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)
文献类型： 外文期刊
作者： Bao, Da-Peng 1 ; Bai, Rui 4 ; Gao, Ying-Nv 1 ; Wu, Ying-Ying 1 ; Wang, Ying 1 ;
作者机构： 1.Natl Engn Res Ctr Edible Fungi Key, Shanghai, Peoples R China
2.Minist Agr, Key Lab Appl Mycol Resources & Utilizat, Shanghai, Peoples R China
3.Shanghai Acad Agr Sci, Inst Edible Fungi, Shanghai Key Lab Agr Genet & Breeding, Shanghai, Peoples R China
4.Shanghai Ocean Univ,
关键词： dimerization; electrostatic interaction; fungal immunomodulatory proteins (FIPs); Ganoderma lucidum; LZ-8; medicinal mushrooms; protein-protein docking
期刊名称：INTERNATIONAL JOURNAL OF MEDICINAL MUSHROOMS （ 影响因子：1.921； 五年影响因子：1.879 ）
ISSN： 1521-9437
年卷期： 2018 年 20 卷 6 期
页码：
收录情况： SCI
摘要： Ling zhi-8 (LZ-8) is the first fungal immunomodulatory protein (HP) 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 volyacca, 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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