Structural basis for broad anti-phage immunity by DISARM

Jack P. K. Bravo, Cristian Aparicio-Maldonado, Franklin L. Nobrega, Stan J. J. Brouns () and David W. Taylor ()
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Jack P. K. Bravo: University of Texas at Austin
Cristian Aparicio-Maldonado: Delft University of Technology
Franklin L. Nobrega: University of Southampton
Stan J. J. Brouns: Delft University of Technology
David W. Taylor: University of Texas at Austin

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract In the evolutionary arms race against phage, bacteria have assembled a diverse arsenal of antiviral immune strategies. While the recently discovered DISARM (Defense Island System Associated with Restriction-Modification) systems can provide protection against a wide range of phage, the molecular mechanisms that underpin broad antiviral targeting but avoiding autoimmunity remain enigmatic. Here, we report cryo-EM structures of the core DISARM complex, DrmAB, both alone and in complex with an unmethylated phage DNA mimetic. These structures reveal that DrmAB core complex is autoinhibited by a trigger loop (TL) within DrmA and binding to DNA substrates containing a 5′ overhang dislodges the TL, initiating a long-range structural rearrangement for DrmAB activation. Together with structure-guided in vivo studies, our work provides insights into the mechanism of phage DNA recognition and specific activation of this widespread antiviral defense system.

Date: 2022
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DOI: 10.1038/s41467-022-30673-1

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