LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity

We report the isolation and characterization of a novel human peptide with antimicrobial activity, termed LEAP-1 (liver-expressed antimicrobial peptide). Using a mass spectrometric assay detecting cysteine-rich peptides, a 25-residue peptide containing four disulfide bonds was identified in human bl...

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Bibliographic Details
Published in:FEBS letters 2000-09, Vol.480 (2), p.147-150
Main Authors: Krause, Alexander, Neitz, Susanne, Mägert, Hans-Jürgen, Schulz, Axel, Forssmann, Wolf-Georg, Schulz-Knappe, Peter, Adermann, Knut
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anti-Bacterial Agents
Anti-Infective Agents - classification
Anti-Infective Agents - pharmacology
Antimicrobial Cationic Peptides
Antimicrobial peptide
Bacillus megaterium - drug effects
Bacillus subtilis - drug effects
Base Sequence
Cysteine-rich peptide
Disulfides
DNA, Complementary
Hemofiltrate
Hepcidins
Humans
Liver
Microbial Sensitivity Tests
Micrococcus luteus - drug effects
Molecular Sequence Data
Neisseria - drug effects
Peptides - classification
Peptides - genetics
Peptides - pharmacology
Proteins - classification
Proteins - genetics
Proteins - pharmacology
Saccharomyces cerevisiae - drug effects
Sequence Analysis, DNA
Staphylococcus - drug effects
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Summary:We report the isolation and characterization of a novel human peptide with antimicrobial activity, termed LEAP-1 (liver-expressed antimicrobial peptide). Using a mass spectrometric assay detecting cysteine-rich peptides, a 25-residue peptide containing four disulfide bonds was identified in human blood ultrafiltrate. LEAP-1 expression was predominantly detected in the liver, and, to a much lower extent, in the heart. In radial diffusion assays, Gram-positive Bacillus megaterium, Bacillus subtilis, Micrococcus luteus, Staphylococcus carnosus, and Gram-negative Neisseria cinerea as well as the yeast Saccharomyces cerevisiae dose-dependently exhibited sensitivity upon treatment with synthetic LEAP-1. The discovery of LEAP-1 extends the known families of mammalian peptides with antimicrobial activity by its novel disulfide motif and distinct expression pattern.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01920-7