title: A one-step affinity-purification protocol to purify NB-LRR immune receptors from plants that mediate resistance to fungal pathogens.
abstract: Nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors from plants confer resistance to fungal pathogens and many other pathogenic organisms. Their low expression makes it challenging to purify these receptors from plants in sufficient quantities to be able to identify interacting proteins by mass spectrometry. Here we describe a protocol to affinity-purify recombinant NB-LRR immune receptors, fused to the streptavidin-binding peptide tag.
authors.affiliation: Laboratory of Phytopathology, Wageningen University, Wageningen, The Netherlands. wladimir.tameling@wur.nl
authors.forename: Wladimir I L
authors.initials: WI
authors.lastname: Tameling
mesh_terms: D002352:Carrier Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*; D010940:Plant Proteins / Q000276:immunology / Q000302:isolation & purification*; D010944:Plants / Q000276:immunology*; D011971:Receptors, Immunologic / Q000276:immunology / Q000302:isolation & purification*; D011993:Recombinant Fusion Proteins / Q000276:immunology / Q000302:isolation & purification*
chemical_list: D002352:Carrier Proteins; D010940:Plant Proteins; D011971:Receptors, Immunologic; D011993:Recombinant Fusion Proteins; C452700:streptavidin-binding peptide