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SJTU Researchers Discovered N-Glycosylated Ganoderma FIPs Improved Anti-inflammatory Activity

May 07, 2021      Author:

On April 26, the research team led by Prof. Zhou Xuanwei from School of Agriculture and Biology, SJTU published their research article titled “N-Glycosylated Ganoderma lucidum immunomodulatory protein improved anti-inflammatory activity via inhibition of the p38 MAPK pathway” on the website of Food & Function 2021,12, 3393-3404. This research indicated that N-linked glycans could improve the biotic function of Ganoderma lucidum fungal immunomodulatory protein (FIP-glu), thus paving way for the application of FIPs in food, cosmeceuticals, and medicine.


Ganoderma spp, a traditional edible fungus in China, has been classified into the national pharmacopoeia and also approved by the state as a new resource food. The fungal immunomodulatory proteins (in Ganoderma are important bioactive substances with extensive medicinal values in treatment against cancer, allergy, immune rejection, and in immune regulation, etc.


The research found that N-linked FIP-glu could improve anti-inflammatory activity via inhibition of p38 MAPK phosphorylation.

Dr. Li Qizhang (professor of Hubei University of Technology) and Dr. Chen Xin (postdoctoral research fellow at Stanford University, School of Medicine) are the co-first authors. Prof. Zhou Xuanwei from SJTU is the only corresponding author. Master students Mao Peiwen, Jin Mengyuan, and Wu Qin also made their share of contributions to the project. This research has been sponsored by Entrust projects  (19H10000039320H100000595) of enterprises and institutions.



Source: School of Agriculture and Biology, SJTU

Translated by Zhang Wenying

Proofread by Xiao Yangning, Fu Yuhe



The global health emergency generated by coronavirus disease-2019 has prompted the search for immunomodulatory agents. There are many potential natural products for drug discovery and development to tackle this disease. One of these candidates is the Ganoderma lucidum fungal immunomodulatory protein (FIP-glu). In the present study, we clarify . Four proteins, including FIP-glu (WT) and its mutants N31S, T36N and N31S/T36N, were successfully expressed in P. pastoris, of which T36N and N31S/T36N were glycoproteins. After treatment with peptide-N-glycosidase F, the results of SDS-PAGE and Western blot showed that the glycan moiety was removed completely, indicating that the glycan moiety was N-linked. This was also demonstrated by UPLC-qTOF-MS. The cytotoxicity assay showed that N-linked glycans decreased the cytotoxicity of WT; while, the RT-qPCR assay showed that N-glycosylated WT regulated the mRNA expression of IL-6 and TGF-β1. The Western blot results showed that N-glycosylated WT reduced the phosphorylation level of p38 MAPK. In conclusion, our findings revealed a novel mechanism by which N-glycosylation of FIP-glu improved its anti-inflammatory activity through the regulation of the expression of inflammatory cytokines in RAW264.7 via inhibition of p38 MAPK phosphorylation. It was proved that N-glycosylation significantly improved the functional properties of FIP-glu,