Isolation and sequencing of the <i>Candida albicans MSI3</i>, a putative novel member of the HSP70 family

Cho, Tamaki; Toyoda, Mika; Sudoh, Masayuki; Nakashima, Yukihiko; Calderone, Richard; Kaminishi, Hidenori

doi:10.1002/yea.952

Cited by 12 publications

(23 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was approximately 28% identical to the Ssa1 and Ssb1 homologues of C. albicans . CaMSI3 complemented a temperature‐sensitive Msi3 mutant of S. cerevisiae (Cho et al , 2003).…”

Section: Hsps and Pathogenic Fungimentioning

confidence: 99%

Fungal heat-shock proteins in human disease

Burnie¹,

Carter²,

Hodgetts³

et al. 2006

FEMS Microbiol Rev

132

108

View full text Add to dashboard Cite

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.

show abstract

“…It was approximately 28% identical to the Ssa1 and Ssb1 homologues of C. albicans . CaMSI3 complemented a temperature‐sensitive Msi3 mutant of S. cerevisiae (Cho et al , 2003).…”

Section: Hsps and Pathogenic Fungimentioning

confidence: 99%

Fungal heat-shock proteins in human disease

Burnie¹,

Carter²,

Hodgetts³

et al. 2006

FEMS Microbiol Rev

132

108

View full text Add to dashboard Cite

show abstract

“…CaMSI3 encodes a putative novel member of the heat shock protein 70 family [13]. Since morphological transition in C. albicans is affected by temperature [17], expression of the five genes described above before and after heat shock was measured in strains JCM9061 and CAI4 (Fig.…”

Section: Effect Of Heat Shock On Gene Expression In Strains Jcm9061 Amentioning

confidence: 99%

Transcriptional profiling of the early stages of germination in by real-time RT-PCR

Toyoda

Cho

Kaminishi

et al. 2004

FEMS Yeast Research

View full text Add to dashboard Cite

By using real-time RT-PCR, we profiled the expression of CGR1, CaMSI3, EFG1, NRG1, and TUP1 in Candida albicans strains JCM9061 and CAI4 under several conditions, including induction of morphological transition, heat shock, and treatment with calcium inhibitors. Expression of CaMSI3 changed under these growth conditions except during heat shock. CGR1 expression increased during the early stages of hyphal growth in JCM9061, while expression was strain-dependent during heat shock. Both EFG1 and NRG1 were similarly expressed under hypha-inducing conditions and heat shock. Expression of TUP1 was slightly different from the expression of EFG1 or NRG1.

show abstract

“…However, the client proteins of S. cerevisiae Sse1p in the cells have not been identified. We previously reported that C. albicans MSI3 can complement the temperature sensitivity of the SSE1-disrupted mutant strain of S. cerevisiae (Cho et al, 2003). However, the role of Msi3p in C. albicans remains to be elucidated, for instance, in terms of the cellular functions that it regulates and whether it functions cooperatively with Hsp90.…”

Section: Introductionmentioning

confidence: 99%

Candida albicans Msi3p, a homolog of the Saccharomyces cerevisiae Sse1p of the Hsp70 family, is involved in cell growth and fluconazole tolerance

et al. 2012

Self Cite

View full text Add to dashboard Cite

We investigated the cellular function of Msi3p, belonging to the heat shock protein 70 family, in Candida albicans. The mutant strain tetMSI3 was generated, in which MSI3 was controlled by a tetracycline-repressive promoter, because there is evidence to suggest that MSI3 is an essential gene. We controlled the MSI3 expression level by doxycycline (DOX) and compared its phenotype with that of a control strain with the tetracycline-repressive promoter and a wild-type copy MSI3. The results indicated that MSI3 was essential for cell growth. In addition, all the tetMSI3-infected mice survived after DOX administration. Drug susceptibility tests indicated that repression of MSI3 expression resulted in hypersensitivity to fluconazole and conferred fungicidal activity to fluconazole. The expression levels of MSI3 and calcineurin-dependent genes were upregulated in response to fluconazole in the control strain. In tetMSI3, the upregulation of MSI3 was lost, and the expression level of the calcineurin-dependent genes was no longer elevated in response to fluconazole and was not affected by DOX, indicating that the upregulation of MSI3 expression was required for the induction of the calcineurin-dependent gene expression. These data suggest that Msi3p confers fluconazole tolerance by partially influencing the calcineurin signaling pathway and also other tolerance mechanisms.

show abstract

Isolation and sequencing of the Candida albicans MSI3, a putative novel member of the HSP70 family

Cited by 12 publications

References 32 publications

Fungal heat-shock proteins in human disease

Fungal heat-shock proteins in human disease

Transcriptional profiling of the early stages of germination in by real-time RT-PCR

Candida albicans Msi3p, a homolog of the Saccharomyces cerevisiae Sse1p of the Hsp70 family, is involved in cell growth and fluconazole tolerance

Contact Info

Product

Resources

About