones in these events (Jesuíno et al , 2002). Thus, as for S. cerevisiae , these data open perspectives for further study of reassembly of regulatory sequences of the Pb Cnx gene as well as analyses of expression of this gene by heat‐shock treatment.…”

Section: Resultsmentioning

confidence: 99%

Cloning, characterization and expression of a calnexin homologue from the pathogenic fungus Paracoccidioides brasiliensis

Feitosa

Soares

Santos

et al. 2006

Yeast

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We report the cloning of a Paracoccidioides brasiliensis cDNA, here named PbCnx, encoding the homologue of the endoplasmic reticulum molecular chaperone calnexin. Calnexin specifically recognizes monoglucosylated glycoproteins in the endoplasmic reticulum, thus being an essential component of the complex that interacts with the folded state of nascent secreted glycoproteins. The PbCnx open reading frame was found in a 1701 base pair (bp) fragment that encodes a 567 amino acid protein with an estimated mass of 62 680 Da. Northern and Southern blot hybridizations showed that PbCnx is encoded by a single, or a low number of, gene copies. PbCnx contains the hallmark KPEDWD motifs that are found in all members of the calnexin/calreticulin family proteins. A cDNA-encoding PbCnx was overexpressed as recombinant protein in Escherichia coli. The purified recombinant PbCnx was recognized by 6 out of 10 sera from PCM patients, a result that rules out its possible consideration for further use in diagnosis. Using confocal microscopy with anti-PbCnx mouse serum against yeast forms, a cytoplasmic staining pattern was observed.

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Characterization of a chaperone ClpB homologue ofParacoccidioides brasiliensis

Abstract: Abstract

Cited by 13 publications

References 48 publications

Fungal heat-shock proteins in human disease

Fungal heat-shock proteins in human disease

The glyceraldehyde-3-phosphate dehydrogenase homologue is differentially regulated in phases of Paracoccidioides brasiliensis: molecular and phylogenetic analysis

Cloning, characterization and expression of a calnexin homologue from the pathogenic fungus Paracoccidioides brasiliensis

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