ArticleApplied and environmental microbiology2022
Molecular Characterization and the Essential Biological Function of the Metal Chaperone Protein MtmA in Aspergillus fumigatus.
Article in Applied and environmental microbiology, 2022. 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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4 citing papers in PubMed, 7 citations in OpenAlex.
- Oxidoreductase geneMicrobiology spectrum · 2026Article
- New developments in Aspergillus fumigatus and host reactive oxygen species responses.Current opinion in microbiology · 2024Review
- Fungal Zinc Homeostasis and Its Potential as an Antifungal Target: A Focus on the Human PathogenMicroorganisms · 2022Review
- The metal chaperone protein MtmA plays important roles in antifungal drug susceptibility inFrontiers in microbiology · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The detoxification system of reactive oxygen species (ROS) plays critical roles in the survival and virulence of fungal pathogens in infected hosts, while superoxide dismutase (SOD) is the primary ROS scavenger. In the model yeast Saccharomyces cerevisiae, the metal chaperone protein Mtm1 is required for mitochondrial Sod2 activation and responses to oxidative stress. However, the function of the S. cerevisiae Mtm1 homolog in the human fungal pathogen Aspergillus fumigatus has not yet been clarified. In this study, we found that mitochondria-localized MtmA in A. fumigatus, a putative homolog of yeast Mtm1, not only has a similar function to Mtm1 in responding to oxidative stress resistance by affecting SodB (MnSOD) activity but is also essential for hyphal growth such that repressed expression of MtmA results in severe growth defects in A. fumigatus. In addition, the chelation of Zn
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