Analysis of evolutionary conserved viral nucleic acid binding proteins

We are very happy that our manuscript on evolutionary conserved viral nucleic acid binding proteins was published in Nature Communications.

It describes the most comprehensive evaluation of viral nucleic acid interactions in human, mouse and flies. We used conservation of binding properties over evolution to identify proteins that are relevant for innate immunity.

This was a great collaborative effort particularly between our laboratory and the laboratories of Jean-Luc Imler and Carine Meignin. Congratulations to Rike, Chris, Alexey, Line, Vincent, Teresa, Cathleen, Lila, Matthias & Andreas!    

Read more in the Nature Communications paper: Cross-species analysis of viral nucleic acid interacting proteins identifies TAOKs as innate immune regulators

Therapeutic potential of ACE2-IgG4-Fc fusion protein against SARS coronaviruses

In collaboration with Ulla Protzer’s and Johannes Buchner’s lab, without forgetting the engineering skills of Formycon AG, we set up and characterized how ACE2-IgG4-Fc fusion protein could provide us new therapeutic tools in our non-stopping fight against COVID-19. While this construct can neutralize all SARS coronaviruses, including its variants of concern, it also has an activity at the picomolar range.

Congratulation to all the people involved in this great study!

Read more in the Antiviral Research paper: Picomolar inhibition of SARS-CoV-2 variants of concern by an engineered ACE2-IgG4-Fc fusion protein

Mechanism of transcriptional modulation by NS1 of Respiratory Syncytial Virus (RSV)

In a joint collaborative battle, Daisy Leung published a mechanism employed by NS1 of Respiratory Syncytial Virus (RSV) to modulate gene transcription: We (Valter/Philipp/Andreas) identified that NS1 binds to the mediator complex, an essential component of inducible gene expression. Jingjing and Daisy could show that NS1 thereby blunts the expression of genes associated with innate immunity.

Congratulations particularly to Jingjing, Nina, Jacqueline and Daisy, well done!

Read more in the Cell Reports paper: Nuclear-localized human respiratory syncytial virus NS1 protein modulates host gene transcription

HCMV infection induces citrullination to evade the antiviral defence

Gloria Griffante and colleagues (Santo Landolfo laboratory, University of Turin, Italy) discovered that HCMV infection induced protein citrullination, a post-translational modification catalyzed by PADs. In particular, the host defense protein IFIT1 was citrullinated by PAD2 and treatment with the enzyme impaired its ability to bind 5’PPP-RNA, thus constituting a novel immune evasion strategy. We contributed with mass-spectrometry and RNA-protein binding assays to characterize IFIT1 citrullination sites and PAD2-dependant modulation of its interaction with RNA.

Congratulations for this great work!

Read more in the Nature paper: Human cytomegalovirus-induced host protein citrullination is crucial for viral replication