| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1928235 | Biochemical and Biophysical Research Communications | 2015 | 5 Pages |
•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.
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.
