Pseudomonas syringae HopN1 Binds Plant VAP12 and a Rho-GTPase, Suggesting a Role in Membrane-Associated Processes
Charlotte Brinkmann1, Jennifer Bortlik1,2, Frederik Börnke1,3
1Plant Metabolism Group, Leibniz-Institute of Vegetable and Ornamental Crops (IGZ), Großbeeren, Germany.
Contact (Thousand Oaks (Ventura County, Calif.))
|September 8, 2025
Summary
Bacterial type III effector proteins (T3Es) mimic host FFAT motifs to interact with VAMP-associated proteins (VAPs). Pseudomonas syringae
Area of Science:
- Microbiology
- Plant Pathology
- Molecular Biology
Background:
- Gram-negative bacterial pathogens use type III effector proteins (T3Es) to manipulate host cells and evade immunity.
- Some T3Es mimic eukaryotic FFAT (two phenylalanines in an acidic tract) motifs, interacting with VAMP-associated proteins (VAPs) to target host membranes.
- The role and prevalence of FFAT mimicry in bacterial pathogenesis are not well understood.
Purpose of the Study:
- To investigate FFAT motif mimicry in T3Es of the plant pathogen *Pseudomonas syringae* pv. *tomato* (Pst) DC3000.
- To characterize the interaction of the Pst T3E HopN1 with host proteins.
Main Methods:
- Bioinformatic analysis of Pst DC3000 T3Es for FFAT motifs.
- Yeast two-hybrid assays to detect protein-protein interactions.
- In planta co-immunoprecipitation assays to confirm interactions in a host environment.
Main Results:
- The Pst T3E HopN1 contains a functional FFAT motif.
- HopN1 interacts with plant VAP proteins (e.g., VAP12) and a plant RHO-GTPase.
- These interactions suggest a potential role for HopN1 in membrane localization and host manipulation.
Conclusions:
- HopN1 utilizes FFAT mimicry to interact with plant VAPs, potentially influencing its subcellular localization.
- The interaction with RHO-GTPase suggests functional parallels with mammalian YopT.
- Further research is needed to confirm the functional significance of FFAT mimicry and VAP interaction in HopN1 virulence.
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