XopM, An FFAT Motif-Containing Type III Effector Protein From Xanthomonas, Suppresses MTI Responses at the Plant

Charlotte Brinkmann1, Jennifer Bortlik1, Margot Raffeiner1,2

  • 1Plant Metabolism Group, Leibniz-Institute of Vegetable and Ornamental Crops (IGZ), Großbeeren, Germany.

Molecular Plant Pathology
|December 10, 2024
PubMed

Insights

Xanthomonas campestris pv. vesicatoria

Area of Science:

  • Plant pathology
  • Bacteriology
  • Molecular biology

Background:

  • Gram-negative bacteria utilize type III effector proteins (T3Es) to suppress host immunity and cause disease.
  • The molecular functions of many T3Es remain uncharacterized, hindering our understanding of bacterial pathogenesis.
  • Xanthomonas campestris pv. vesicatoria (Xcv) employs numerous T3Es, including XopM, to overcome plant defenses and establish infection.

Purpose of the Study:

  • To elucidate the molecular function and host interaction of XopM, a T3E from Xcv.
  • To investigate the role of XopM in suppressing plant immunity and promoting bacterial virulence.
  • To determine the structural and functional relationship between XopM's VAP interaction and its immune-suppressive activity.

Main Methods:

  • Investigated XopM's interaction with vesicle-associated membrane protein (VAMP)-associated proteins (VAPs) using isoform-specific assays.
  • Analyzed XopM for FFAT motifs and assessed their role in VAP binding and host membrane localization.
  • Evaluated XopM's ability to suppress plant immunity by measuring reactive oxygen species production and supporting nonpathogenic bacterial growth.

Main Results:

  • XopM interacts with VAPs in an isoform-specific manner, mediated by two FFAT motifs.
  • XopM localizes to the host membrane system and suppresses microbe-associated molecular pattern-triggered immunity (MTI).
  • The VAP interaction and MTI suppression are separable but require membrane localization for full activity.

Conclusions:

  • XopM utilizes FFAT motifs to target host membranes, interfering with early MTI responses.
  • XopM's ability to suppress plant immunity is linked to its membrane association.
  • Understanding XopM's mechanism provides insights into bacterial virulence strategies and host-pathogen interactions.

Related Concept Videos

Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
8.0K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.0K
Antimicrobial Proteins01:23

Antimicrobial Proteins

Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
900
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.1K
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
1.9K