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Merck
  • The receptor-like kinase NIK1 targets FLS2/BAK1 immune complex and inversely modulates antiviral and antibacterial immunity.

The receptor-like kinase NIK1 targets FLS2/BAK1 immune complex and inversely modulates antiviral and antibacterial immunity.

Nature communications (2019-11-05)
Bo Li, Marco Aurélio Ferreira, Mengling Huang, Luiz Fernando Camargos, Xiao Yu, Ruan M Teixeira, Paola A Carpinetti, Giselle C Mendes, Bianca C Gouveia-Mageste, Chenglong Liu, Claudia S L Pontes, Otávio J B Brustolini, Laura G C Martins, Bruno P Melo, Christiane E M Duarte, Libo Shan, Ping He, Elizabeth P B Fontes
摘要

Plants deploy various immune receptors to recognize pathogens and defend themselves. Crosstalk may happen among receptor-mediated signal transduction pathways in the same host during simultaneous infection of different pathogens. However, the related function of the receptor-like kinases (RLKs) in thwarting different pathogens remains elusive. Here, we report that NIK1, which positively regulates plant antiviral immunity, acts as an important negative regulator of antibacterial immunity. nik1 plants exhibit dwarfed morphology, enhanced disease resistance to bacteria and increased PAMP-triggered immunity (PTI) responses, which are restored by NIK1 reintroduction. Additionally, NIK1 negatively regulates the formation of the FLS2/BAK1 complex. The interaction between NIK1 and FLS2/BAK1 is enhanced upon flg22 perception, revealing a novel PTI regulatory mechanism by an RLK. Furthermore, flg22 perception induces NIK1 and RPL10A phosphorylation in vivo, activating antiviral signalling. The NIK1-mediated inverse modulation of antiviral and antibacterial immunity may allow bacteria and viruses to activate host immune responses against each other.

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Sigma-Aldrich
单克隆抗-FLAG® M2-过氧化物酶(HRP) 小鼠抗, clone M2, purified immunoglobulin, buffered aqueous glycerol solution
Sigma-Aldrich
抗 AtMPK3 兔抗, affinity isolated antibody, buffered aqueous solution