Gil Amitai

This study shows that XopQ, a bacterial virulence protein, cleaves 2'cADPR to suppress plant TIR immune signaling and promote pathogen virulence.

The paper investigates the functional diversity of phage sponge proteins that sequester host immune signals, identifying new specificities against CBASS, Pycsar, and Thoeris systems.

The paper shows a secreted bacterial protease reduces phage infectivity by degrading phage DNA, with phages escaping by mutating a tail-associated protein.

This study shows that TIR domains in animals, including human TLR4, have conserved catalytic activity that produces cADPR and is essential for TLR4 signaling.

The paper identifies viral proteins that manipulate bacterial immune signaling by analyzing structural and biophysical traits, and develops a computational pipeline to predict such proteins in phage genomes.

The paper identifies His-ADPR as a novel TIR-derived immune signaling molecule in bacteria, showing its role in phage defense and structural basis for recognition.

This study identifies a bacterial immune system where TIR-domain proteins activate caspase-like proteases to induce cell death and block phage replication.

The paper shows that KpAvs2 recognizes a different phage protein, Ksap1, during infection compared to heterologous co-expression assays.

This study shows that SARM1 TIR domains produce minor amounts of glycocyclic ADPR molecules in vitro and in bacterial cells, suggesting a potential role in axonal death.

This study identifies anti-defense proteins in phages that inhibit bacterial immune systems like Gabija, Thoeris, and Hachiman.