Ilya А. Osterman

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

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 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.

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

This study identifies macrolactin A as an inhibitor of bacterial protein synthesis by targeting EF-Tu, revealing its mechanism of action as an elfamycin-like antibiotic.

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

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

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

This paper investigates how thermorubin inhibits translation by causing ribosome stalling and affecting tRNA binding and translation elongation.

The paper discovers a new LAP antibiotic, phazolicin, which inhibits bacterial ribosomes in a species-specific manner by blocking the exit tunnel.