Here below you will find our most important Sino-German joint publications starting from January 2019. For joint publications until December 2018:
SGVIVI members are marked in bold.
Essen, Bochum and Wuhan, October 2020Susceptibility of SARS-CoV-2 to UV irradiation
Essen and Wuhan, September 2020Impaired Cytotoxic CD8 + T Cell Response in Elderly COVID-19 Patients
. 2020 Sep 18;11(5):e02243-20. doi: 10.1128/mBio.02243-20.Bio
Essen and Wuhan, September 2020O-GlcNAcylation modulates HBV replication through regulating cellular autophagy at multiple levels
Essen and Wuhan, August 2020Major Vault Protein Promotes Hepatocellular Carcinoma Through Targeting Interferon Regulatory Factor 2 and Decreasing p53 Activity.
Essen and Wuhan, July 2020Controversial: Early Innate Responses to Hepatitis B Virus Infection, an Explanation for Viral Persistence?
Essen and Shanghai, April 2020Functional Comparison of IFN-α Subtypes Reveals Potent HBV Suppression by a Concerted Action of IFN-α and -γ Signaling
Chen J, Li Y, Lai F, Wang Y, Sutter K, Dittmer U, Ye J, Zai W, Liu M, Shen F, Wu M, Hu K, Li B, Lu M, Zhang X, Zhang J, Li J, Chen Q, Yuan Z.
Hepatology. 2020 Apr 25. doi: 10.1002/hep.31282. [Epub ahead of print]
Essen, April 2020Invention by SGVIVI members: Artificial Interferons
Chimeric mutants of interferon alpha 2 and other interferon alpha subtypes with improved antiviral activity
The SGVIVI members Ulf Dittmer and Kathrin Sutter have discovered that IFNα14 is more efficient for the treatment of HBV and HIV infections, whereas the most potent IFNα subtype against Influenza Virus is IFNα16. These findings were not only generated in vitro, but also in humanized mouse models and human organoid cultures. Based on these and earlier findings regarding the different antiviral activities of IFNα subtypes, the researchers designed chimeric mutants of the known IFNα2 and IFNα6/IFNα14/IFNα16 proteins that use the IFNα2 backbone, which is clinically well-established, with a variety of point mutations derived from the IFNα6/IFNα14/IFNα16 amino acid sequences that show significantly higher antiviral activity than IFNα2. More
Please also see the relevant joint publication here above: Chen J., et al.(2020)
Wuhan and Essen, November 2019 MVP promotes hepatocellular carcinoma via targeting IRF2 and decreasing p53 activity.
Yu H, Li M, He R, Fang P, Wang Q, Yu Yu, Wang F, Zhou L, ZhangY, Chen A, Peng N, Liu D, Trilling M, Broering R, Wiemer EAC, Lu M, Zhu Y, Liu S
Major vault protein (MVP) is up regulated during infections with hepatitis B and C virus. Here, we found that MVP deficiency inhibited hepatocellular carcinoma (HCC) development induced by di-ethyl-nitrosamine (DEN), HBx, and HCV Core. Forced MVP expression was sufficient to induce HCC in mice. Mechanistic studies demonstrate that the ubiquitin ligase Human Double Minute 2 (HDM2) forms mutual exclusive complexes either with interferon regulatory factor 2 (IRF2) or with p53. In presence of MVP, HDM2 is liberated from IRF2 leading to the ubiquitination of the tumor suppressor p53. Mouse xenograft models showed that Hepatitis B and C virus promote carcinogenesis through MVP induction, resulting in a loss of p53 mediated by HDM2. Analyses of clinical samples from chronic hepatitis B, liver cirrhosis, and HCC revealed that MVP upregulation correlates with several hallmarks of malignancy, and associates with poor overall survival. Taken together, through the sequestration of IRF2, MVP promotes an HDM2-dependent loss of p53 that promotes HCC development.