Molecular and functional characterization of the plant immune receptor RLP32
K. FROEHLICH (1), E. Melzer (2), L. Fan (3), T. Nuernberger (3) (1) Center for Plant Molecular Biology, Department of Plant Biochemistry, Germany; (2) Center for Plant Molecular Biology, Department of Plant Biochemistry, Germany; (3) Center for Plant Molecular Biology, Department of Plant Biochemistry, Germany

Plants are able to detect pathogens via pattern recognition receptors (PRRs) that bind pathogen-associated molecular patterns (PAMPs), thereby inducing PAMP triggered immunity (PTI). Ralstonia solanacearum is a plant pathogenic bacterium causing wilt in a wide range of host species. Purification of R. s. cell extracts revealed a new PAMP, RsE, which is also conserved in E. coli. It is able to trigger early immune responses in A. thaliana, such as ethylene production and oxidative burst. Forward genetic analysis identified the receptor-like protein RLP32 as the receptor of RsE in A. thaliana. RLP32 is a leucine-rich repeat receptor protein lacking an intracellular kinase domain. Co-immunoprecipitation experiments showed an interaction of RLP32 with SOBIR1 as well as members of the SERK family. Solanaceous crops like tomato, tobacco and potato lack an RLP32-homolog and are susceptible towards R. solanacearum. After stable transformation of N. benthamiana with RLP32 immune responses are induced when elicitated with RsE, indicating that N. benthamiana gained responsiveness to R. solanacearum. We now aim to show enhanced resistance to R. solanacearum and potential other bacterial pathogens containing RsE by interfamily transfer of RLP32 to N. benthamiana and tomato as a proof of concept for a new strategy to produce multi-resistant transgenic crops.

Abstract Number: P17-523
Session Type: Poster