Aarhus University Seal / Aarhus Universitets segl

Daniel Otzen

Eurocin, a new fungal defensin: structure, lipid binding and its mode of action

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Jesper S Oeemig, Aalborg Univeristy, Denmark
  • Carina Lynggaard, Aalborg Univeristy, Denmark
  • Daniel Knudsen, Institut for Planlægning, Aalborg Univeristy, Denmark
  • Frederik T Hansen, Denmark
  • Kent D Noergaard, Aalborg Univeristy, Denmark
  • Tanja Schneider, University of Bonn, Germany
  • Brian S Vad, Denmark
  • Dorthe Sandvang, Novozymes A/S, Denmark
  • Line Nielsen, Novozymes A/S, Denmark
  • Soeren Neve, Novozymes A/S, Denmark
  • Hans-Henrik Kristensen, Novozymes A/S, Denmark
  • Hans-Georg Sahl, University of Bonn, Denmark
  • Daniel Otzen
  • Reinhard Wimmer, Aalborg University, Denmark
Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications, since they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, that have been found in different species. Here we describe a new fungal defensin, eurocin. Eurocin acts against a range of gram-positive human pathogens, but not against gram-negative bacteria. Eurocin consists of 42 amino acids, forming a cysteine-stabilized α/β fold. Thermal denaturation data point shows the disulphide bridges being responsible for the stability of the fold. Eurocin does not form pores in cell membranes at physiologically relevant concentrations, it does, however, lead to limited leakage of a fluorophore from small unilamellar vesicles. Eurocin interacts with detergent micelles, and it inhibits the synthesis of cell walls by binding equimolarly to the cell wall precursor lipid II.
Original languageEnglish
JournalJournal of Biological Chemistry
Volume7
Pages (from-to)42361-42372
Number of pages11
ISSN0021-9258
DOIs
Publication statusPublished - 7 Dec 2012

See relations at Aarhus University Citationformats

ID: 50640879