Molecular detection and characterisation of fungal heat shock protein 60

Abstract

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). Fully automated RNA extraction was followed by quantitative real-time RT-PCR targeting fungus-specific Hsp60 mRNA and sequencing of the amplicon. Levels of temperature-dependent gene expression were evaluated and rates of similarity and identity were compared. While Hsp60 mRNA was constitutively expressed in all the samples tested, a temperature-dependent induction was not shown in C. cladosporioides. In the 80-amino acid fragment from the hypothetical protein, 66% of the amino acids were identical, 20% showed a conserved and 8% a semi-conserved substitution. Our findings should contribute to a better understanding of host-pathogen relationship and suggest that fungal Hsp60 under temperature-related stress conditions might act as an immunogenic trigger in orchestrating fungi-related diseases.

Proteomic study of the yeast Rhodotorula mucilaginosa RCL-11 under copper stress

“…Another essential mitochondrial chaperone, Hsp60, was also overexpressed under copper overload (spot 13, showing a 2.8-fold induction in cells under copper overload). There exists a collective of double-ring assemblies that promote the folding of proteins to their native state, by importing the proteins into the mitochondrial matrix or into the intermembrane space (Raggam et al 2010). Hsp60 has been directly associated with the response to oxidative stress.…”

“…was too low to be used as reference value Proteomic analysis of yeast cells showed that Hsps are induced in response to H 2 O 2 stress, which is important for the protection of cells against this adverse condition. They help abnormal proteins that accumulate under stress conditions regain their proper folding or assist in their proteolytic degradation (Raggam et al 2010).…”

Copper Resistance and Oxidative Stress Response in Rhodotorula mucilaginosa RCL-11. Yeast Isolated from Contaminated Environments in Tucumán, Argentina

“…15.2 ). There exists a collective of double-ring assemblies that promote the folding of proteins to their native state, by importing the proteins into the mitochondrial matrix or into the intermembrane space ( Raggam et al 2011 ). Hsp60 has been directly associated with the response to oxidative stress.…”

“…Proteomic analysis of yeast cells showed that Hsps are induced in response to H 2 O 2 stress, which is important for the protection of cells against this adverse condition. They help abnormal proteins that accumulate under stress conditions regain their proper folding or assist in their proteolytic degradation (Raggam et al 2011 ). One protein overexpressed in R. mucilaginosa RCL-11 has been characterized as Hsp88, which appears to be a normal cellular constituent.…”

Small heat shock proteins, phylogeny in filamentous fungi and expression analyses in Aspergillus nidulans

“…In Aspergillus, the main heat shock proteins, such as HSP60, HSP70, HSP90, and HSP100, are highly conserved and have been extensively studied with respect to regulation of drug resistance as well as environmental stress responses (Lamoth et al, 2014;Blatzer et al, 2015;Raggam et al, 2011;Lamoth et al, 2012). However, sHSPs have not been well characterized and their biological roles are rarely known.…”