Format

Send to

Choose Destination
See comment in PubMed Commons below
FEBS Lett. 2010 Apr 16;584(8):1543-8. doi: 10.1016/j.febslet.2010.03.004. Epub 2010 Mar 7.

Functional interaction of human neutrophil peptide-1 with the cell wall precursor lipid II.

Author information

1
University of Maryland Baltimore School of Medicine, Institute of Human Virology, Department of Biochemistry and Molecular Biology, Baltimore, MD 21201, USA. edeleeuw2@ihv.umaryland.edu

Abstract

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.

PMID:
20214904
PMCID:
PMC3417325
DOI:
10.1016/j.febslet.2010.03.004
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley Icon for PubMed Central
    Loading ...
    Support Center