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fungi Hsp

Nilce M Martinez-Rossi, Tiago R Jacob, Pablo R Sanches, Nalu T A Peres, Elza A S Lang, Maíra P Martins, Antonio Rossi
Heat shock proteins (HSPs) are proteins whose transcription responds rapidly to temperature shifts. They constitute a family of molecular chaperones, involved in the proper folding and stabilisation of proteins under physiological and adverse conditions. HSPs also assist in the protection and recovery of cells exposed to a variety of stressful conditions, including heat. The role of HSPs extends beyond chaperoning proteins, as they also participate in diverse cellular functions, such as the assembly of macromolecular complexes, protein transport and sorting, dissociation of denatured protein aggregates, cell cycle control, and programmed cell death...
April 2016: Current Genomics
Xue Zhang, Ang Ren, Meng-Jiao Li, Peng-Fei Cao, Tian-Xi Chen, Guang Zhang, Liang Shi, Ai-Liang Jiang, Ming-Wen Zhao
UNLABELLED: Heat stress (HS) influences the growth and development of organisms. Thus, a comprehensive understanding of how organisms sense HS and respond to it is required. Ganoderma lucidum, a higher basidiomycete with bioactive secondary metabolites, has become a potential model system due to the complete sequencing of its genome, transgenic systems, and reliable reverse genetic tools. In this study, we found that HS inhibited mycelium growth, reduced hyphal branching, and induced the accumulation of ganoderic acid biosynthesis and heat shock proteins (HSPs) in G...
July 15, 2016: Applied and Environmental Microbiology
Tiago R Jacob, Nalu T A Peres, Maíra P Martins, Elza A S Lang, Pablo R Sanches, Antonio Rossi, Nilce M Martinez-Rossi
Treatment of fungal infections is difficult due to several reasons, such as side effects of drugs, emergence of resistant strains, and limited number of molecular targets for the drug compounds. In fungi, heat shock proteins (Hsps) have been implicated in several processes with the conserved molecular chaperone Hsp90 emerging as a potential target for antifungal therapy. It plays key cellular roles by eliciting molecular response to environmental changes, morphogenesis, antifungal resistance, and fungal pathogenicity...
2015: Frontiers in Microbiology
M R van Leeuwen, T T Wyatt, T M van Doorn, L G Lugones, H A B Wösten, J Dijksterhuis
Hydrophilins are proteins that occur in all domains of life and protect cells and organisms against drought and other stresses. They include most of the late embryogenesis abundant (LEA) proteins and the heat shock protein (HSP) Hsp12. Here, the role of a predicted LEA-like protein (LeamA) and two Hsp12 proteins (Hsp12A and Hsp12B) of Neosartorya fischeri was studied. This filamentous fungus forms ascospores that belong to the most stress-resistant eukaryotic cells described to date. Heterologous expression of LeamA, Hsp12A and Hsp12B resulted in increased tolerance against salt and osmotic stress in Escherichia coli...
February 2016: Environmental Microbiology Reports
Carolina P Silveira, Alicia C Piffer, Lívia Kmetzsch, Fernanda L Fonseca, Danielle A Soares, Charley C Staats, Marcio L Rodrigues, Augusto Schrank, Marilene H Vainstein
The pathogenic yeast Cryptococcus neoformans secretes numerous proteins, such as heat shock proteins, by unconventional mechanisms during its interaction with host cells. Hsp70 is a conserved chaperone that plays important roles in various cellular processes, including the interaction of fungi with host immune cells. Here, we report that sera from individuals with cryptococcosis infection recognize a recombinant C. neoformans Hsp70 (Cn_rHsp70). Moreover, immunofluorescence assays using antibodies against Cn_rHsp70 revealed the localization of this protein at the cell surface mainly in association with the capsular network...
November 2013: Fungal Genetics and Biology: FG & B
Dianne Grunes, Mary Beth Beasley
Hypersensitivity pneumonitis (HSP) is a poorly understood entity typically caused by exposure to an inciting antigen such as fungi, thermophilic bacteria or animal protein. Clinically, HSP is often divided into acute, subacute and chronic forms. While the subacute form is best described from a pathologic standpoint, the pathology of chronic HSP has only been critically evaluated in the past decade and the pathology of acute HSP is poorly described. The aim of this review is to summarise the current knowledge of pathogenetic theories of HSP and to review the current knowledge of the pathology of each stage of HSP and the main entities in the differential diagnosis...
October 2013: Journal of Clinical Pathology
Bruno H R Barros, Sérgio H da Silva, Everaldo Dos Reis dos ReisMarques, José C Rosa, Ana Patrícia Yatsuda, Donald W Roberts, Gilberto U L Braga
Metarhizium spp. is an important worldwide group of entomopathogenic fungi used as an interesting alternative to chemical insecticides in programs of agricultural pest and disease vector control. Metarhizium conidia are important in fungal propagation and also are responsible for host infection. Despite their importance, several aspects of conidial biology, including their proteome, are still unknown. We have established conidial and mycelial proteome reference maps for Metarhizium acridum using two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption/ionization-time of flight-mass spectrometry (MALDI-TOF MS)...
July 2010: Fungal Biology
Reinhard B Raggam, Helmut J F Salzer, Egon Marth, Bettina Heiling, Astrid H Paulitsch, Walter Buzina
Heat shock proteins (Hsp) are highly conserved molecules, which are both constitutively expressed and up-regulated in response to various stress conditions. In particular, fungal Hsp60 can act as immunodominant antigens and facilitate powerful immunological properties. A possible cellular heat shock response was investigated in eight fungi (Aspergillus fumigatus, Aspergillus terreus, Penicillium chrysogenum, Cladosporium cladosporioides, Scedosporium apiospermum, Trichophyton mentagrophytes, Candida albicans and Saccharomyces cerevisiae)...
September 2011: Mycoses
Guillaume F Bouvet, Volker Jacobi, Karine V Plourde, Louis Bernier
The mobility of transposable elements (TEs) can contribute to genome plasticity, under- or over-expression of genes and ectopic recombination. The data collected in this study provide evidence of stress-induced mobility of OPHIO1 and OPHIO2 transposons, recently detected in Ophiostoma ulmi and O. novo-ulmi, the causal agents of Dutch elm disease (DED). The analyses of OPHIO UTRs and TIRs indicated the presence of two potential binding site motifs and a heat shock protein (hsp) promoter which could be involved in the mobility of OPHIO1 following a heat shock stress...
April 2008: Fungal Genetics and Biology: FG & B
Agnieszka Maciejewska
The genus Paramecium has been known to science for 250 years and contains some of the most widely studied species of ciliates. At present, the basic research object for phylogenetic studies is the genome of various paramecia. One of the most widely used markers are genes coding for various rRNA's. Comparative analyses of sequences coding rRNA were applied for resolving the systematic position of some paramecia species and also for the establishment of an accurate taxonomy of Paramecium. Paramecia were also model organisms for their systematic group in more general studies in a comparative analysis among ciliates, fungi, plants and multicellular animals, illustrating the evolutionary relationships between Archaebacteria and Eucaryota...
2007: Folia Biologica (Krakow)
J Miersch, K Grancharov
Induction of heat shock protein (Hsp) 70 and distinct metallothionein-like proteins (MTLPs) in response to Cd and heat treatment were studied in two strains of the aquatic hyphomycete Heliscus lugdunensis: Hl-H4, isolated from a heavy metal polluted site, and Hl-BB taken from an unpolluted area. Upon Cd-exposure, Hsp70 was actively synthesized in the strain Hl-H4, and to a much lower degree in the strain Hl-BB. The Hsp70-expression was time- and dose-dependent, reaching a maximum after 24 h incubation with 80 microM Cd...
February 2008: Amino Acids
Vijay Gadkar, Matthias C Rillig
Work on glomalin-related soil protein produced by arbuscular mycorrhizal (AM) fungi (AMF) has been limited because of the unknown identity of the protein. A protein band cross-reactive with the glomalin-specific antibody MAb32B11 from the AM fungus Glomus intraradices was partially sequenced using tandem liquid chromatography-mass spectrometry. A 17 amino acid sequence showing similarity to heat shock protein 60 (hsp 60) was obtained. Based on degenerate PCR, a full-length cDNA of 1773 bp length encoding the hsp 60 gene was isolated from a G...
October 2006: FEMS Microbiology Letters
James P Burnie, Tracey L Carter, Samantha J Hodgetts, Ruth C Matthews
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...
January 2006: FEMS Microbiology Reviews
Ruibo Wang, Joseph T Kovalchin, Peggy Muhlenkamp, Rajiv Y Chandawarkar
The extracellular presence of endotoxin-free heat shock protein 70 (HSP70) enhances the rate and capacity of macrophage-mediated phagocytosis at 6 times the basal rate. It is protein-specific, dose- and time-dependent and involves the internalization of inert microspheres, Gram-positive and -negative bacteria and fungi. Structurally, exogenous HSP70 binds the macrophage plasma membrane, specifically on its lipid raft-microdomain. Disruption of lipid rafts, HSP70-LR interaction, or denaturing HSP70 abrogates the HSP-mediated increase in phagocytosis...
February 15, 2006: Blood
M S R Sastry, Konstantin Korotkov, Yan Brodsky, Francois Baneyx
The Escherichia coli chromosome contains several uncharacterized heat-inducible loci that may encode novel molecular chaperones or proteases. Here we show that the 31-kDa product of the yedU gene is an efficient homodimeric molecular chaperone that is conserved in a number of pathogenic eubacteria and fungi. Heat shock protein (Hsp) 31 relies on temperature-driven conformational changes to expose structured hydrophobic domains that are likely responsible for substrate binding. Complementing the function of refolding, remodeling, and holding chaperones, Hsp 31 preferentially interacts with early unfolding intermediates and rapidly releases them in an active form after transfer to low temperatures...
November 29, 2002: Journal of Biological Chemistry
C Bayerl, E Fuhrmann, C C Coelho, L J Lauk, I Moll, E G Jung
We report on a 58-year-old woman with long-lasting (36 years) chromomycosis on the foot and secondary self-inoculation from foot to hand 4 years ago. Mycological classification was performed after culture on Sabouraud glucose agar. We used haematoxylin and eosin and Giemsa staining and an antibody to heat shock protein (HSP) 27 (Stress Gen, Clone G3.1) on paraffin-embedded and cryostat specimens of chromomycosis. The mycological culture revealed the fungus Fonsecaea pedosoi. Histopathology revealed dermal fibrosis with persistent fungi (Medlar bodies), numerous mast cells and pseudoepitheliomatous hyperplasia...
December 1998: Mycoses
L Rensing, C Monnerjahn, U Meyer
Stress genes are differentially expressed during the development of Neurospora crassa and other fungi. Large amounts of constitutive heat shock protein 70 (HSC70) are found in dormant conidia of N. crassa, whereas little mRNA of the related glucose-regulated protein (grp78) is detected. It is, however, not generally clear whether heat shock protein or mRNA is preferentially stored in dormant spores. Germinating spores of N. crassa increase the level of grp mRNA. During this developmental stage, the induction of inducible heat shock protein (hsp) genes can be elicited by heat shock only at certain times after the beginning of germination...
November 15, 1998: FEMS Microbiology Letters
L Rensing, C Monnerjahn
Significant circadian rhythms in heat shock gene expression were observed in a prokaryotic species (Synechocystis). In eukaryotes, in contrast, several heat shock genes (constitutive and inducible) were shown to be constantly expressed. A few cases of circadian expression of heat shock proteins (HSPs), however, have been reported. Significant circadian changes of thermotolerance were observed in yeast and several plant species. Higher thermotolerance can be attributed to a higher abundance of HSPs, but also to other adaptive mechanisms...
October 1996: Chronobiology International
R S Gupta
The heat shock protein (Hsp) sequences, because of their ubiquity and high degree of conservation, provide useful models for phylogenetic analysis. In this paper I have carried out a global alignment of all available sequences (a total of 31) for the 90-kD heat shock protein (Hsp90) family. The minimum amino acid identity that is seen between presently known Hsp90 homologs is about 40% over the entire length, indicating that it is a highly conserved protein. Based on the alignment, a number of signature sequences that either are distinctive of the Hsp90 family or that distinguish between the cytosolic and the endoplasmic reticular forms of Hsp90 have been identified...
November 1995: Molecular Biology and Evolution
C P Joshi, H T Nguyen
5' untranslated leaders (5' UTLs) are suggested to play a crucial role in the selective translation of their eukaryotic mRNAs encoding heat shock proteins (HSP) during heat stress conditions. However, the structural features of the HSP mRNAs which cause this effect are mostly unknown. We have compiled the 5' UTLs from about 140 eukaryotic HSP mRNAs including vertebrates, invertebrates, higher and lower plants. A detailed analysis of these sequences according to length, A+T content, context of functional ATGs and presence of upstream non-functional ATGs was made...
February 25, 1995: Nucleic Acids Research
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