Journal
SCIENCE
Volume 328, Issue 5982, Pages 1168-1172Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1185723
Keywords
-
Categories
Funding
- Obel Foundation
- European Union [PIAP-GA-2008-218191]
- German Research Foundation [SA 292/10-2, SA 292/13-1]
- Bundesministerium fur Bildung und Forschung (SkinStaph)
- Medical Faculty, University of Bonn
- Netherlands Organization for Scientific Research [700.56.442]
- Danish Research Council for Technology and Production [274-05-0435]
Ask authors/readers for more resources
Host defense peptides such as defensins are components of innate immunity and have retained antibiotic activity throughout evolution. Their activity is thought to be due to amphipathic structures, which enable binding and disruption of microbial cytoplasmic membranes. Contrary to this, we show that plectasin, a fungal defensin, acts by directly binding the bacterial cell-wall precursor Lipid II. A wide range of genetic and biochemical approaches identify cell-wall biosynthesis as the pathway targeted by plectasin. In vitro assays for cell-wall synthesis identified Lipid II as the specific cellular target. Consistently, binding studies confirmed the formation of an equimolar stoichiometric complex between Lipid II and plectasin. Furthermore, key residues in plectasin involved in complex formation were identified using nuclear magnetic resonance spectroscopy and computational modeling.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available