The geminivirus nuclear shuttle protein is a virulence factor that suppresses transmembrane receptor kinase activity

• Published in: Genes & development 2004-10, Vol.18 (20), p.2545-2556
• Main Authors: Fontes, Elizabeth P B, Santos, Anesia A, Luz, Dirce F, Waclawovsky, Alessandro J, Chory, Joanne
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Arabidopsis - virology; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Binding Sites; Geminiviridae - metabolism; Geminiviridae - pathogenicity; Geminivirus; Membrane Proteins - metabolism; Microscopy, Fluorescence; Molecular Sequence Data; Phosphorylation; Protein Binding; Protein Kinases - metabolism; Recombinant Fusion Proteins; Research Papers; Reverse Transcriptase Polymerase Chain Reaction; Sequence Alignment; Sequence Analysis, DNA; Signal Transduction; Two-Hybrid System Techniques; Viral Proteins - genetics; Viral Proteins - metabolism; Virulence - genetics
• ISSN: 0890-9369; 1549-5477
• DOI: 10.1101/gad.1245904

Despite the large number of leucine-rich-repeat (LRR) receptor-like-kinases (RLKs) in plants and their conceptual relevance in signaling events, functional information is restricted to a few family members. Here we describe the characterization of new LRR-RLK family members as virulence targets of the geminivirus nuclear shuttle protein (NSP). NSP interacts specifically with three LRR-RLKs, NIK1, NIK2, and NIK3, through an 80-amino acid region that encompasses the kinase active site and A-loop. We demonstrate that these NSP-interacting kinases (NIKs) are membrane-localized proteins with biochemical properties of signaling receptors. They behave as authentic kinase proteins that undergo autophosphorylation and can also phosphorylate exogenous substrates. Autophosphorylation occurs via an intermolecular event and oligomerization precedes the activation of the kinase. Binding of NSP to NIK inhibits its kinase activity in vitro, suggesting that NIK is involved in antiviral defense response. In support of this, infectivity assays showed a positive correlation between infection rate and loss of NIK1 and NIK3 function. Our data are consistent with a model in which NSP acts as a virulence factor to suppress NIK-mediated antiviral responses.