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国际药用蘑菇期刊
影响因子: 1.423 5年影响因子: 1.525 SJR: 0.431 SNIP: 0.661 CiteScore™: 1.38

ISSN 打印: 1521-9437
ISSN 在线: 1940-4344

国际药用蘑菇期刊

DOI: 10.1615/IntJMedMushrooms.2018026264
pages 537-548

Computational Insights into the Molecular Mechanism of the High Immunomodulatory Activity of LZ-8 Protein Isolated from the Lingzhi or Reishi Medicinal Mushroom Ganoderma lucidum (Agaricomycetes)

Da-Peng Bao
National Engineering Research Center of Edible Fungi, Ministry of Science and Technology (MOST), Key Laboratory of Edible Fungal Resources and Utilization (South), Key Laboratory of Agricultural Genetics and Breeding of Shanghai, Institute of Edible Fungi, Shanghai Academy of Agricultural Sciences, Shanghai 201403, China
Rui Bai
College of Food Science, Shanghai Ocean University, Shanghai, People's Republic of China
Ying-Nv Gao
National Engineering Research Center of Edible Fungi; Key Laboratory of Applied Mycological Resources and Utilization, Ministry of Agriculture; Shanghai Key Laboratory of Agricultural Genetics and Breeding, Institute of Edible Fungi, Shanghai Academy of Agriculture Science, Shanghai, People's Republic of China
Ying-Ying Wu
National Engineering Research Center of Edible Fungi, Ministry of Science and Technology (MOST), Key Laboratory of Edible Fungal Resources and Utilization (South), Key Laboratory of Agricultural Genetics and Breeding of Shanghai, Institute of Edible Fungi, Shanghai Academy of Agricultural Sciences, Shanghai 201403, China
Ying Wang
National Engineering Research Center of Edible Fungi; Key Laboratory of Applied Mycological Resources and Utilization, Ministry of Agriculture; Shanghai Key Laboratory of Agricultural Genetics and Breeding, Institute of Edible Fungi, Shanghai Academy of Agriculture Science, Shanghai, People's Republic of China

ABSTRACT

Ling zhi-8 (LZ-8) is the first fungal immunomodulatory protein (FIP) isolated from the lingzhi or reishi medicinal mushroom, Ganoderma lucidum. LZ-8 effectively induces interleukin 2 expression and secretion by forming a stable homodimer, and it is regarded as a good candidate to become a new therapeutic agent and/or functional food supplement. However, the molecular mechanism by which LZ-8 dimerization influences the regulation of interleukin 2 is not clear. In this study we performed structure-based multiple alignment of LZ-8 and an FIP from Volvariella volvacea, compared the electrostatic potential of their protein surfaces, and developed a model summarizing the unique electrostatic interaction in LZ-8 dimerization. In addition, further electrostatic potential and virtual amino acid mutation analyses suggested that L10, W12, and D45 are the key amino acid residues responsible for the protein's high immunomodulatory activity. These findings may provide useful insights into the design and construction of a new FIP mutant for use in treating and preventing autoimmune diseases.


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