JIUNN-LIANG KO2026-10-162026-10-161997-07-01Pure ID: 15468123Pure UUID: d15ed6fc-db89-45a9-bcac-d6868dbab04chttps://www.scopus.com/pages/publications/0030797511https://scholars.csmu.edu.tw/handle/123456789/29866FIP-fve, a fungal immunomodulatory protein, was isolated from the fruiting bodies of the edible mushroom, Flammulina velutipes. FIP-fve was shown to stimulate blast-forming activity of human peripheral blood lymphocytes and gene expression of interleukin-2, interferon-γ and tumor necrosis factor-α. Repeated administration of FIP-fve to mice inhibits the Arthur and systemic anaphylaxis reactions. FIP-fve cDNA was cloned and sequenced, and the amino acid sequence of FIP-fve deduced from the nucleotide sequence is identical to that previously determined by protein sequencing. FIP-fve cDNA was amplified by polymerase chain reaction, ligated into the expression vector, pGEX-2T, and expressed in Escherichia coli as a fusion protein of glutathione S-transferase (GST) and FIP-fve. The GST-FIP-fve fusion protein was soluble, and the yield of recombinant FIP-fve was about 5 mg/L of induced culture. The recombinant FIP-fve was obtained by cleaving the GST-FIP-fve fusion protein with thrombin and purifying to homogeneity. The recombinant FIP-fve had about 50% of the immunomodulatory activity of the native FIP-fve.8enjournal article