Abstract
Heat shock proteins are constitutively expressed chaperones induced by cellular stress, such as changes in temperature, pH, and osmolarity. These proteins, present in all organisms, are highly conserved and are recruited for the assembly of protein complexes, transport, and compartmentalization of molecules. In fungi, these proteins are related to their adaptation to the environment, their evolutionary success in acquiring new hosts, and regulation of virulence and resistance factors. These characteristics are interesting for assessment of the host adaptability and ecological transitions, given the emergence of infections by these microorganisms. Based on phylogenetic inferences, we compared the sequences of HSP9, HSP12, HSP30, HSP40, HSP70, HSP90, and HSP110 to elucidate the evolutionary relationships of different fungal organisms to suggest evolutionary patterns employing the maximum likelihood method. By the different reconstructions, our inference supports the hypothesis that these classes of proteins are associated with pathogenic gains against endothermic hosts, as well as adaptations for phytopathogenic fungi.
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Abbreviations
- HSP:
-
Heat shock protein
- HSF:
-
Heat shock factors
- NBD:
-
Nucleotide-biding domain
- SBD:
-
Substrate-binding domain
- sHSPs:
-
Small HSPs
- cAMP:
-
Cyclic AMP
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All authors contributed to the study conception and design. Material preparation, data collection, and analysis were performed by João Pedro Sagini and Rodrigo Ligabue-Braun. The first draft of the manuscript was written by João Pedro Sagini, and all authors commented on previous versions of the manuscript. All authors read and approved the final manuscript.
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Sagini, J.P.N., Ligabue-Braun, R. Fungal heat shock proteins: molecular phylogenetic insights into the host takeover. Sci Nat 111, 16 (2024). https://doi.org/10.1007/s00114-024-01903-x
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DOI: https://doi.org/10.1007/s00114-024-01903-x