Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents
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Anti-Infective Agents / classification
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Anti-Infective Agents / pharmacology*
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Antimicrobial Cationic Peptides
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Bacillus megaterium / drug effects
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Bacillus subtilis / drug effects
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Base Sequence
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DNA, Complementary
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Disulfides
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Hepcidins
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Humans
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Microbial Sensitivity Tests
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Micrococcus luteus / drug effects
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Molecular Sequence Data
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Neisseria / drug effects
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Peptides / classification
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Peptides / genetics
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Peptides / pharmacology*
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Proteins / classification
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Proteins / genetics
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Proteins / pharmacology*
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Saccharomyces cerevisiae / drug effects
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Sequence Analysis, DNA
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Staphylococcus / drug effects
Substances
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Anti-Bacterial Agents
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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DNA, Complementary
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Disulfides
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HAMP protein, human
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Hepcidins
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Peptides
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Proteins
Associated data
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GENBANK/AD000684
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GENBANK/AJ277280
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GENBANK/P81172