ArticlePloS one2017
D19S Mutation of the Cationic, Cysteine-Rich Protein PAF: Novel Insights into Its Structural Dynamics, Thermal Unfolding and Antifungal Function.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 34 citations in OpenAlex.
- Engineering Penicillium expansum antifungal proteins unveils new clues about their mode of action.Applied microbiology and biotechnology · 2026Article
- Small Disulfide Proteins with Antifungal Impact: NMR Experimental Structures as Compared to Models of Alphafold Versions.International journal of molecular sciences · 2025Article
- Navigating the fungal battlefield: cysteine-rich antifungal proteins and peptides from Eurotiales.Frontiers in fungal biology · 2024Review
- Novel findings about the mode of action of the antifungal protein PeAfpA against Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2023Article
- A comprehensive review on the medicinally valuable endosymbiotic fungi Penicillium chrysogenum.Archives of microbiology · 2023Review
- 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
- Article
- An Overview of the Potentialities of Antimicrobial Peptides Derived from Natural Sources.Antibiotics (Basel, Switzerland) · 2022Review
- TheJournal of fungi (Basel, Switzerland) · 2022Article
- Small, Cationic Antifungal Proteins from Filamentous Fungi InhibitMicrobiology spectrum · 2022Article
- Article
- TheJournal of fungi (Basel, Switzerland) · 2020Article
- Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum: A comparative study of PAF and PAFB.Biochimica et biophysica acta. Biomembranes · 2020Review
- Characterization of a fungal competition factor: Production of a conidial cell-wall associated antifungal peptide.PLoS pathogens · 2020Article
- Article
- The Myosin Motor Domain-Containing Chitin Synthases Are Involved in Cell Wall Integrity and Sensitivity to Antifungal Proteins inFrontiers in microbiology · 2019Article
- Membrane Sphingolipids Regulate the Fitness and Antifungal Protein Susceptibility ofFrontiers in microbiology · 2019Article
- Structure and Synthesis of Antifungal Disulfide β-Strand Proteins from Filamentous Fungi.Microorganisms · 2018Review
- New Antimicrobial Potential and Structural Properties of PAFB: A Cationic, Cysteine-Rich Protein from Penicillium chrysogenum Q176.Scientific reports · 2018Article
- Three Antifungal Proteins FromFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
The cysteine-rich, cationic, antifungal protein PAF is abundantly secreted into the culture supernatant of the filamentous Ascomycete Penicillium chrysogenum. The five β-strands of PAF form a compact β-barrel that is stabilized by three disulphide bonds. The folding of PAF allows the formation of four surface-exposed loops and distinct charged motifs on the protein surface that might regulate the interaction of PAF with the sensitive target fungus. The growth inhibitory activity of this highly stable protein against opportunistic fungal pathogens provides great potential in antifungal drug research. To understand its mode of action, we started to investigate the surface-exposed loops of PAF and replaced one aspartic acid at position 19 in loop 2 that is potentially involved in PAF active or binding site, with a serine (Asp19 to Ser19). We analysed the overall effects, such as unfolding, electrostatic changes, sporadic conformers and antifungal activity when substituting this specific amino acid to the fairly indifferent amino acid serine. Structural analyses revealed that the overall 3D solution structure is virtually identical with that of PAF. However, PAFD19S showed slightly increased dynamics and significant differences in the surface charge distribution. Thermal unfolding identified PAFD19S to be rather a two-state folder in contrast to the three-state folder PAF. Functional comparison of PAFD19S and PAF revealed that the exchange at residue 19 caused a dramatic loss of antifungal activity: the binding and internalization of PAFD19S by target cells was reduced and the protein failed to trigger an intracellular Ca2+ response, all of which are closely linked to the antifungal toxicity of PAF. We conclude that the negatively charged residue Asp19 in loop 2 is essential for full function of the cationic protein PAF.
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Registered trials
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.