ArticleScientific reports2017
Structural determinants of Neosartorya fischeri antifungal protein (NFAP) for folding, stability and antifungal activity.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Fungal expression strategies for heterologous production of antimicrobial peptides.Fungal biology and biotechnology · 2026Review
- Navigating the fungal battlefield: cysteine-rich antifungal proteins and peptides from Eurotiales.Frontiers in fungal biology · 2024Review
- Hard nut to crack: Solving the disulfide linkage pattern of the Neosartorya (Aspergillus) fischeri antifungal protein 2.Protein science : a publication of the Protein Society · 2023Article
- DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study.International journal of molecular sciences · 2023Article
- Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC.International journal of molecular sciences · 2021Article
- The potential use of the Penicillium chrysogenum antifungal protein PAF, the designed variant PAFMicrobial biotechnology · 2020Article
- TheJournal of fungi (Basel, Switzerland) · 2020Article
- Characterization of a fungal competition factor: Production of a conidial cell-wall associated antifungal peptide.PLoS pathogens · 2020Article
- Biofungicidal Potential ofFrontiers in microbiology · 2020Article
- Nutrient Excess Triggers the Expression of theMicroorganisms · 2019Article
- Cysteine-Rich Antifungal Proteins from Filamentous Fungi are Promising Bioactive Natural Compounds in Anti-Israel journal of chemistry · 2019Review
- Article
- Structure and Synthesis of Antifungal Disulfide β-Strand Proteins from Filamentous Fungi.Microorganisms · 2018Review
- Rational Design and Biotechnological Production of Novel AfpB-PAF26 Chimeric Antifungal Proteins.Microorganisms · 2018Article
- New Antimicrobial Potential and Structural Properties of PAFB: A Cationic, Cysteine-Rich Protein from Penicillium chrysogenum Q176.Scientific reports · 2018Article
- Regulated Cell Death as a Therapeutic Target for Novel Antifungal Peptides and Biologics.Oxidative medicine and cellular longevity · 2018Review
- Anti-Candidal Activity and Functional Mapping of Recombinant and SyntheticFrontiers in microbiology · 2018Article
- Efficient production and characterization of the novel and highly active antifungal protein AfpB from Penicillium digitatum.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The recent global challenges to prevent and treat fungal infections strongly demand for the development of new antifungal strategies. The structurally very similar cysteine-rich antifungal proteins from ascomycetes provide a feasible basis for designing new antifungal molecules. The main structural elements responsible for folding, stability and antifungal activity are not fully understood, although this is an essential prerequisite for rational protein design. In this study, we used the Neosartorya fischeri antifungal protein (NFAP) to investigate the role of the disulphide bridges, the hydrophobic core, and the N-terminal amino acids in the formation of a highly stable, folded, and antifungal active protein. NFAP and its mutants carrying cysteine deletion (NFAPΔC), hydrophobic core deletion (NFAPΔh), and N-terminal amino acids exchanges (NFAPΔN) were produced in Pichia pastoris. The recombinant NFAP showed the same features in structure, folding, stability and activity as the native protein. The data acquired with mass spectrometry, structural analyses and antifungal activity assays of NFAP and its mutants proved the importance of the disulphide bonding, the hydrophobic core and the correct N-terminus for folding, stability and full antifungal function. Our findings provide further support to the comprehensive understanding of the structure-function relationship in members of this protein group.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.