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Antifungal Protein Research

Antifungal Protein Research

Working Group of Florentine Marx-Ladurner

About

Research

Projects

People

About

WG Marx-Ladurner

Our main scientific interest lies in the identification and characterization of antimicrobial proteins secreted by filamentous ascomycetes. These proteins are small in size, cationic and contain 6-8 cysteines which form disulphide bonds that are important for correct protein folding and high stability against harsh environmental conditions. These bioactive proteins are promising candidates for new antimicrobial strategies and the development of novel drugs.

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Research

  • Topics
  • Technologies
  • Key Publications
    • Characterization of Antimicrobial Proteins
    • Identification of New Antifungal Drug Targets
    • Structure-Function Analyses of Cationic and Cysteine-rich Antimicrobial Proteins
    • Antimicrobial activity assays
    • Site-directed mutagenesis
    • State-of-the-art molecular biology techniques
    • Expression and purification of recombinant proteins
    • Microscopy
    • Activity assays of histone-modifying enzymes
    • Hegedüs, N., and Marx, F. (2013). Antifungal proteins: More than antimicrobials? Fungal Biol. Rev. 26: 132-145
    • Fizil, Á., Gáspári, Z., Barna, T., Marx, F., and Batta, G. (2015). "Invisible" conformers of an antifungal disulfide protein revealed by constrained cold an heat unfolding, CEST-NMR experiments, and molecular dynamics calculations. Chemistry 21: 5136-5144
    • Binder, U., Bencina, M., Fizil, Á., Batta, G., Chhillar, A.K., and Marx, F. (2015). Protein kinase A signaling and calcium ions are major players in PAF mediated toxicity against Aspergillus niger. FEBS Lett. 589: 1266-1271

Projects

Hunting for new antifungal strategies: the antifungal protein PAF - In addition to a detailed knowledge about the antifungal potential of PAF, our studies will significantly contribute to a better insight into specific aspects of cellular processes that are less well understood in filamentous model ascomycetes compared to other well characterized models like yeasts.

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Structure and function of the antifungal proteins PAFB and NFAP - The proposed project aims at (1) investigating the solution structure, dynamics, folding/unfolding of PAFB and NFAP, (2) identifying core elements that are responsible for the correct folding and the interaction of the proteins with their fungal targets and (3) making first steps towards the characterization of potential fungal targets.

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The gamma-core motif of antifungal proteins from Ascomycetes - The accomplishment of our objectives will allow important new insights into the functional and structural role of the highly conserved gamma-core motif and provide the first steps towards a biotechnological application by developing bioactive molecules with worldwide economic and societal impact.

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People

Group Leader

Ao. Univ. Prof. Mag. Florentine Marx-Ladurner

  • Medical University of Innsbruck - Division of Molecular Biology
  • florentine.marx@i-med.ac.at
  • +43 512 9003 70207

Group Members

Doris Bratschun-Khan
Technician; doris.bratschun@i-med.ac.at
Anna Huber, MSc
PhD student, Research topic: Identification of fungal cell targets that mediate the toxicity of antifungal proteins. a.huber@i-med.ac.at
Jeanett Holzknecht, MSc
PhD Student; jeanett.holzknecht@i-med.ac.at
Anant Kakar, MSc
PhD Student; anant.kakar@i-med.ac.at
© Mycology Tyrol 2016 - 2021
University of Innsbruck & Medical University of Innsbruck
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