ArticleMetallomics : integrated biometal science2022
Specific Zn(II)-binding site in the C-terminus of Aspf2, a zincophore from Aspergillus fumigatus.
Article in Metallomics : integrated biometal science, 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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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Structural insights into mechanisms of zinc scavenging by the Candida albicans zincophore Pra1.Nature communications · 2025Article
- An Introduction to the Influence of Nutritional Factors on the Pathogenesis of Opportunist Fungal Pathogens in Humans.Pathogens (Basel, Switzerland) · 2025Review
- CH vs. HC-Promiscuous Metal Sponges in Antimicrobial Peptides and Metallophores.Molecules (Basel, Switzerland) · 2023Article
- Fungal Zinc Homeostasis and Its Potential as an Antifungal Target: A Focus on the Human PathogenMicroorganisms · 2022Review
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Authors and funding
4 authors at 2 institutions in 1 country.
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Abstract
Aspergillus fumigatus, one of the most widespread opportunistic human fungal pathogens, adapts to zinc limitation by secreting a 310 amino acid Aspf2 zincophore, able to specifically bind Zn(II) and deliver it to a transmembrane zinc transporter, ZrfC. In this work, we focus on the thermodynamics of Zn(II) complexes with unstructured regions of Aspf2; basing on a variety of spectrometric and potentiometric data, we show that the C-terminal part has the highest Zn(II)-binding affinity among the potential binding sites, and Ni(II) does not compete with Zn(II) binding to this region. The 14 amino acid Aspf2 C-terminus coordinates Zn(II) via two Cys thiolates and two His imidazoles and it could be considered as a promising A. fumigatus targeting molecule.
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