CLCuMuB βC1 Subverts Ubiquitination by Interacting with NbSKP1s to Enhance Geminivirus Infection in Nicotiana benthamiana

PLoS Pathogens

Shaojie Han¹  Yiguo Hong²  Daoxin Xie³  Yule Liu⁴  Jinping Zhao⁴  Rena Gorovits⁴  Xijuan Zhao⁴  Yanwan Dai⁴  Na Liu⁴  Lichao Qian⁴  Ke Xie⁴  Qi Jia⁴  Yunjing Wang⁴ 

[1] College of Biological Sciences, China Agricultural University, Beijing, China;Institute of Plant Sciences and Genetics in Agriculture, Robert H. Smith Faculty of Agriculture, Food and Environment, Hebrew University of Jerusalem, Rehovot, Israel;Institute of Virology and Biotechnology, Zhejiang Academy of Agricultural Sciences, Hangzhou, China;MOE Key Laboratory of Bioinformatics, Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing, China

关键词: Leaves;    Polymerase chain reaction;    Genetically modified plants;    RNA extraction;    Membrane staining;    Ubiquitination;    DNA extraction;    Protein extraction;   

DOI  :  10.1371/journal.ppat.1005668

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Viruses interfere with and usurp host machinery and circumvent defense responses to create a suitable cellular environment for successful infection. This is usually achieved through interactions between viral proteins and host factors. Geminiviruses are a group of plant-infecting DNA viruses, of which some contain a betasatellite, known as DNAβ. Here, we report that Cotton leaf curl Multan virus (CLCuMuV) uses its sole satellite-encoded protein βC1 to regulate the plant ubiquitination pathway for effective infection. We found that CLCuMu betasatellite (CLCuMuB) βC1 interacts with NbSKP1, and interrupts the interaction of NbSKP1s with NbCUL1. Silencing of either NbSKP1s or NbCUL1 enhances the accumulation of CLCuMuV genomic DNA and results in severe disease symptoms in plants. βC1 impairs the integrity of SCFCOI1 and the stabilization of GAI, a substrate of the SCFSYL1 to hinder responses to jasmonates (JA) and gibberellins (GA). Moreover, JA treatment reduces viral accumulation and symptoms. These results suggest that CLCuMuB βC1 inhibits the ubiquitination function of SCF E3 ligases through interacting with NbSKP1s to enhance CLCuMuV infection and symptom induction in plants.

【 授权许可】

CC BY