Abstract
Heat shock proteins (HSPs) are involved in critical processes like host tissue invasion, resistance, and pathogenicity in dermatophytes. RNA-Seq analysis of Trichophyton rubrum exposed to undecanoic acid (UDA) revealed intron retention events in HSP transcripts. Because HSPs are modulated in response to various stimuli and as alternative splicing (AS) can result in a broad diversity in the proteome of eukaryotic cells, our objective was to confirm the aforementioned retention events, investigating their consequences and extent. Furthermore, we aimed to determine: (1) the expression profile of HSP genes in an infection-like scenario and (2) the importance of Hsp90 for the keratinolytic potential of T. rubrum. RT and qPCR analyses comparing the exposure to UDA and terbinafine (TRB) confirmed the presence of two mRNA isoforms of the hsp7-like gene, with distinct expression patterns in response to UDA and TRB. The HSP expression profile revealed two upregulated, three downregulated, and four unmodulated transcripts; Hsp90 inhibition by 17-AAG resulted in a significant decrease in keratinolytic potential at 37 °C. Altogether, these results broaden the current knowledge on the importance of HSP-mediated pathways for cell adaptation and other aspects of dermatophyte biology, indicating that HSP network proteins can be potential targets for antifungal therapy.
Highlights
Heat shock proteins (HSPs) are a highly conserved group of chaperones found in virtually all living organisms, both prokaryotes and eukaryotes [1,2]
The objective of this study is to investigate the occurrence of intron retention events in the transcripts of Hsp70 family members, and to discuss the role played by the regulation of HSP-mediated networks in cell adaptation in T. rubrum
In silico investigations performed for both genes demonstrated that conventional processing of their respective pre-mRNAs produces functional proteins, both belonging to the Hsp70 family (Figure 1)
Summary
Heat shock proteins (HSPs) are a highly conserved group of chaperones found in virtually all living organisms, both prokaryotes and eukaryotes [1,2]. Sharing the characteristic attribute of having their expression rapidly modulated by various stress conditions, HSPs act at different stages to regulate the following features of target proteins: folding, maintenance of native conformation, and fragmentation of aggregates. They are involved in transport and degradation pathways, signaling, and cell cycle regulation [2,3,4]. Anthropophilic dermatophytes are responsible for causing chronic, slow-progression infections in humans as a result of long-term co-evolutionary dynamics with hosts. Keratinized body parts such as hair, skin, and nails are those most affected, with colonization usually remaining limited to the
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