Abstract
An antifungal peptide with a molecular mass of 9 kDa was isolated from fresh fruiting bodies of the mushroom Agrocybe cylindracea. The isolation procedure comprised ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and FPLC-gel filtration on a Superdex 75 column. The antifungal peptide, designated as agrocybin, was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. Agrocybin exerted antifungal activity against several fungal species but lacked inhibitory activity against bacteria when tested up to 300 microM. The activity of HIV-1 reverse transcriptase was attenuated in the presence of agrocybin. It exhibited weaker mitogenic activity than Con A on isolated murine splenocytes, but was devoid of antiproliferative activity on Hep G2 (hepatoma) cells when tested at 110 microM.
MeSH terms
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Agaricales / chemistry*
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Amino Acid Sequence
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Animals
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Anti-HIV Agents / pharmacology
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Antifungal Agents / analysis
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Antifungal Agents / chemistry
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Antifungal Agents / isolation & purification*
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Antifungal Agents / pharmacology
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Cell Division / drug effects
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Cell Line, Tumor
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Cell Proliferation / drug effects
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Cells, Cultured
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Chromatography, Affinity
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Chromatography, Gel
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Chromatography, Ion Exchange
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Concanavalin A / pharmacology
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Fungal Proteins / chemistry
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Fusarium / drug effects
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HIV Reverse Transcriptase / drug effects
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Lectins / pharmacology
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Male
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Mice
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Mice, Inbred C57BL
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Molecular Weight
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Peptides / analysis
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Peptides / chemistry
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Peptides / isolation & purification*
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Peptides / pharmacology
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Plant Extracts / chemistry*
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Plant Extracts / isolation & purification
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Plant Extracts / pharmacology
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Reverse Transcriptase Inhibitors / pharmacology
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Spleen / cytology
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Thymidine
Substances
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Anti-HIV Agents
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Antifungal Agents
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Fungal Proteins
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Lectins
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Peptides
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Plant Extracts
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Reverse Transcriptase Inhibitors
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agrocybin protein, Agrocybe cylindracea
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Concanavalin A
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HIV Reverse Transcriptase
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Thymidine