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Immunopathology of Virus Infections

ISG20, a host nuclease that degrades HBV’s cccDNA

Together with our institute colleagues from the group of Ulrike Protzer and many other collaborating laboratories, we identified a new anti-HBV host factor, ISG20. This protein is induced upon interferon treatment and works in concert with APOBEC3 proteins to degrade HBV’s cccDNA in the nucleus of infected cells. By using affinity purification mass spectrometry, our laboratory (Chris/Andreas) confirmed the targeting of APOBEC3-modified cccDNA mimetics by ISG20.

Beautiful story and great work spearheaded by Daniela Stadler!

Read more in the EMBO Reports paper: Interferon-induced degradation of the persistent hepatitis B virus cccDNA form depends on ISG20

Our multi-omics analysis of SARS-COV-2 and SARS-CoV – in Nature!

An example from our COVINET showing the regulation of PLAU upon infection, as well as its interaction with the ORF8 of CoV2.

We applied multi-omics data analysis to understand the interactions and impact of SARS-CoV-2 and SARS-CoV on the human proteome. In particular, we applied state of the art bioinformatics methods to precisely characterize what SARS-CoV-2 and SARS-CoV do to the proteome and provide links to potential molecular mechanism leading to COVID-19. Moreover, we established an integrated database (https://covinet.innatelab.org) that allows us to search for the effect of SARS-CoV-2 and SARS-CoV infection.

 

Congratulations to this tour de force to all involved people in our lab, particularly, Alexey, Virginie, Vincent, Valter, Chris, Darya and Yiqi as well as Ozge Karayel and Matthias Mann with whom we tightly collaborated. Moreover, we thank many other contributors who were instrumental to get this over the line! 

Please read our original manuscript published in Nature:

Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV

Feel free to dive into the data at:

https://covinet.innatelab.org

New paper on inflammasome activation by dsRNA published in Science!

Virus generated dsRNA directly binds to NLRP1 to activate the inflammasome. NLRP1 has a quite restricted expression pattern and therefore this type of inflammasome activation escaped the attention thus far. Through the use of our virus collection, we identified the activation of NLRP1 by the dsRNA producing virus Semliki forest virus. The paper just got online in Science, great stuff.

The article can be found here.