Rotem Sorek

This study identifies a bacterial defense system, Metis, that detects virus-induced genome degradation through methylated mononucleotides, leading to inhibition of phage infection.

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

The paper designs synthetic proteins that inhibit bacterial defense systems, enabling phage infection and plasmid transformation in otherwise resistant strains.

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 identifies a bacterial defense mechanism, aRES, that depletes NAD+ by producing ADPR-1P, which resists phage NARP1 reconstitution, and describes phage countermeasures including phosphatases and inhibitors.

This study identifies RyDEP as an enzyme that degrades 2'cADPR and 3'cADPR immune signals, inactivating bacterial defense and restoring NAD+.

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 systematically identifies TIR-based immune signaling systems in bacteria, finding they exist in 8% of bacterial genomes and use signaling molecules similar to those in plant and human immunity.

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 identifies Acb4, a viral protein that inhibits bacterial anti-phage defense by sequestering nucleotide signals.

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

This study identifies two phage pathways, NARP1 and NARP2, that reconstitute NAD+ from its degradation products to counter bacterial immunity.

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.

The paper shows short prokaryotic Argonautes, when associated with Sir2, deplete NAD+ to defend against invading DNA.

The paper quantifies age-related somatic mutations and epimutations in a wild Populus trichocarpa tree over 330 years, showing lower mutation rates than annuals and distinct epimutation origins.