Abstract
A strain of Streptoverticillium cinnamoneum produced a peptide antibiotic named lanthiopeptin, which contained four unusual amino acids, erythro-beta-hydroxyaspartic acid, mesolanthionine, threo-beta-methyllanthionine and lysinoalanine. Lanthiopeptin showed antiviral activity against herpes simplex virus type 1 KOS strain infection in Vero cells by cytopathic effect reduction assay. The structure of lanthiopeptin is similar to that of ancovenin.
MeSH terms
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Amino Acid Sequence
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Amino Acids / analysis
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Animals
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Anti-Bacterial Agents* / analysis
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Anti-Bacterial Agents* / biosynthesis
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Anti-Bacterial Agents* / isolation & purification*
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Anti-Bacterial Agents* / pharmacology
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Antifungal Agents / analysis
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Antifungal Agents / biosynthesis
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Antifungal Agents / isolation & purification
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Antifungal Agents / pharmacology
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Antiviral Agents / analysis
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Antiviral Agents / biosynthesis
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Antiviral Agents / isolation & purification*
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Antiviral Agents / pharmacology
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Bacteria / drug effects
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Chromatography, Gel
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Cytopathogenic Effect, Viral / drug effects
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Fermentation
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Magnetic Resonance Spectroscopy
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Molecular Sequence Data
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Peptide Biosynthesis
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Peptides / analysis
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Peptides / isolation & purification*
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Peptides / pharmacology
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Peptides, Cyclic
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Simplexvirus / drug effects*
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Soil Microbiology
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Solubility
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Spores, Bacterial
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Streptomycetaceae / growth & development
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Streptomycetaceae / metabolism*
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Streptomycetaceae / physiology
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Vero Cells
Substances
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Amino Acids
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Anti-Bacterial Agents
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Antifungal Agents
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Antiviral Agents
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Peptides
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Peptides, Cyclic
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lanthiopeptin