Heat Shock Protein 90 (Hsp90) in Fungal Growth and Pathogenesis

Lamoth, Frédéric; Juvvadi, Praveen R.; Steinbach, William J.

doi:10.1007/s12281-014-0195-9

Cited by 9 publications

(6 citation statements)

References 49 publications

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“…In our study, transcripts encoding HSPs were also massively induced at 72 hpi in the L958 interaction ( Table 3 , S2 Fig ). Previous reports have indicated that the HSPs of Candida albicans , Aspergillus fumigatus , and Ustilago maydis are essential for intracellular homeostasis, morphogenesis, growth and stress adaptation, all of which are related to fungal pathogenicity and virulence [ 65 , 66 ]. Similarly, it is implied that some HSPs can enhance the capacity of pathogens to attack and that others can reduce the capacity of host defenses in Bgt .…”

Section: Discussionmentioning

confidence: 99%

Comparative transcriptome profiling of Blumeria graminis f. sp. tritici during compatible and incompatible interactions with sister wheat lines carrying and lacking Pm40

Liang

Zhang

et al. 2018

PLoS ONE

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Blumeria graminis f. sp. tritici (Bgt) is an obligate biotrophic fungus that causes wheat powdery mildew, which is a devastating disease in wheat. However, little is known about the pathogenesis of this fungus, and differences in the pathogenesis of the same pathogen at various resistance levels in hosts have not been determined. In the present study, leaf tissues of both Pm40-expressing hexaploid wheat line L658 and its Pm40-deficient sister line L958 were harvested at 0 (without inoculation), 6, 12, 24, 48 and 72 hours post-inoculation (hpi) with Bgt race 15 and then subjected to RNA sequencing (RNA-seq). In addition, we also observed changes in fungal growth morphology at the aforementioned time points. There was a high correlation between percentage of reads mapped to the Bgt reference genome and biomass of the fungus within the leaf tissue during the growth process. The percentage of mapped reads of Bgt in compatible interactions was significantly higher (at the p<0.05 level) than that of reads in incompatible interactions from 24 to 72 hpi. Further functional annotations indicated that expression levels of genes encoding H+-transporting ATPase, putative secreted effector proteins (PSEPs) and heat shock proteins (HSPs) were significantly up-regulated in compatible interactions compared with these levels in incompatible interactions, particularly at 72 hpi. Moreover, Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis suggested that genes involved in the endocytosis pathway were also enriched in compatible interactions. Overall, genes encoding H+-transporting ATPase, PSEPs and HSPs possibly played crucial roles in successfully establishing the pathogenesis of compatible interactions during late stages of inoculation. The study results also indicated that endocytosis is likely to play a potential role in Bgt in establishing compatible interactions.

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Section: Discussionmentioning

confidence: 99%

Comparative transcriptome profiling of Blumeria graminis f. sp. tritici during compatible and incompatible interactions with sister wheat lines carrying and lacking Pm40

Liang

Zhang

et al. 2018

PLoS ONE

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“…Kingdom Fungi encompass a diverse taxonomy involving filamentous and nonfilamentous fungus, which can be classified on the basis of diversity, morphology, growth and development, reproduction, evolution, ability of causing infection, and toxigenicity [ 1 , 2 ]. Throughout the evolution, fungi have developed diverse mode of reproduction and ability to adapt to their environment [ 3 ]. Mode of feeding is absorption in fungi, for which they adhere or grow within the substrate in the form of hyphae.…”

Section: Introductionmentioning

confidence: 99%

Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi

Tiwari

Thakur

Shankar

2015

Biotechnology Research International

193

130

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Stress (biotic or abiotic) is an unfavourable condition for an organism including fungus. To overcome stress, organism expresses heat-shock proteins (Hsps) or chaperons to perform biological function. Hsps are involved in various routine biological processes such as transcription, translation and posttranslational modifications, protein folding, and aggregation and disaggregation of proteins. Thus, it is important to understand holistic role of Hsps in response to stress and other biological conditions in fungi. Hsp104, Hsp70, and Hsp40 are found predominant in replication and Hsp90 is found in transcriptional and posttranscriptional process. Hsp90 and Hsp70 in combination or alone play a major role in morphogenesis and dimorphism. Heat stress in fungi expresses Hsp60, Hsp90, Hsp104, Hsp30, and Hsp10 proteins, whereas expression of Hsp12 protein was observed in response to cold stress. Hsp30, Hsp70, and Hsp90 proteins showed expression in response to pH stress. Osmotic stress is controlled by small heat-shock proteins and Hsp60. Expression of Hsp104 is observed under high pressure conditions. Out of these heat-shock proteins, Hsp90 has been predicted as a potential antifungal target due to its role in morphogenesis. Thus, current review focuses on role of Hsps in fungi during morphogenesis and various stress conditions (temperature, pH, and osmotic pressure) and in antifungal drug tolerance.

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“…On the other hand, it is known that Hsp90 is conserved from bacteria to eukaryotic cell, and recent works indicate that in fungi Hsps are implicated in several processes, including pathogenicity, phase transition in dimorphic fungi, and antifungal drug resistance. 41 Cowen et al 25 demonstrated that in vitro treatment with geldanamycin, an inhibitor of Hsp90 which interferes with the ATP-binding domain, reduced the emergence of resistance to azoles and echinocandins in human pathogenes such as C. albicans and A. fumigatus . 28 Furthermore, chemical inhibition of Hsp90 resulted in increased susceptibility of T. rubrum to itraconazole and micafungin, and decreased its growth in human nails in vitro.…”

Section: Discussionmentioning

confidence: 99%

Antifungal activity of <em>Cardiospermum halicacabum</em> L. (Sapindaceae) against <em>Trichophyton rubrum</em> occurs through molecular interaction with fungal Hsp90

Gaziano¹,

Campione²,

Iacovelli³

et al. 2018

DDDT

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IntroductionDermatophytosis is a superficial fungal infection limited to the stratum corneum of the epidermis, or to the hair and nails, and constitutes an important public health problem because of its high prevalence and associated morbidity. Dermatophyte fungi, especially 2 species, Trichophyton rubrum and Trichophyton mentagrophytes, are the predominant pathogens. Topical antifungal drugs, mainly azoles or allyamines, are currently used for the treatment of dermatophytoses, although in some cases, such as in nail and hair involvement, systemic treatment is required. However, therapeutic efficacy of current antifungal agents can be limited by their side effects, costs, and the emergence of drug resistance among fungi. Plant extracts represent a potential source of active antimicrobial agents, due to the presence of a variety of chemical bioactive compounds. In the present work, we evaluated in silico and in vitro the antifungal activity of an extract of the medicinal plant Cardiospermum halicacabum against T. rubrum suggesting a potential interaction with Hsp90 as playing an important role in both pathogenicity and drug susceptibility of T. rubrum.MethodsWe investigated in vitro the effect of different concentrations of C. halicacabum (from 500 to 31.25 µg) against a clinical isolate of T. rubrum. Furthermore, using a computational assessment, the interaction between different C. halicacabum active compounds and the fungal Hsp90 was also investigated.ResultsOur results indicate a clear-cut antifungal activity of the total plant extract at the highest concentrations (500 and 250 µg). Among all tested C. halicacabum compounds, the luteolin and rutin molecules have been identified in silico as the most important potential inhibitors of Hsp90. Based on these data, luteolin and rutin were also individually assessed for their antifungal activity. Results demonstrate that both substances display an antifungal effect, even if lower than that of the total plant extract.ConclusionOur data indicate a strong fungistatic effect of C. halicacabum against T. rubrum, suggesting its potential therapeutic efficacy in the treatment of dermatophytoses. Additionally, C. halicacabum compounds, and particularly luteolin and rutin, are all possible Hsp90 interactors, explaining their fungistatic activity.

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Heat Shock Protein 90 (Hsp90) in Fungal Growth and Pathogenesis

Cited by 9 publications

References 49 publications

Comparative transcriptome profiling of Blumeria graminis f. sp. tritici during compatible and incompatible interactions with sister wheat lines carrying and lacking Pm40

Comparative transcriptome profiling of Blumeria graminis f. sp. tritici during compatible and incompatible interactions with sister wheat lines carrying and lacking Pm40

Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi

Antifungal activity of <em>Cardiospermum halicacabum</em> L. (Sapindaceae) against <em>Trichophyton rubrum</em> occurs through molecular interaction with fungal Hsp90

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