Abstract
The arms race between bacteria and phages led to the evolution of a wide range of anti-phage defences, several of which are controlled by host cell quorum sensing. In this work we characterize a novel quorum sensing anti-activator protein, known as anti-quorum sensing protein 1 (Aqs1), found in Pseudomonas phage DMS3. We show that Aqs1 inhibits LasR, the master regulator of quorum sensing, and present the X-ray crystal structure of the Aqs1-LasR complex. The 69-residue Aqs1 protein also inhibits PilB, the type IV pilus assembly ATPase protein. This study highlights the remarkable ability of small phage proteins to bind multiple host proteins and disrupt key biological pathways. In addition, this novel quorum sensing anti-activator provides a mechanism by which infecting phages can simultaneously dampen multiple anti-phage defences. As quorum-sensing systems are broadly distributed across bacteria, this mechanism of phage counter-defence likely plays an important role in phage-host evolutionary dynamics.
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