ArticleMemorias do Instituto Oswaldo Cruz2020
The secreted acid trehalase encoded by the CgATH1 gene is involved in Candida glabrata virulence.
Article in Memorias do Instituto Oswaldo Cruz, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Beyond antibiotics: a new anti-virulence strategy combating ESBL-producing Klebsiella pneumoniae by targeting periplasmic trehalase.BMC microbiology · 2026Article
- A trehalase-derived MAMP triggers LecRK-V-mediated immune responses inScience advances · 2025Article
- Sulfur, sterol and trehalose metabolism in the deep-sea hydrocarbon seep tubeworm Lamellibrachia luymesi.BMC genomics · 2023Article
- Lack of Functional Trehalase Activity inJournal of fungi (Basel, Switzerland) · 2022Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCandida 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.
objectiveThis study aimed to characterise the function of the acid trehalase in the physiopathology of C. glabrata.
methodsGene 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.
findingsThe 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
conclusionsThe acid trehalase is involved in the hydrolysis of external trehalose by C. glabrata, and the enzyme also plays a major virulence role during infectivity.
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