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International Journal of Medicinal Mushrooms
IF: 1.423 5-Year IF: 1.525 SJR: 0.431 SNIP: 0.716 CiteScore™: 2.6

ISSN Print: 1521-9437
ISSN Online: 1940-4344

International Journal of Medicinal Mushrooms

DOI: 10.1615/IntJMedMushr.v12.i4.20
pages 347-358

In vitro Synthesis of a Recombinant Fungal Immunomodulatory Protein from Lingzhi or Reishi Medicinal Mushroom, Ganoderma lucidum (W.Curt.:Fr.) P.Karst. (Aphyllophoromycetideae) and Analysis of Its Immunomodulatory Activity

Qi-zhang Li
Plant Biotechnology Research Center, Shanghai Key Laboratory of Agro-biotechnology, School of Agriculture and Biology, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Shanghai Jiao Tong University, Shanghai 200240, P. R. China
Xue-fei Wang
Plant Biotechnology Research Center, Shanghai Key Laboratory of Agro-biotechnology, School of Agriculture and Biology, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Shanghai Jiao Tong University, Shanghai, People's Republic of China
Ting-wen Bao
School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, People's Republic of China
Liang Ran
School of Life Science and Biotechnology, Shanghai Jiao Tong University, Shanghai, People's Republic of China
Juan Lin
College of Biological Sciences and Technology, Fuzhou University, Fuzhou, Fujian, China; Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou, Fujian, China
Xuan-Wei Zhou
School of Agriculture and Biology and Engineering Research Center of Therapeutic Antibody (Ministry of Education), Shanghai Jiao Tong University, Shanghai, People's Republic of China

ABSTRACT

The FIP-glu (Lingzhi-8 or LZ-8) isolated from medicinal mushroom Ganoderma lucidum (Lingzhi or Reishi) was the first identified and characterized fungal immunomodulatory protein (FIP), and its biological functions have been explored extensively. On the basis of cloned LZ-8 gene sequence from the genomic DNA of G. lucidum, we expressed FIP-glu by the expression cassette vector pQE-30. The recombinant protein was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Matrix-assisted laser desorption/ ionization mass spectrometry (MALDI-MS). Finally, its bioactivity was examined by inducing expression of cytokine genes in mouse spleen cells. The results showed that recombinant FIP-glu protein could be expressed in E. coli successfully. The yield of recombinant FIP-glu accounted for 51.1% of the total protein of E. coli, while soluble recombinant FIP-glu accounted for 55.4% of the total soluble protein of E. coli. The purity of recombinant FIP-glu protein was more than 90% after purification. Analysis of RT-PCR demonstrated that the recombinant FIP-glu could enhance the transcription of interleukin (IL)-2, IL-3, IL-4, interferon (IFN)-γ, tumor necrosis factor (TNF)-α, and IL-2 receptor (IL-2R) genes in mouse spleen cells.


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