P-048 - Investigating protein phosphorylation changes during effector-triggered immunity.

Recent advances have shown that NLR activation leads to the assembly of a transmembrane complex known as the resistosome, a calcium-permeable channel and pivotal initiation event in Effector-Triggered Immunity (ETI). The influx of calcium through the resistosome induces cellular changes lead to the disease resistance. Since many studies have already shown the importance of calcium-dependant events during Pattern-triggered immunity, we hypothesized that calcium influx brought about by the ETI also induces post-transcriptional changes in the plant proteome, leading to the immune reaction. We have used a transgenic plant system that allows us to induce an ETI response, based on the tobacco N protein and the tobacco mosaic virus p50 protein, without the presentation of Pathogen-associated molecular patterns (PAMPs), and which has been shown previously to induce an ETI response that inhibits virus RNA translation. We combined this PAMP-free inducible system with a mass-spectrometry-bases analysis to identify proteins whose activity is altered during an ETI response. We expect our study to provide new insights into the proteins responsible for executing the immune response activated by the resistosome and improve our understanding of the execution pathways for antiviral and/or antibacterial immunity.