Abstract
Porcine leukocytes contained three homologous peptides, PG-1, 2 and 3, that manifested potent microbicidal activity against Escherichia coli, Listeria monocytogenes and Candida albicans in vitro. The peptides ('protegrins') were composed of 16 (PG-2) or 18 amino acid residues, and, like tachyplesins (broad-spectrum antibiotic peptides of horseshoe crab hemocytes), they contained two intramolecular cystine disulfide bonds. Considerably smaller than defensins, protegrins nevertheless showed substantial homology to them, especially to the 'corticostatic' rabbit defensin, NP-3a. The relatively simple structure of protegrins should provide useful prototypes for constructing congeners with selectively enhanced host defense activities.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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 / pharmacology
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Antimicrobial Cationic Peptides*
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Blood Proteins / chemistry*
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Blood Proteins / isolation & purification*
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Blood Proteins / pharmacology
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Chromatography, High Pressure Liquid
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / pharmacology
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Defensins
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Electrophoresis, Polyacrylamide Gel
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Leukocytes / chemistry*
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / isolation & purification
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Peptides / pharmacology
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Peptides, Cyclic*
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Sequence Homology, Amino Acid
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Swine
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alpha-Defensins*
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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Blood Proteins
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DNA-Binding Proteins
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Defensins
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Peptides
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Peptides, Cyclic
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alpha-Defensins
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defensin NP-3a
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tachyplesin peptide, Tachypleus tridentatus