PlzR regulates type IV pili assembly in Pseudomonas aeruginosa via PilZ binding

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.

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Publication Details

Journal
Nature Communications
Published
2024-10-08
DOI
https://doi.org/10.1038/s41467-024-52732-5
Citations
10
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
5.50

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article

PlzR regulates type IV pili assembly in Pseudomonas aeruginosa via PilZ binding

Vera van Noort, Marta Vallino, Eveline‐Marie Lammens, A. Van Ítterbeek et al.
10 citations
Nature Communications
Bacterial Genetics and Biotechnology
5.50
article

PlzR regulates type IV pili assembly in Pseudomonas aeruginosa via PilZ binding

Vera van Noort, Marta Vallino, Eveline‐Marie Lammens, A. Van Ítterbeek, Matthias D. Koch, Jean‐Paul Noben, Rob Lavigne, Hanne Hendrix, Lize Delanghe, Maarten Boon, Hannelore Longin, Farhana Haque, Ahmed Yusuf, Eveline Vriens
article en
10 citations

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.

Nature CommunicationsVol. 15(1)
Leiden University (NL), Institute for Sustainable Plant Protection (IT), Transnational University Limburg (BE), National Research Council (IT), Hasselt University (BE), Texas A&M University (US), KU Leuven (BE)
Texas A and M University, KU Leuven, Bijzonder Onderzoeksfonds UGent
Zero hunger
Openalex Percentile: Top 4%
Bacterial Genetics and Biotechnology
5.50
DOIOpen Access PDFOpenAlex
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