Abstract
Ta0-a, the gene encoding the mature antimicrobial peptide tachyplesin II, was engineered to optimize the coding sequence according to codon usage bias in yeast. Ta0-a was efficiently expressed in the methylotrophic yeast Pichia pastoris strain SMD1168. The recombinant peptide Ta0 reached 150mg/L after methanol induction for 6 d. Ta0 was rapidly purified to homogeneity by a single step of size-exclusion chromatography. The minimal lethal concentrations of Ta0 to the Escherichia coli strain K12 was 30 microg/mL. Ta0 exhibited a wide range of antimicrobial activity: the growth of 26 bacterial and fungal strains, including some typical food/feed spoilage microorganisms, was all substantially inhibited. This result indicates the potential practical application of the recombinant peptide in various industrial products.
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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Antimicrobial Cationic Peptides / biosynthesis*
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Antimicrobial Cationic Peptides / pharmacology*
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Cloning, Molecular
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DNA-Binding Proteins / biosynthesis*
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DNA-Binding Proteins / pharmacology*
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Disulfides / analysis
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Escherichia coli / drug effects
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Escherichia coli / metabolism
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Fungi / drug effects
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Microbial Sensitivity Tests
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Peptides, Cyclic / biosynthesis*
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Peptides, Cyclic / pharmacology*
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Pichia / metabolism
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / pharmacology
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Salmonella / drug effects
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Shigella dysenteriae / drug effects
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Staphylococcus aureus / drug effects
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Yeasts / drug effects
Substances
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Antimicrobial Cationic Peptides
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DNA-Binding Proteins
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Disulfides
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Peptides, Cyclic
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Recombinant Proteins
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tachyplesin peptide, Tachypleus tridentatus