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Metal-based combinations that target protein synthesis by fungi

Valli�res, Cindy; Avery, Simon V.

Authors

Cindy Valli�res

Simon V. Avery



Abstract

A wide range of fungicides (or antifungals) are used in agriculture and medicine, with activities against a spectrum of fungal pathogens. Unfortunately, the evolution of fungicide resistance has become a major issue. Therefore, there is an urgent need for new antifungal treatments. Certain metals have been used for decades as efficient fungicides in agriculture. However, concerns over metal toxicity have escalated over this time. Recent studies have revealed that metals like copper and chromate can impair functions required for the fidelity of protein synthesis in fungi. This occurs through different mechanisms, based on targeting of iron–sulphur cluster integrity or competition for uptake with amino acid precursors. Moreover, chromate at least acts synergistically with other agents known to target translation fidelity, like aminoglycoside antibiotics, causing dramatic and selective growth inhibition of several fungal pathogens of humans and plants. As such synergy allows the application of decreased amounts of metals for effective inhibition, it lessens concerns about nonspecific toxicity and opens new possibilities for metal applications in combinatorial fungicides targeting protein synthesis.

Citation

Vallières, C., & Avery, S. V. (2017). Metal-based combinations that target protein synthesis by fungi. Advances in Microbial Physiology, 70, 105-121. https://doi.org/10.1016/bs.ampbs.2017.01.001

Journal Article Type Article
Acceptance Date Dec 15, 2016
Online Publication Date Feb 11, 2017
Publication Date May 18, 2017
Deposit Date Jul 25, 2017
Publicly Available Date Mar 29, 2024
Journal Advances in Microbial Physiology
Electronic ISSN 2162-5468
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 70
Pages 105-121
Book Title Microbiology of Metal Ions
DOI https://doi.org/10.1016/bs.ampbs.2017.01.001
Keywords Metals; Copper; Chromium; Antifungals; Fungi; Pathogens; Protein synthesis
Public URL https://nottingham-repository.worktribe.com/output/860944
Publisher URL http://www.sciencedirect.com/science/article/pii/S0065291117300012
Additional Information Chapter 4.