Evidence map›Paper›PMID 23242918›Full record

ArticlePlant molecular biology2013

Expression of the chimeric receptor between the chitin elicitor receptor CEBiP and the receptor-like protein kinase Pi-d2 leads to enhanced responses to the chitin elicitor and disease resistance against Magnaporthe oryzae in rice.

Yusuke Kouzai, Hanae Kaku, Naoto Shibuya, Eiichi Minami, Yoko Nishizawa

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Article in Plant molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

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19citing papers in PubMed
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1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
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  4. All Roads Lead to Rome: Pathways to Engineering Disease Resistance in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Yusuke KouzaiGenetically Modified Organism Research Center, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8602, Japan.
Hanae Kaku
Naoto Shibuya
Eiichi Minami
Yoko Nishizawa

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously reported that rice plants expressing the chimeric receptor consisting of rice chitin oligosaccharides binding protein (CEBiP) and the intracellular protein kinase region of Xa21, which confers resistance to rice bacterial blight, showed enhanced cellular responses to a chitin elicitor N-acetylchitoheptaose and increased resistance to the rice blast fungus Magnaporthe oryzae. Here, we investigated whether CEBiP fused with another type of receptor-like protein kinase (RLK) also functions as a chimeric receptor. Fusion proteins CRPis consist of CEBiP and the intracellular protein kinase region of a true resistance gene Pi-d2. Transgenic rice expressing a CRPi showed enhanced cellular responses specifically to N-acetylchitoheptaose in cultured cells and increased levels of disease resistance against M. oryzae in plants. These responses depended on the amino acid sequences predicted to be essential for the protein kinase activity of CRPi. The structure of the transmembrane domain in CRPi affected the protein accumulation, cellular responses, and disease resistance in transgenic rice. These results suggest that the chimeric receptor consisting of CEBiP and Pi-d2 functions as a receptor for chitin oligosaccharides and CEBiP-based chimeric receptors fused with other RLKs may also act as functional receptors.

Indexed as

Amino Acid SequenceCells, CulturedChitinDisease ResistanceGene ExpressionGene Expression Regulation, PlantHost-Pathogen InteractionsHydrogen PeroxideMagnaportheMolecular Sequence DataMutationOligosaccharidesOryzaPlant DiseasesPlant LeavesPlant ProteinsChitinHydrogen PeroxideN-acetylchitoheptaoseOligosaccharidesPlant ProteinsRecombinant Fusion Proteins

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.