Poster
Johana Misas Villamil
University of Cologne
Cologne, Nordrhein-Westfalen, Germany
Daniel Moser
University of Cologne
Koeln, Nordrhein-Westfalen, Germany
Nina Solia
University of Cologne
Köln, Nordrhein-Westfalen, Germany
Christian-Frederic Kaiser
Institute for Cell and Interaction Biology, Heinrich Heine University of Duesseldorf
Duesseldorf, Nordrhein-Westfalen, Germany
Lioba Rüger
Max Planck Institute for Plant Breeding
Köln, Nordrhein-Westfalen, Germany
Parisa Kakanj
University of Cologne
Köln, Nordrhein-Westfalen, Germany
Lucie Hansen
University of Cologne
Köln, Nordrhein-Westfalen, Germany
Guido Grossmann
Prof. Dr.
Heinrich-Heine-Universitaet Duesseldorf- ICIB
Düsseldorf, Nordrhein-Westfalen, Germany
Tonni Andersen
Max Planck Institute for Plant Breeding
Köln, Nordrhein-Westfalen, Germany
Gunther Doehlemann
Professor
University of Cologne
Cologne, Nordrhein-Westfalen, Germany
Papain-like cysteine proteases (PLCPs) are hubs in plant immunity, targeted by pathogen effectors due to their ability to release microbe- and damage-associated molecular patterns. While their role in activating salicylic acid (SA)-mediated defense responses in maize leaves is well-documented, their function in root-bacterial interactions remains unexplored. We hypothesize that non-pathogenic bacteria modulate root immunity by inhibiting SA-associated PLCPs. Pseudomonas species exhibit diverse lifestyles. The pathogen P. syringae pv. tomato produces a chagasin-like inhibitor, Cip1, which enhances virulence on tomato by inhibiting PLCPs. Cip1 is a conserved lipoprotein in Pseudomonads, including P. putida, a prominent root-associated commensal. Fluorescent microscopy and biochemical assays confirmed Cip1’s surface localization on P. putida. Moreover, Cip1 influences the composition of a maize synthetic community (SynCom), particularly at early colonization stages, where Cip1-deficient P. putida mutants show reduced colonization. In Arabidopsis roots, Cip1 promotes early colonization in the meristematic and elongation zones. Our findings suggest that Cip1 may protect bacterial surface proteins from proteolytic degradation by inhibiting plant PLCPs, potentially preventing the release of MAMPs that could trigger immune responses and hinder bacterial colonization. Alternatively, Cip1 could act as a public good, benefiting microbial colonization by modulating plant immunity.