XiaoPan Gao

Abstract Crimean-Congo hemorrhagic fever virus (CCHFV), designated by the WHO as a priority pathogen under its R&D Blueprint for emerging epidemics, poses a major global health threat, yet licensed vaccines or specific antiviral treatments are lacking. As the sole viral enzyme responsible for genome replication and transcription, the CCHFV L protein is a large, multienzymatic protein, but its exceptional size (> 450 kDa) and extensive domain architecture have hindered structural analysis.

Keywords CRISPR-Cas Racrs structural Cas7f RacrIF1 crRNA Get full text access Log in, subscribe or purchase for full access. References 1. Hampton, H.G. ∙ Watson, B.N.J. ∙ Fineran, P.C. The arms race between bacteria and their phage foes Nature. 2020; 577:327-336 2. Mayo-Muñoz, D. ∙ Pinilla-Redondo, R. ∙ Birkholz, N. ... A host of armor: Prokaryotic immune strategies against mobile genetic elements Cell Rep. 2023; 42, 112672 3. Georjon, H. ∙ Bernheim, A.

Abstract The NADase activity of the defense-associated sirtuins (DSRs) is activated by the phage tail tube protein (TTP). Herein, we report cryo-EM structures of a free-state Bacillus subtilis DSR2 tetramer and a fragment of the tetramer, a phage SPR tail tube, and two DSR2-TTP complexes. DSR2 contains an N-terminal SIR2 domain, a middle domain (MID) and a C-terminal domain (CTD). The DSR2 CTD harbors the α-solenoid tandem-repeats like the HEAT-repeat proteins.