Evidence map›Paper›PMID 33846308›Full record

ArticleNature communications2021

The Botrytis cinerea Crh1 transglycosylase is a cytoplasmic effector triggering plant cell death and defense response.

Kai Bi, Loredana Scalschi, Namrata Jaiswal, Tesfaye Mengiste, Renana Fried, Ana Belén Sanz, Javier Arroyo, Wenjun Zhu, Gal Masrati, Amir Sharon

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
17.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 101 citations in OpenAlex.

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  17. WRKY45 is a negative regulator ofFrontiers in plant science · 2025
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4 · The record

Corrections and comments

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

10 authors at 5 institutions in 4 countries.

Kai BiSchool of Plant Sciences and Food Security, Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Loredana ScalschiSchool of Plant Sciences and Food Security, Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Namrata JaiswalDepartment of Botany and Plant Pathology, College of Agriculture, Purdue University, West Lafayette, IN, USA.
Tesfaye MengisteDepartment of Botany and Plant Pathology, College of Agriculture, Purdue University, West Lafayette, IN, USA.
Renana FriedSchool of Plant Sciences and Food Security, Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Ana Belén SanzDpto. Microbiología y Parasitología, Facultad de Farmacia, Universidad Complutense, IRYCIS, Madrid, Spain.
Javier ArroyoDpto. Microbiología y Parasitología, Facultad de Farmacia, Universidad Complutense, IRYCIS, Madrid, Spain.ORCID http://orcid.org/0000-0002-1971-1721
Wenjun ZhuCollege of Life Science and Technology, Wuhan Polytechnic University, Wuhan City, Hubei Province, China.
Gal MasratiSchool of Neurobiology, Biochemistry and Biophysics, Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.ORCID http://orcid.org/0000-0003-1322-5762
Amir SharonSchool of Plant Sciences and Food Security, Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel. amirsh@tauex.tau.ac.il.ORCID http://orcid.org/0000-0002-6045-9169
Tel Aviv University · ILPurdue University West Lafayette · USUniversidad Complutense de Madrid · ESWuhan Polytechnic University · CNUniversitat Jaume I · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Crh proteins catalyze crosslinking of chitin and glucan polymers in fungal cell walls. Here, we show that the BcCrh1 protein from the phytopathogenic fungus Botrytis cinerea acts as a cytoplasmic effector and elicitor of plant defense. BcCrh1 is localized in vacuoles and the endoplasmic reticulum during saprophytic growth. However, upon plant infection, the protein accumulates in infection cushions; it is then secreted to the apoplast and translocated into plant cells, where it induces cell death and defense responses. Two regions of 53 and 35 amino acids are sufficient for protein uptake and cell death induction, respectively. BcCrh1 mutant variants that are unable to dimerize lack transglycosylation activity, but are still able to induce plant cell death. Furthermore, Arabidopsis lines expressing the bccrh1 gene exhibit reduced sensitivity to B. cinerea, suggesting a potential use of the BcCrh1 protein in plant immunization against this necrotrophic pathogen.

Indexed as

AgrobacteriumArabidopsisBotrytisCell DeathCytoplasmDisease ResistanceFungal ProteinsGlycosyltransferasesNicotianaPlant CellsPlant DiseasesPlant ImmunityProtein MultimerizationReactive Oxygen SpeciesFungal ProteinsGlycosyltransferasesReactive Oxygen Species

Identifiers

PMID33846308
PMCPMC8042016
OpenAlexW3155158695

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.