Evidence map›Paper›PMID 39738104›Full record

ArticleScientific reports2024

A new type III effector from Bradyrhizobium sp. DOA9 encoding a putative SUMO-protease blocks nodulation in Arachis hypogaea L.

Beedou Aphaiso, Pongdet Piromyou, Pakpoom Boonchuen, Pongpan Songwattana, Jenjira Wongdee, Teerana Greetatorn, Kamonluck Teamtisong, Alicia Camuel, Panlada Tittabutr, Nantakorn Boonkerd and 2 more

Abstract read
In one paragraph

Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

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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

2 citing papers in PubMed.

  1. 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

12 authors.

Beedou AphaisoSchool of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Pongdet PiromyouInstitute of Research and Development, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Pakpoom BoonchuenSchool of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Pongpan SongwattanaInstitute of Research and Development, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Jenjira WongdeeInstitute of Research and Development, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Teerana GreetatornInstitute of Research and Development, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Kamonluck TeamtisongThe Center for Scientific and Technological Equipment, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Alicia CamuelIRD/CIRAD/INRAE, PHIM, Plant Health Institute of Montpellier, UMR-PHIM, Université de Montpellier/Institut Agro, Montpellier, 34398, France.
Panlada TittabutrSchool of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Nantakorn BoonkerdSchool of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
Eric GiraudIRD/CIRAD/INRAE, PHIM, Plant Health Institute of Montpellier, UMR-PHIM, Université de Montpellier/Institut Agro, Montpellier, 34398, France. eric.giraud@ird.fr.
Neung TeaumroongSchool of Biotechnology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand. neung@sut.ac.th.

Funding

French National Research Agency ANR-20-CE20-0012JSPS-NRCT by National Research Council of Thailand N11A670769The NSRF via the Program Management Unit for Human Resources & Institutional Development, Research and Innovation B16F640113
6 · The paper itself

Abstract

Effector proteins secreted via the type III secretion system (T3SS) of nitrogen-fixing rhizobia are key determinants of symbiotic compatibility in legumes. Previous report revealed that the T3SS of Bradyrhizobium sp. DOA9 plays negative effects on Arachis hypogaea symbiosis. In this study, we characterized the symbiotic role of 4 effector proteins (p0490, p0871, SkP48, and p0903) containing the small ubiquitin-like modifier (SUMO) protease domain identified in DOA9 during symbiosis. While the DOA9 strain and the two mutants of SUMO-proteases, p0490 and p0871, induced inefficient nodulation in A. hypogaea, the mutation of SUMO-proteases SkP48 or p0903 promoted efficient symbiosis comparable to the type strain Bradyrhizobium arachidis CCBAU051107. Complementation study of ∆p0903 with various mutated forms of p0903 highlighted importance of ubiquitin-like protein (ULP) domain in restriction of nodulation in A. hypogaea. We observed the accumulation of jasmonic acid (JA) and upregulation of several defence genes involved in the JA/ethylene (ET) signalling pathway at the early stage of infection in roots inoculated with DOA9 strain compared with those inoculated with the DOA9-∆p0903 strain. Our data highlight the importance of SUMO-protease effectors during the symbiotic interaction between bradyrhizobia and A. hypogaea, which could be useful for the development of high-performance inocula to improve its growth.

Indexed as

ArachisBacterial ProteinsBradyrhizobiumPlant Root NodulationSymbiosisCyclopentanesMutationOxylipinsType III Secretion SystemsBacterial ProteinsCyclopentanesjasmonic acidOxylipinsType III Secretion Systemsand SUMO-proteaseArachis hypogaeaBradyrhizobium spT3SS

Identifiers

PMID39738104
PMCPMC11685577

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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.