Fungal heat shock proteins: molecular phylogenetic insights into the host takeover

• Published in: Die Naturwissenschaften 2024-04, Vol.111 (2), p.16-16, Article 16
• Main Authors: Sagini, João Pedro Nunes, Ligabue-Braun, Rodrigo
• Format: Article
• Language: English
• Subjects: Adaptability; Adaptation; Biomedical and Life Sciences; Ecology; endothermy; Environment; Evolution; Fungi; gene expression; Heat shock proteins; heat stress; heat-shock protein 40; Hsp40 protein; Hsp70 protein; Hsp90 protein; Life Sciences; Maximum likelihood method; Microorganisms; Original Article; Osmolarity; Phylogenetics; Phylogeny; Phytopathogenic fungi; Protein transport; Proteins; Resistance factors; statistical analysis; temperature; Virulence
• ISSN: 0028-1042; 1432-1904
• DOI: 10.1007/s00114-024-01903-x

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.