Philip J. Kranzusch

The paper identifies a bacterial anti-phage defense system called Panoptoo, which uses DAC enzymes to synthesize nucleotide signals that counteract phage immune evasion.

The paper shows human ISGs can restrict bacterial phage replication, revealing conserved antiviral mechanisms across kingdoms.

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

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

This study determines the structural basis of QueC-family protein function in the qatABCD anti-phage defense system, showing their role in targeting protein substrates for N-terminal modification.

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 phage protease activation of CBASS immunity by cleaving CD-NTase activation loops, revealing a conserved mechanism for antiviral defense.

This study identifies a bacterial anti-phage defense system, Clover, which uses nucleotide signals to dynamically regulate antiviral immunity while avoiding cellular toxicity.

The paper identifies that giant DNA viruses encode a functional IF4F translation initiation complex, enabling viral protein synthesis and challenging the distinction between cellular and acellular biology.

This study determines the structure of HSV-1 helicase-primase inhibited by HPIs and reveals how it interacts with the replication fork complex.

The paper identifies 7-deazapurine protein conjugation as essential for type IV CBASS immunity, revealing the roles of Cap9 and Cap10 in this process.

The paper identifies a cGLR-STING signaling pathway in choanoflagellates, showing evolutionary links between bacterial and animal immunity.

The paper analyzes 16 nuclease-NTPase systems to identify shared features controlling bacterial anti-phage defense, revealing universal protein complex formation and broad nucleic acid degradation capabilities.

The paper shows that HIV-1 capsids protect reverse-transcribed DNA from cGAS detection, and that disrupting the capsid enhances cGAS activity.

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

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.

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

The paper identifies recurrent loss-of-function mutations in OAS1 across primates, showing that the cytotoxic effects of OAS1 activation can outweigh its antiviral benefits, leading to reduced catalytic activity.