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Fungal heat shock proteins: molecular phylogenetic insights into the host takeover.
Sagini, João Pedro Nunes; Ligabue-Braun, Rodrigo.
Afiliação
  • Sagini JPN; Graduate Program in Biological Sciences (PPGBio), Federal University of Health Sciences of Porto Alegre (UFCSPA), Sarmento Leite, 245, Porto Alegre, 90050-170, Brazil. pedrosagini@gmail.com.
  • Ligabue-Braun R; Graduate Program in Biological Sciences (PPGBio), Federal University of Health Sciences of Porto Alegre (UFCSPA), Sarmento Leite, 245, Porto Alegre, 90050-170, Brazil.
Naturwissenschaften ; 111(2): 16, 2024 Mar 14.
Article em En | MEDLINE | ID: mdl-38483597
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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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Chaperonas Moleculares / Proteínas de Choque Térmico Idioma: En Revista: Naturwissenschaften Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Brasil País de publicação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Chaperonas Moleculares / Proteínas de Choque Térmico Idioma: En Revista: Naturwissenschaften Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Brasil País de publicação: Alemanha