Plant receptor-like protein activation by a microbial glycoside hydrolase

Yue Sun, Yan Wang (), Xiaoxiao Zhang, Zhaodan Chen, Yeqiang Xia, Lei Wang, Yujing Sun, Mingmei Zhang, Yu Xiao, Zhifu Han (), Yuanchao Wang () and Jijie Chai ()
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Yue Sun: Tsinghua University
Yan Wang: Nanjing Agricultural University
Xiaoxiao Zhang: Tsinghua University
Zhaodan Chen: Nanjing Agricultural University
Yeqiang Xia: Nanjing Agricultural University
Lei Wang: Nanjing Agricultural University
Yujing Sun: Nanjing Agricultural University
Mingmei Zhang: Nanjing Agricultural University
Yu Xiao: Tsinghua University
Zhifu Han: Tsinghua University
Yuanchao Wang: Nanjing Agricultural University
Jijie Chai: Tsinghua University

Nature, 2022, vol. 610, issue 7931, 335-342

Abstract: Abstract Plants rely on cell-surface-localized pattern recognition receptors to detect pathogen- or host-derived danger signals and trigger an immune response1–6. Receptor-like proteins (RLPs) with a leucine-rich repeat (LRR) ectodomain constitute a subgroup of pattern recognition receptors and play a critical role in plant immunity1–3. Mechanisms underlying ligand recognition and activation of LRR-RLPs remain elusive. Here we report a crystal structure of the LRR-RLP RXEG1 from Nicotiana benthamiana that recognizes XEG1 xyloglucanase from the pathogen Phytophthora sojae. The structure reveals that specific XEG1 recognition is predominantly mediated by an amino-terminal and a carboxy-terminal loop-out region (RXEG1(ID)) of RXEG1. The two loops bind to the active-site groove of XEG1, inhibiting its enzymatic activity and suppressing Phytophthora infection of N. benthamiana. Binding of XEG1 promotes association of RXEG1(LRR) with the LRR-type co-receptor BAK1 through RXEG1(ID) and the last four conserved LRRs to trigger RXEG1-mediated immune responses. Comparison of the structures of apo-RXEG1(LRR), XEG1–RXEG1(LRR) and XEG1–BAK1–RXEG1(LRR) shows that binding of XEG1 induces conformational changes in the N-terminal region of RXEG1(ID) and enhances structural flexibility of the BAK1-associating regions of RXEG1(LRR). These changes allow fold switching of RXEG1(ID) for recruitment of BAK1(LRR). Our data reveal a conserved mechanism of ligand-induced heterodimerization of an LRR-RLP with BAK1 and suggest a dual function for the LRR-RLP in plant immunity.

Date: 2022
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DOI: 10.1038/s41586-022-05214-x

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