Evidence map›Paper›PMID 32574207›Full record

ArticlePLoS pathogens2020

A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization.

Andrea Sánchez-Vallet, Hui Tian, Luis Rodriguez-Moreno, Dirk-Jan Valkenburg, Raspudin Saleem-Batcha, Stephan Wawra, Anja Kombrink, Leonie Verhage, Ronnie de Jonge, H Peter van Esse and 4 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
11.6field-weighted citation impact, top 2% 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

38 citing papers in PubMed, 86 citations in OpenAlex.

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  13. Histone MethyltransferaseJournal of fungi (Basel, Switzerland) · 2024
    Article
  14. Article
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  18. Journal of fungi (Basel, Switzerland) · 2023
    Article
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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

14 authors at 5 institutions in 3 countries.

Andrea Sánchez-ValletLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.ORCID 0000-0002-3668-9503
Hui TianLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.
Luis Rodriguez-MorenoLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.ORCID 0000-0003-2385-8782
Dirk-Jan ValkenburgLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.
Raspudin Saleem-BatchaInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany.ORCID 0000-0003-3361-823X
Stephan WawraUniversity of Cologne, Institute for Plant Sciences, Cluster of Excellence on Plant Sciences (CEPLAS), Cologne, Germany.
Anja KombrinkLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.
Leonie VerhageLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.ORCID 0000-0001-6402-3605
Ronnie de JongeLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.ORCID 0000-0001-5065-8538
H Peter van EsseLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.ORCID 0000-0002-3667-060X
Alga ZuccaroUniversity of Cologne, Institute for Plant Sciences, Cluster of Excellence on Plant Sciences (CEPLAS), Cologne, Germany.ORCID 0000-0002-8026-0114
Daniel CrollInstitute of Biology, University of Neuchâtel, Neuchâtel, Switzerland.ORCID 0000-0002-2072-380X
Jeroen R MestersInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany.ORCID 0000-0001-8532-6699
Bart P H J ThommaLaboratory of Phytopathology, Wageningen University& Research, Wageningen, The Netherlands.ORCID 0000-0003-4125-4181
Wageningen University & Research · NLUniversity of Cologne · DEUniversity of Lübeck · DEETH Zurich · CHUniversity of Neuchâtel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants trigger immune responses upon recognition of fungal cell wall chitin, followed by the release of various antimicrobials, including chitinase enzymes that hydrolyze chitin. In turn, many fungal pathogens secrete LysM effectors that prevent chitin recognition by the host through scavenging of chitin oligomers. We previously showed that intrachain LysM dimerization of the Cladosporium fulvum effector Ecp6 confers an ultrahigh-affinity binding groove that competitively sequesters chitin oligomers from host immune receptors. Additionally, particular LysM effectors are found to protect fungal hyphae against chitinase hydrolysis during host colonization. However, the molecular basis for the protection of fungal cell walls against hydrolysis remained unclear. Here, we determined a crystal structure of the single LysM domain-containing effector Mg1LysM of the wheat pathogen Zymoseptoria tritici and reveal that Mg1LysM is involved in the formation of two kinds of dimers; a chitin-dependent dimer as well as a chitin-independent homodimer. In this manner, Mg1LysM gains the capacity to form a supramolecular structure by chitin-induced oligomerization of chitin-independent Mg1LysM homodimers, a property that confers protection to fungal cell walls against host chitinases.

Indexed as

Protein MultimerizationAscomycotaChitinCladosporiumFungal ProteinsHyphaePlant DiseasesProtein Structure, QuaternaryTriticumChitinFungal Proteins

Identifiers

PMID32574207
PMCPMC7337405
OpenAlexW3035973877

What OpenQuestion holds

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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.