Publicação
Profiling of carboxylate transporter genes during systemic infections and virulence of Candida glabrata null mutants
| Resumo: | In the last decades, fungi have emerged as one of the major causes of human infection diseases. Candida species are one of the most common fungal pathogens that can cause both superficial and invasive infections. Under normal conditions, Candida species are commensal microorganisms of the human microflora, however, they can also be successful opportunistic pathogens, especially in individuals with a compromised immune system. Candida species can adapt very easily to several host niches, including colonizing and proliferating in very different environmental conditions. Glucose is generally the preferred carbon source of most microorganisms, however, some of the most common colonization sites by Candida are not rich in this monosaccharide, for example, the vaginal tract. In these cases, the use of alternative carbon sources becomes essential for the survival of these pathogens. The ATO (Acetate Transporter Ortholog) plasma membrane carboxylate transporters are present in different yeast species. These proteins seem to be very important for Candida adaptation to different host environments, especially in those where carboxylic acids are the main carbon source available. The species Candida glabrata, often considered the second or third most common cause of candidiasis in humans, is recognized by its ability to adapt to environmental or host-imposed stresses, like nutrient limitation. This pathogen encodes two homologues of ScATO1 (CgATO1, CgATO2) and one of ScATO3 (CgATO3), that are upregulated in the presence of acetic acid, suggesting that Ato proteins are important for the uptake of this substrate. In addition, C. glabrata encodes two homologues of S. cerevisiae FPS1, CgFPS1 and CgFPS2, that are also expressed in the presence of acetic acid. The main goal of this thesis was to characterize these transporters and channels in terms of the substrates that they transport, their subcellular localization and their importance in the survival of C. glabrata cells after phagocytosis. This study validated the function of these proteins in C. glabrata as acetate transporters and unveiled their role in the adaptation and persistence of this fungus to the intracellular environment of macrophages. |
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| Autores principais: | Duarte, Cláudia Lima |
| Assunto: | Candida glabrata Plasma membrane transporters Channels Carboxylic acids Transportadores de membrana Canais Ácidos carboxílicos Ciências Naturais::Outras Ciências Naturais |
| Ano: | 2020 |
| País: | Portugal |
| Tipo de documento: | dissertação de mestrado |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade do Minho |
| Idioma: | inglês |
| Origem: | RepositóriUM - Universidade do Minho |
| Resumo: | In the last decades, fungi have emerged as one of the major causes of human infection diseases. Candida species are one of the most common fungal pathogens that can cause both superficial and invasive infections. Under normal conditions, Candida species are commensal microorganisms of the human microflora, however, they can also be successful opportunistic pathogens, especially in individuals with a compromised immune system. Candida species can adapt very easily to several host niches, including colonizing and proliferating in very different environmental conditions. Glucose is generally the preferred carbon source of most microorganisms, however, some of the most common colonization sites by Candida are not rich in this monosaccharide, for example, the vaginal tract. In these cases, the use of alternative carbon sources becomes essential for the survival of these pathogens. The ATO (Acetate Transporter Ortholog) plasma membrane carboxylate transporters are present in different yeast species. These proteins seem to be very important for Candida adaptation to different host environments, especially in those where carboxylic acids are the main carbon source available. The species Candida glabrata, often considered the second or third most common cause of candidiasis in humans, is recognized by its ability to adapt to environmental or host-imposed stresses, like nutrient limitation. This pathogen encodes two homologues of ScATO1 (CgATO1, CgATO2) and one of ScATO3 (CgATO3), that are upregulated in the presence of acetic acid, suggesting that Ato proteins are important for the uptake of this substrate. In addition, C. glabrata encodes two homologues of S. cerevisiae FPS1, CgFPS1 and CgFPS2, that are also expressed in the presence of acetic acid. The main goal of this thesis was to characterize these transporters and channels in terms of the substrates that they transport, their subcellular localization and their importance in the survival of C. glabrata cells after phagocytosis. This study validated the function of these proteins in C. glabrata as acetate transporters and unveiled their role in the adaptation and persistence of this fungus to the intracellular environment of macrophages. |
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