Premium
Functional interaction of human neutrophil peptide‐1 with the cell wall precursor lipid II
Author(s) -
de Leeuw Erik,
Li Changqing,
Zeng Pengyun,
Li Chong,
Buin Marlies Diepeveen-de,
Lu Wei-Yue,
Breukink Eefjan,
Lu Wuyuan
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.03.004
Subject(s) - beta defensin , peptide , defensin , antimicrobial peptides , innate immune system , lipid a , lipid ii , bacterial cell structure , antimicrobial , cell membrane , effector , biochemistry , cell , chemistry , cell wall , biology , microbiology and biotechnology , bacteria , receptor , peptidoglycan , genetics
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 α‐defensins does not correlate with antibacterial killing. We further show that the α‐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.