Binding of the <i>Magnaporthe oryzae</i> Chitinase MoChia1 by a Rice Tetratricopeptide Repeat Protein Allows Free Chitin to Trigger Immune Responses

Yang, Chao; Yu, Yongqi; Huang, Jiyong; Meng, Fanwei; Pang, Junfeng; Zhao, Qiqi; Islam, Md. Aminul; Xu, Ning; Tian, Yun; Liu, Jun

doi:10.1105/tpc.18.00382

Cited by 94 publications

(88 citation statements)

References 47 publications

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“…While this article was being revised, another study was published identifying and characterizing MoChi1/ MoChia1 (Yang et al, 2019). This work confirms our finding that MoChi1 is a catalytically active chitinase and that the cell wall is altered in the MoChi1 mutant.…”

Section: Discussionsupporting

confidence: 82%

“…The defect in aggressiveness of MoChi1 mutants was also confirmed. The study by Yang et al (2019) identified a rice tricopeptide-repeat protein, OsTPR1, as an interacting protein with MoChi1 protein and demonstrated that OsTRP1 was membrane localized and interacted with apoplastic MoChi1. In our model shown in Figure 10, we propose that a protein may interact with OsMBL1 to contribute to defense.…”

Section: Discussionmentioning

confidence: 99%

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A Magnaporthe Chitinase Interacts with a Rice Jacalin-Related Lectin to Promote Host Colonization

et al. 2019

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ORCID IDs: 0000-0003-4795-7929 (D.E.); 0000-0001-6325-9165 (G.L.).The genome of rice blast fungus (Magnaporthe oryzae) encodes 15 glycoside hydrolase 18 family chitinases. In this study, we characterized the function of an M. oryzae extracellular chitinase, MoChi1, and its interaction with a host protein, OsMBL1, a jacalin-related Mannose-Binding Lectin (MBL) in rice (Oryza sativa). Deletion of MoChi1 resulted in reduced aerial hyphal formation and reduced virulence in rice by activating the expression of defense-responsive genes. We confirmed MoChi1 interaction with rice OsMBL1 in vitro and in vivo. OsMBL1 was induced by pathogen-associated molecular patterns and M. oryzae infection. Overexpression of OsMBL1 led to activation of rice defense-responsive genes and a chitin-induced reactive oxygen species burst, thereby enhancing resistance to M. oryzae. Knockdown of OsMBL1 enhances susceptibility of rice plants to M. oryzae. Furthermore, MoChi1 suppressed chitin-induced reactive oxygen species in rice cells and competed with OsMBL1 for chitin binding. Taken together, our study reveals a mechanism in which MoChi1 targets a host lectin to suppress rice immunity. cells of wild-type strain Ku80. Hygromycin B-resistant colonies were picked up and replacement verified by PCR amplifications.The complementation of MoChi1 was performed by constructing a 1-kb upstream fragment of the native promoter and MoChi1 ORF region into the pKNTG vector and then transformed into protoplast cells of the MoChi1 deletion strain. The neomycin-resistant transformants were screened and verified by PCR amplifications.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%

A Magnaporthe Chitinase Interacts with a Rice Jacalin-Related Lectin to Promote Host Colonization

et al. 2019

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“…To counter chitin‐triggered immunity, V. dahliae also secretes polysaccharide deacetylase 1 (PDA1) to directly deacetylate chitin oligomers (Gao et al 2019). In addition, it has been reported that the fungal pathogen of rice, Magnaporthe oryzae , uses chitinase MoChia1 to bind and protect chitin from the perception of rice PRRs, whereas rice tetratricopeptide repeat protein OsTPR1 competitively binds MoChia1, leading to the accumulation of chitin in the apoplast (Yang et al 2019).…”

Section: Recent Discoveries Of the Activation Of Immunity Mediated Bymentioning

confidence: 99%

Plant immune signaling: Advancing on two frontiers

Wang

Feng

Zhou

et al. 2020

JIPB

165

144

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Plants have evolved multiple defense strategies to cope with pathogens, among which plant immune signaling that relies on cell-surface localized and intracellular receptors takes fundamental roles. Exciting breakthroughs were made recently on the signaling mechanisms of pattern recognition receptors (PRRs) and intracellular nucleotide-binding site (NBS) and leucine-rich repeat (LRR) domain receptors (NLRs). This review summarizes the current view of PRRs activation, emphasizing the most recent discoveries about PRRs' dynamic regulation and signaling mechanisms directly leading to downstream molecular events including mitogen-activated protein kinase (MAPK) activation and calcium (Ca 2+ ) burst. Plants also have evolved intracellular NLRs to perceive the presence of specific pathogen effectors and trigger more robust immune responses. We also discuss the current understanding of the mechanisms of NLR activation, which has been greatly advanced by recent breakthroughs including structures of the first full-length plant NLR complex, findings of NLR sensor-helper pairs and novel biochemical activity of Toll/interleukin-1 receptor (TIR) domain.

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“…M. oryzae has 15 genes that are annotated as GH_18 family chitinases. MoChia1 is involved in the fungal virulence through degrading chitin into small fragments, which would escape the recognition of plant immune receptors [33, 60]. Different chitinases had their specific expression in different cell types, AMCase maintains the highest expression level in appressorium among 15 chitinases, indicating AMCase is likely to be associated with fungal infection [33].…”

Section: Discussionmentioning

confidence: 99%

Comparative secretome of Magnaporthe oryzae identified proteins involved in virulence and cell wall integrity

Liu

Huang

et al. 2020

Preprint

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Plant fungal pathogens secrete numerous proteins into the apoplast at the plant–fungus contact sites to facilitate colonization. Only a few secreted proteins were functionally characterized in Magnaporthe oryzae, the fungal pathogen causing rice blast disease worldwide. ALG3 is an α-1, 3-mannosyltransferase function in N-glycan synthesis for secreted N-glycosylated proteins, and the Δalg3 mutants show strong defects in cell wall integrity and fungal virulence, indicating a potential effect on the secretion of multiple proteins. In this study, we compared the secretome of wild type and Δalg3 mutants, and identified 51 proteins that require ALG3 for proper secretion. These are predicted to be involved in metabolic processes, interspecies interactions, cell wall organization, and response to chemicals. The tested secreted proteins localized at the apoplast region surrounding the fungal infection hyphae. Moreover, the N-glycosylation of candidate proteins was significantly changed in the Δalg3 mutant, leading to the reduction of protein secretion and abnormal protein localization. Furthermore, we tested the function of two genes, one is a previously reported M. oryzae gene Invertase 1 (INV1) encoding a secreted invertase, and the other one is a gene encoding an Acid mammalian chinitase (AMCase). The fungal virulence was significantly reduced and the cell wall integrity was altered in the Δinv1 and Δamcase mutant strains. Elucidation of the comparative secretome of M. oryzae improves our understanding of the proteins that require ALG3 for secretion, and of their function in fungal virulence and cell wall integrity.

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Binding of the Magnaporthe oryzae Chitinase MoChia1 by a Rice Tetratricopeptide Repeat Protein Allows Free Chitin to Trigger Immune Responses

Cited by 94 publications

References 47 publications

A Magnaporthe Chitinase Interacts with a Rice Jacalin-Related Lectin to Promote Host Colonization

A Magnaporthe Chitinase Interacts with a Rice Jacalin-Related Lectin to Promote Host Colonization

Plant immune signaling: Advancing on two frontiers

Comparative secretome of Magnaporthe oryzae identified proteins involved in virulence and cell wall integrity

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