9e4w

Structure of Bacillus phage SPO1 anti-CBASS 4 (Acb4) in complex with 3'3'-cGAMP

spinqualitylabelsall models 9e4w, resolution 2.08Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9e4w is a 20 chain structure with sequence from Bacillus phage SPO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.08Å Ligands: 4BW Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B6V2Y3_BPSP1 Publication Abstract from PubMed Cyclic oligonucleotide-based antiviral signaling systems (CBASS) are bacterial anti-phage defense operons that use nucleotide signals to control immune activation. Here we biochemically screen 57 diverse E. coli and Bacillus phages for the ability to disrupt CBASS immunity and discover anti-CBASS 4 (Acb4) from the Bacillus phage SPO1 as the founding member of a large family of >1,300 immune evasion proteins. A 2.1 A crystal structure of Acb4 in complex with 3'3'-cGAMP reveals a tetrameric assembly that functions as a sponge to sequester CBASS signals and inhibit immune activation. We demonstrate Acb4 alone is sufficient to disrupt CBASS activation in vitro and enable immune evasion in vivo. Analyzing phages that infect diverse bacteria, we explain how Acb4 selectively targets nucleotide signals in host defense and avoids disruption of cellular homeostasis. Together, our results reveal principles of immune evasion protein evolution and explain a major mechanism phages use to inhibit host immunity. A widespread family of viral sponge proteins reveals specific inhibition of nucleotide signals in anti-phage defense.,Chang RB, Toyoda HC, Hobbs SJ, Richmond-Buccola D, Wein T, Burger N, Chouchani ET, Sorek R, Kranzusch PJ bioRxiv [Preprint]. 2024 Dec 31:2024.12.30.630793. doi: , 10.1101/2024.12.30.630793. PMID:39803557 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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