Nutritional stress proteins in Candida albicans

Dabrowa, Nina; Zeuthen, Marie L.; Howard, Dexter H.

doi:10.1099/00221287-136-7-1387

Cited by 7 publications

(4 citation statements)

References 23 publications

(29 reference statements)

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“…Initial studies (Dabrowa & Howard, 1984; Zeuthen et al , 1988; Zeuthen & Howard, 1989; Dabrowa et al , 1990) examined the expression of cytoplasmic proteins in response to heat shock, ethanol, nutritional stress and thermotolerance followed by heat shock. Heat shock from 23 to 37°C induced proteins at 18, 22, 40, 68 and 70 kDa (Dabrowa & Howard, 1984).…”

Section: Hsps and Pathogenic Fungimentioning

confidence: 99%

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: 99%

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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“…Proteins responding to stress or heat-shock conditions have been described in Candida albicans (Zeuthen and Howard, 1989;Dabrowa et al, 1990;Howard et al, 1991). Hsps, particularly the members of the hsp70 family, one of the most highly conserved proteins in the cell, are major immunogens during a variety of infections, including candidiasis (Matthews, 1992;Swovoda et al, 1993;Kaufmann and Schoel, 1994).…”

Section: Introductionmentioning

confidence: 99%

Molecular Cloning of a Candida albicans Gene (SSB1) Coding for a Protein Related to the Hsp70 Family

Maneu¹,

Cervera²,

Martinez³

et al. 1997

Yeast

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We have cloned and sequenced a Candida albicans gene (SSB1) encoding a potential member of the heat-shock protein seventy (hsp70) family. The protein encoded by this gene contains 613 amino acids and shows a high degree (85%) of sequence identity to the ssb subfamily (ssb1 and ssb2) of the Saccharomyces cerevisiae hsp70 family. The transcribed mRNA (2·1 kb) is present in similar amounts both in yeast and germ tube cells of C. albicans.

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“…We have named the gene corresponding to clone R SSA2. Proteins responding to heat shock or stress have previously been reported in C. albicans (26,70). Several of these appeared to correspond in size to those associated with the general heat shock response, including a protein of 70 kDa.…”

Section: Discussionmentioning

confidence: 81%

Evidence for presence in the cell wall of Candida albicans of a protein related to the hsp70 family

et al. 1996

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We have previously reported the isolation of several clones from a cDNA expression library from Candida albicans, one of which was associated with a constitutively expressed 70-kDa protein. The moiety was present in the ␤-mercaptoethanol extracts of cell walls from both blastoconidia and germ tubes. The surface expression of this moiety was revealed by an indirect immunofluorescence assay using affinity-purified antibody to the fusion protein produced by the clone. The 0.68-kb cDNA insert was sequenced. A database search revealed extensive homology with the 70-kDa family of stress or heat shock proteins (hsps). The 77% homology with another C. albicans HSP70 sequence suggested that this fragment represented a second member of the HSP70 family in this organism. Homology ranging from 65 to 76% was observed with members of four subfamilies (SSA, SSB, SSC, and SSD) of the Saccharomyces cerevisiae HSP70 gene family. The nucleic acid sequence and the deduced amino acid sequence of the open reading frame showed greatest homology with SSA1 and SSA2 sequences, and the gene corresponding to the cDNA clone was designated C. albicans SSA2. The relationship with the SSA family was supported by reactivity of the 70-kDa component with antibody recognizing the Ssa proteins of S. cerevisiae. The presence of an hsp70 in the cell wall was confirmed by two additional methods. Cell wall proteins were biotinylated with a non-membrane-permeable derivative to distinguish extracellular from cytosolic proteins. Biotinylated hsp70 was detected by Western blotting (immunoblotting) among the biotinylated components affinity purified by chromatography on streptavidin, thereby establishing its presence in the cell wall. Immunoelectron microscopy showed that the 70-kDa component was present at the cell surface as well as the outer surface of the plasma membrane and extended through the cell wall, occasionally appearing to reach the cell surface through channels. Northern (RNA) blot analysis showed that the gene was expressed in yeast cells growing in yeast extract-peptone medium at both 25 and 37؇C and in Lee medium at 25؇C and during formation of germ tubes in Lee medium 37؇C. No obvious increase in the expression level was detected after the temperature shift. Members of the hsp70 family have been reported to be immunoreactive. The fusion protein produced by the cDNA clone was recognized by serum from healthy individuals and patients with candidiasis. Since members of the hsp70 family of eucaryotic proteins are associated with chaperone and translocation functions, in addition to being immunogenic, this protein may play a role in the assembly and function of other cell wall proteins.

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Nutritional stress proteins in Candida albicans

Cited by 7 publications

References 23 publications

Fungal heat-shock proteins in human disease

Fungal heat-shock proteins in human disease

Molecular Cloning of a Candida albicans Gene (SSB1) Coding for a Protein Related to the Hsp70 Family

Evidence for presence in the cell wall of Candida albicans of a protein related to the hsp70 family

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