A new fungal immunomodulatory protein, FIP-fve isolated from the edible mushroom, Flammulina velutipes and its complete amino acid sequence

• Published in: European journal of biochemistry Vol. 228; no. 2; pp. 244 - 249
• Main Authors: Ko, J L, Hsu, C I, Lin, R H, Kao, C L, Lin, J Y
• Format: Journal Article
• Language: English
• Published: England 01.03.1995
• Subjects: Adjuvants, Immunologic - isolation & purification; Amino Acid Sequence; Animals; Base Sequence; Basidiomycota - chemistry; Cytokines - biosynthesis; Fungal Proteins - chemistry; Fungal Proteins - isolation & purification; Fungal Proteins - pharmacology; Hemagglutination; Lectins; Mice; Mice, Inbred BALB C; Molecular Sequence Data
• ISSN: 0014-2956; 1432-1033
• DOI: 10.1111/j.1432-1033.1995.tb20256.x

A new fungal immunomodulatory protein (FIP-fve) has been isolated and purified from the edible golden needle mushroom (Flammulina velutipes). The apparent molecular mass of FIP-fve determined by SDS/PAGE agrees well with the value of 12704 Da calculated from its amino acid composition and sequence. The complete amino acid sequence of FIP-fve was elucidated by protein sequencing techniques. FIP-fve consists of 114 amino acid residues with an acetylated amino end, and lacks methionine, half-cystine and histidine residues. FIP-fve was able to hemagglutinate human red blood cells. The immunomodulatory activity of FIP-fve was demonstrated by its stimulatory activity toward human peripheral blood lymphocytes, and its suppression of systemic anaphylaxis reactions and local swelling of mouse footpads. FIP-fve was found to enhance the transcriptional expression of interleukin-2 and interferon-gamma.