Evidence map›Paper›PMID 40315235›Full record

ArticlePLoS pathogens2025

A GDP-mannose-1-phosphate guanylyltransferase as a potential HIGS target against Sclerotinia sclerotiorum.

Cheng Zhang, Yan Xu, Lin Li, Mingsong Wu, Zheyi Fang, Jinyi Tan, Jeffrey A Rollins, Honghui Lin, Xinyi Huang, Shawn D Mansfield and 2 more

Abstract read
In one paragraph

Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

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

7 citing papers in PubMed.

  1. Review
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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.

Cheng ZhangKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.
Yan XuKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.
Lin LiKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.
Mingsong WuKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.
Zheyi FangKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.
Jinyi TanMichael Smith Laboratories, University of British Columbia, Vancouver, Canada.
Jeffrey A RollinsDepertment of Plant Pathology, University of Florida, Gainesville, Florida, United States of America.
Honghui LinKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.
Xinyi HuangDepartment of Botany, University of British Columbia, Vancouver, Canada.
Shawn D MansfieldDepartment of Botany, University of British Columbia, Vancouver, Canada.
Xin LiMichael Smith Laboratories, University of British Columbia, Vancouver, Canada.ORCID 0000-0002-6354-2021
Yuelin ZhangKey Laboratory of Bio-resource and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu, China.

Funding

Fundamental Research Funds for the Central UniversitiesNatural Sciences and Engineering Research Council of Canada (NSERC)
6 · The paper itself

Abstract

Sclerotinia stem rot is a devastating disease affecting vegetables and oil crops worldwide. It is caused by the necrotrophic ascomycete Sclerotinia (S.) sclerotiorum. Host-induced gene silencing (HIGS) has shown promise in disease control against insects and fungal pathogens, but effective HIGS target genes against S. sclerotiorum remain limited. In this study, we identified a GDP-mannose pyrophosphorylase (GMPP) SsMPG2 through forward genetic analysis. Ssmpg2 mutants exhibit abnormal sclerotia and compound appressoria, along with defective cell wall integrity and attenuated virulence. Meanwhile, knocking out SsMPG2 reduced the GMPP activity and glycosylation of proteins. In addition, SsMPG2 interacts with SsMPG1, which is essential in S. sclerotiorum. Downstream of the SsMPG1-SsMPG2 complex, SsPMT4, which encodes an O-mannosyltransferase, is also critical for compound appressoria formation and virulence. Notably, MPG2 is essential for the virulence of several other fungal pathogens such as Botrytis cinerea, Magnaporthe oryzae, and Fusarium graminearum. Furthermore, expressing hairpin RNAs against SsMPG1 and SsMPG2 in Nicotiana benthamiana and Arabidopsis thaliana significantly reduced disease symptoms caused by S. sclerotiorum. Collectively, our findings demonstrate the critical roles of GMPP in the virulence of phytopathogenic fungi and suggest that MPGs are promising HlGS targets for controlling S. sclerotiorum.

Indexed as

AscomycotaFungal ProteinsNucleotidyltransferasesPlant DiseasesArabidopsisGene SilencingNicotianaVirulenceFungal Proteinsmannose 1-phosphate guanylyltransferaseNucleotidyltransferases

Identifiers

PMID40315235
PMCPMC12068732

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Registered trials

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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.