Abstract
A novel antimicrobial peptide named as ixosin was isolated from the salivary glands of the hard tick, Ixodes sinensis, by gel filtration, ion exchange chromatography and reverse-phase high-performance liquid chromatography (RP-HPLC). Its amino acid sequence was determined as GLHKVMREVLGYERNSYKKFFLR by Edman degradation and its molecular weight was 2870.5 analyzed by fast atom bombardment (FAB) mass spectrometry. This is the first antimicrobial peptide from ticks that lacks cysteine in its primary structure. The cDNA encoding ixosin was cloned by cDNA library screening. The predicted protein from the cDNA sequence composed of 79 amino acids including mature ixosin. Purified ixosin exerted its antimicrobial activities against bacteria and fungi. No similarity was found by BLAST search to any database entries and, thus, our findings describe a novel antimicrobial peptide.
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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Animals
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / isolation & purification
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Anti-Infective Agents / metabolism*
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Antimicrobial Cationic Peptides / chemistry
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Antimicrobial Cationic Peptides / genetics
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Antimicrobial Cationic Peptides / isolation & purification
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Antimicrobial Cationic Peptides / metabolism*
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Base Sequence
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Candida albicans / growth & development
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Escherichia coli / growth & development
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Female
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Hemolysis / physiology
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Ixodes / genetics
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Ixodes / metabolism*
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Male
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Molecular Sequence Data
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Salivary Proteins and Peptides / chemistry
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Salivary Proteins and Peptides / genetics
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Salivary Proteins and Peptides / isolation & purification
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Salivary Proteins and Peptides / metabolism*
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Staphylococcus aureus / growth & development
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Salivary Proteins and Peptides
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ixosin protein, Ixodes sinensis