Journal
FEBS LETTERS
Volume 584, Issue 8, Pages 1543-1548Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.03.004
Keywords
Human neutrophil peptide-1; Defensin; Lipid II
Funding
- National Science and Technology Major Project [2009ZX09310-006]
- National Institutes of Health [AI061482, AI072732]
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Defensins constitute a major class of cationic antimicrobial peptides in mammals and vertebrates, acting as effectors of innate immunity against infectious microorganisms. It is generally accepted that defensins are bactericidal by disrupting the anionic microbial membrane. Here, we provide evidence that membrane activity of human alpha-defensins does not correlate with antibacterial killing. We further show that the alpha-defensin human neutrophil peptide-1 (HNP1) binds to the cell wall precursor lipid II and that reduction of lipid II levels in the bacterial membrane significantly reduces bacterial killing. The interaction between defensins and lipid II suggests the inhibition of cell wall synthesis as a novel antibacterial mechanism of this important class of host defense peptides. Published by Elsevier B. V. on behalf of the Federation of European Biochemical Societies.
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