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Eurocin, a New Fungal Defensin

Authors :
Tanja Schneider
Frederik Teilfeldt Hansen
Hans-Georg Sahl
Daniel E. Otzen
Søren Neve
Kent D. Nørgaard
Daniel H. Knudsen
Carina Lynggaard
Reinhard Wimmer
Line Anker Nielsen
Hans-Henrik Kristensen
Brian S. Vad
Jesper S. Oeemig
Dorthe Sandvang
Source :
Journal of Biological Chemistry. 287:42361-42372
Publication Year :
2012
Publisher :
Elsevier BV, 2012.

Abstract

Antimicrobial peptides are a new class of antibiotics that are promising for pharmaceutical applications because they have retained efficacy throughout evolution. One class of antimicrobial peptides are the defensins, which 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. The thermal denaturation data point shows the disulfide 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.

Details

ISSN :
00219258
Volume :
287
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry
Accession number :
edsair.doi...........99adb1853469121f1eb7e9a2af59d084