All plants encounter threats to their health from pathogens, including bacteria, viruses and fungi in the environment.
A protein-based innate immune system allows plants to respond and protect themselves from pathogen attack via the activation of molecular defences.
However, pathogens have evolved strategies to suppress this initial plant immune response. Among these tactics is the introduction of effector proteins directly into a plant cell to inhibit its immune proteins, leading to evasion of the plant’s defence mechanisms.
The Nucleotide-Binding Leucine-Rich-Repeat (NLR) Immune Receptors are a protein superfamily which function to detect pathogen effectors in a process termed Effector Triggered Immunity (ETI); the plant’s secondary response to pathogen attack.
The NLR protein pair RRS1/RPS4 contributes to the ETI response of Arabidopsis thaliana by detecting the presence of the effector AvrRPS4 from the phytopathogen Pseudomonas syringae.
I am interested to understand the molecular interactions between RRS1/RPS4 and AvrRPS4. My work involves purification of these proteins from either N. benthamiana or E. coli as protein expression hosts. I aim to produce a 3D structure depicting this interaction via X-ray crystallography.