The secreted acid trehalase encoded by the CgATH1 gene is involved in Candida glabrata virulence

Autor(es)

Rafael G Lopes ^[1] ; Julián E Muñoz ; Ludmila M Barros ^[3] ; Sergio L Alves-Jr ^[4] ; Carlos P Taborda ; Boris U Stambuk ^[6]

Afiliação do(s) autor(es)

^[1] Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Departamento de Bioquímica - Brasil

^[3] Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Departamento de Bioquímica - Brasil

^[4] Universidade Federal da Fronteira Sul. Laboratório de Bioquímica e Genética - Brasil

^[6] Universidade Federal de Santa Catarina. Centro de Ciências Biológicas. Departamento de Bioquímica - Brasil

• Tipo de documento: Artigo Científico
• Fonte: Memórias do Instituto Oswaldo Cruz; v. 115, 2020-10-30.

Resumo

BACKGROUND Candida glabrata yeast is the second cause of candidiasis worldwide. Differs from other yeasts since assimilates only glucose and trehalose (a characteristic used in rapid identification tests for this pathogen) by secreting into the medium a highly active acid trehalase encoded by the CgATH1 gene. OBJECTIVE This study aimed to characterise the function of the acid trehalase in the physiopathology of C. glabrata. METHODS Gene deletion was performed to obtain a mutant ath1Δ strain, and the ability of the ath1Δ strain to grow in trehalase, or the presence of trehalase activity in the ath1Δ yeast cells, was verified. We also tested the virulence of the ath1Δ strain in a murine model of infection. FINDINGS The ath1Δ mutant strain grows normally in the presence of glucose, but loses its ability to grow in trehalose. Due to the high acid trehalase activity present in wild-type cells, the cytoplasmic neutral trehalase activity is only detected in the ath1Δ strain. We also observed a significantly lower virulence of the ath1Δ strain in a murine model of infection with either normal or immunocompromised mice. MAIN CONCLUSIONS The acid trehalase is involved in the hydrolysis of external trehalose by C. glabrata, and the enzyme also plays a major virulence role during infectivity. (AU)

• Processo FAPESP: 16/08730-6 - Patogenicidade fúngica: efeito do tabagismo, resposta imune e a modulação vacinal na paracoccidioidomicose e na histoplasmose
• Beneficiário: Carlos Pelleschi Taborda
• Modalidade de apoio: Auxílio à Pesquisa - Temático