Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/44609
Title: PlzR regulates type IV pili assembly in Pseudomonas aeruginosa via PilZ binding
Authors: 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
Issue Date: 2024
Publisher: NATURE PORTFOLIO
Source: Nature communications, 15 (1) (Art N° 8717)
Abstract: 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.
Notes: Lavigne, R (corresponding author), Katholieke Univ Leuven, Dept Biosyst, Lab Gene Technol, Heverlee, Belgium.
rob.lavigne@kuleuven.be
Keywords: Protein Binding;Cyclic GMP;Gene Expression Regulation, Bacterial;Promoter Regions, Genetic;Molecular Chaperones;Oxidoreductases;Pseudomonas aeruginosa;Fimbriae, Bacterial;Bacterial Proteins;Fimbriae Proteins
Document URI: http://hdl.handle.net/1942/44609
e-ISSN: 2041-1723
DOI: 10.1038/s41467-024-52732-5
ISI #: 001331421200001
Datasets of the publication: https://doi.org/10.5281/zenodo. 11936574
Rights: The Author(s) 2024. Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http:// creativecommons.org/licenses/by-nc-nd/4.0/.
Category: A1
Type: Journal Contribution
Appears in Collections:Research publications

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