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Zinc potentiates the antibacterial effects of histidine‐rich peptides against Enterococcus faecalis
Author(s) -
Rydengård Victoria,
Andersson Nordahl Emma,
Schmidtchen Artur
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05246.x
Subject(s) - histidine , enterococcus faecalis , peptide , antimicrobial , antimicrobial peptides , biochemistry , chemistry , antibacterial activity , microbiology and biotechnology , bacteria , antibacterial peptide , biology , amino acid , escherichia coli , genetics , gene
Antimicrobial peptides are effector molecules of the innate immune system. We have recently shown that peptides containing multiples of the heparin‐binding Cardin and Weintraub motifs AKKARA and ARKKAAKA exert antimicrobial activities. Here, we show that replacement of lysine and arginine in these motifs by histidine abrogates the antibacterial effects of these peptides. Antibacterial activity of the histidine‐rich peptides against the Gram‐positive bacterium Enterococcus faecalis was restored by the addition of Zn 2+ . Fluorescence microscopy experiments showed that Zn 2+ enabled binding of the histidine‐rich peptides to Enterococcus faecalis bacteria. Similar Zn 2+ ‐dependent antibacterial activities were shown for histatin 5 as well as histidine‐containing peptides derived from the Zn 2+ ‐ and heparin‐binding domain 5 of human kininogen. Thus, the results demonstrate a previously undisclosed Zn 2+ ‐dependent antibacterial activity of kininogen‐derived peptides and indicate an important role for Zn 2+ in regulating the antimicrobial activities of histidine‐rich peptides.