Contributors: Longin, Hannelore/0000-0001-8524-5768; Hendrix , Hanne; Itterbeek, Annabel; Longin, Hannelore; Delanghe, Lize; Vriens, Eveline; Vallino, Marta; Lammens, Eveline-Marie; Haque, Farhana; Yusuf, Ahmed; NOBEN, Jean-Paul; Boon, Maarten; Koch, Matthias D.; van Noort, Vera; Lavigne, Rob
نبذة مختصرة : Type IV pili (T4P) are thin, flexible filaments exposed on the cell surface of gram-negative bacteria and are involved in pathogenesis-related processes, including cell adsorption, biofilm formation, and twitching motility. Bacteriophages often use these filaments as receptors to infect host cells. Here, we describe the identification of a protein that inhibits T4P assembly in Pseudomonas aeruginosa, discovered during a screen for host factors influencing phage infection. We show that expression of PA2560 (renamed PlzR) in P. aeruginosa inhibits adsorption of T4P-dependent phages. PlzR does this by directly binding the T4P chaperone PilZ, which in turn regulates the ATPase PilB and results in disturbed T4P assembly. As the plzR promoter is induced by cyclic di-GMP, PlzR might play a role in coupling T4P function to levels of this second messenger. ; We thank Prof. Abram Aertsen (Laboratory of Food Microbiology, KU Leuven, Heverlee, Belgium) for his practical advice and valuable discussions. This research was financially supported by the KU Leuven Project C1 ACES [C16/20/001] (H.H., H.L.). M.B. was funded by a grant from the Special Research Fund [iBOF/21/092]. M.K. was supported by generous startup funds provided by Texas A&M University.
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