Evidence map›Paper›PMID 33803725›Full record

ReviewInternational journal of molecular sciences2021

Lysin Motif (LysM) Proteins: Interlinking Manipulation of Plant Immunity and Fungi.

Shu-Ping Hu, Jun-Jiao Li, Nikhilesh Dhar, Jun-Peng Li, Jie-Yin Chen, Wei Jian, Xiao-Feng Dai, Xing-Yong Yang

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
9.5field-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

24 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
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  16. Article
  17. Frontiers in microbiology · 2023
    Article
  18. Review
  19. Plant lectins: Handymen at the cell surface.Cell surface (Amsterdam, Netherlands) · 2022
    Review
  20. Article
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

8 authors at 3 institutions in 2 countries.

Shu-Ping HuSchool of Life Sciences, Chongqing Normal University, Chongqing 401331, China.
Jun-Jiao Lic/o State Key Laboratory for Biology of Plant Diseases and Insect Pests, Department of Plant Pathology, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
Nikhilesh DharDepartment of Plant Pathology, University of California Davis, Salinas, CA 93905, USA.ORCID 0000-0002-2268-9633
Jun-Peng LiSchool of Life Sciences, Chongqing Normal University, Chongqing 401331, China.
Jie-Yin Chenc/o State Key Laboratory for Biology of Plant Diseases and Insect Pests, Department of Plant Pathology, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.ORCID 0000-0002-8040-099X
Wei JianSchool of Life Sciences, Chongqing Normal University, Chongqing 401331, China.
Xiao-Feng Daic/o State Key Laboratory for Biology of Plant Diseases and Insect Pests, Department of Plant Pathology, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing 100193, China.ORCID 0000-0002-5012-5114
Xing-Yong YangSchool of Life Sciences, Chongqing Normal University, Chongqing 401331, China.
Chongqing Normal University · CNInstitute of Plant Protection · CNUniversity of California, Davis · US

Funding

National Key Research and Development Program of China 2018YFE0112500
6 · The paper itself

Abstract

The proteins with lysin motif (LysM) are carbohydrate-binding protein modules that play a critical role in the host-pathogen interactions. The plant LysM proteins mostly function as pattern recognition receptors (PRRs) that sense chitin to induce the plant's immunity. In contrast, fungal LysM blocks chitin sensing or signaling to inhibit chitin-induced host immunity. In this review, we provide historical perspectives on plant and fungal LysMs to demonstrate how these proteins are involved in the regulation of plant's immune response by microbes. Plants employ LysM proteins to recognize fungal chitins that are then degraded by plant chitinases to induce immunity. In contrast, fungal pathogens recruit LysM proteins to protect their cell wall from hydrolysis by plant chitinase to prevent activation of chitin-induced immunity. Uncovering this coevolutionary arms race in which LysM plays a pivotal role in manipulating facilitates a greater understanding of the mechanisms governing plant-fungus interactions.

Indexed as

Plant ImmunityAmino Acid MotifsFungiHost-Pathogen InteractionsPlantsProteinsProteinschitinimmunity manipulationlysin motif (LysM) proteinplant-fungus interactions

Identifiers

PMID33803725
PMCPMC8003243
OpenAlexW3138784736

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.