ABSTRACT
Plant cell surface pattern recognition receptors (PRRs) and intracellular immune receptors cooperate to provide immunity to microbial infection. Both receptor families have coevolved at an accelerated rate, but the evolution and diversification of PRRs is poorly understood. We have isolated potato surface receptor Pep-13 receptor unit (PERU) that senses Pep-13, a conserved immunogenic peptide pattern from plant pathogenic Phytophthora species. PERU, a leucine-rich repeat receptor kinase, is a bona fide PRR that binds Pep-13 and enhances immunity to Phytophthora infestans infection. Diversification in ligand binding specificities of PERU can be traced to sympatric wild tuber-bearing Solanum populations in the Central Andes. Our study reveals the evolution of cell surface immune receptor alleles in wild potato populations that recognize ligand variants not recognized by others.
Subject(s)
Phytophthora infestans , Plant Immunity , Receptors, Immunologic , Solanum tuberosum , Ligands , Receptors, Immunologic/genetics , Receptors, Immunologic/metabolism , Solanum tuberosum/genetics , Solanum tuberosum/immunology , Solanum tuberosum/microbiologyABSTRACT
Plant pathogens cause recurrent epidemics, threatening crop yield and global food security. Efforts to retool the plant immune system have been limited to modifying natural components and can be nullified by the emergence of new pathogen strains. Made-to-order synthetic plant immune receptors provide an opportunity to tailor resistance to pathogen genotypes present in the field. In this work, we show that plant nucleotide-binding, leucine-rich repeat immune receptors (NLRs) can be used as scaffolds for nanobody (single-domain antibody fragment) fusions that bind fluorescent proteins (FPs). These fusions trigger immune responses in the presence of the corresponding FP and confer resistance against plant viruses expressing FPs. Because nanobodies can be raised against most molecules, immune receptor-nanobody fusions have the potential to generate resistance against plant pathogens and pests delivering effectors inside host cells.
Subject(s)
Disease Resistance , Plant Diseases , Receptors, Immunologic , Single-Domain Antibodies , Disease Resistance/immunology , Genotype , Receptors, Immunologic/immunology , Single-Domain Antibodies/immunology , Plant Diseases/immunology , Plant Diseases/prevention & control , Luminescent ProteinsABSTRACT
Ca(II)-alginate beads are being produced for a broad spectrum of biotechnological uses. Despite the simplicity of their manufacturing process, in these highly complex arrangements, the final properties of the material strongly depend on the supramolecular scaffolding. Here we present a cost-effective automatized Optical Video Microscopy approach for in situ evaluation of the kinetics of alginate bead formation. With simple mathematic modeling of the acquired data, we obtained key parameters that reveal valuable information on the system: the time course of gel-front migration correlates with the plateau of the storage module, and total volume shrinkage is highly related to the stabilization of shear strain and shear stress at the yield point. Our results provide feasible and reproducible tools, which allow for a better interpretation of bead formation kinetics and a rapid screening technique to use while designing gelling materials with specific properties for technological applications.
