Details

Autor(en) / Beteiligte

• Michalek, Matthias
• Jung, Sascha
• Shomali, Mohammad R.
• Cauchard, Severine
• Sönnichsen, Frank D.
• Grötzinger, Joachim

Titel

Solution structure and functional studies of the highly potent equine antimicrobial peptide DEFA1

Ist Teil von

• Biochemical and biophysical research communications, 2015-04, Vol.459 (4), p.668-672

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2015

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Defensins are small effector molecules of the innate immune system that are present in almost all organisms including plants and animals. These peptides possess antimicrobial activity against a broad range of microbes including bacteria, fungi and viruses and act as endogenous antibiotics. α-Defensins are a subfamily of the defensin family and their expression is limited to specific tissues. Equine DEFA1 is an enteric α-defensin exclusively secreted by Paneth cells and shows an activity against a broad spectrum of microbes, including typical pathogens of the horse such as Rhodococcus equi, various streptococci strains, Salmonella choleraesuis, and Pasteurella multocida. Here, we report the three-dimensional structure of DEFA1 solved by NMR-spectroscopy and demonstrate its specific function of aggregating various phospholipids. •Solution structure of DEFA1 reveals differences in charge distribution compared with other α-defensins.•DEFA1 aggregates lipid vesicles composed of anionic charged phospholipids.•DEFA1's mode of action is described as the barnacle model.