Evidence map›Paper›PMID 26531228›Full record

ArticleGlycobiology2016

Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum.

Wael Elhenawy, Nichollas E Scott, M Laura Tondo, Elena G Orellano, Leonard J Foster, Mario F Feldman

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 36 citations in OpenAlex.

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  11. Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021
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  13. Virulence of the emerging pathogen,Future microbiology · 2020
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  14. Loss ofmSphere · 2019
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  15. Article
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  17. A General ProteinFrontiers in microbiology · 2018
    Article
  18. 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

6 authors at 3 institutions in 3 countries.

Wael ElhenawyDepartment of Biological Sciences, University of Alberta, Edmonton, AB, Canada.
Nichollas E ScottCentre for High-Throughput Biology, University of British Columbia, Vancouver, BC, Canada.
M Laura TondoFacultad de Ciencias Bioquímicas y Farmacéuticas (FBIOYF-UNR), Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Rosario, Santa Fe, Argentina.
Elena G OrellanoFacultad de Ciencias Bioquímicas y Farmacéuticas (FBIOYF-UNR), Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Rosario, Santa Fe, Argentina.
Leonard J FosterCentre for High-Throughput Biology, University of British Columbia, Vancouver, BC, Canada.
Mario F FeldmanDepartment of Biological Sciences, University of Alberta, Edmonton, AB, Canada Department of Molecular Microbiology, Washington University School of Medicine St. Louis, St. Louis, MO, USA mariofeldman@wustl.edu.
Instituto de Biología Molecular y Celular de Rosario · ARUniversity of Alberta · CAUniversity of British Columbia · CA

Funding

Canadian Institutes of Health Research MOP-77688
6 · The paper itself

Abstract

Ralstonia solanacearum is one of the most lethal phytopathogens in the world. Due to its broad host range, it can cause wilting disease in many plant species of economic interest. In this work, we identified the O-oligosaccharyltransferase (O-OTase) responsible for protein O-glycosylation in R. solanacearum. An analysis of the glycoproteome revealed that 20 proteins, including type IV pilins are substrates of this general glycosylation system. Although multiple glycan forms were identified, the majority of the glycopeptides were modified with a pentasaccharide composed of HexNAc-(Pen)-dHex(3), similar to the O antigen subunit present in the lipopolysaccharide of multiple R. solanacearum strains. Disruption of the O-OTase led to the total loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. Comparative proteomic analysis revealed that the loss of glycosylation is not associated with widespread proteome changes. Only the levels of a single glycoprotein, the type IV pilin, were diminished in the absence of glycosylation. In parallel, disruption of glycosylation triggered an increase in the levels of a surface lectin homologous to Pseudomonas PA-IIL. These results reveal the important role of glycosylation in the pathogenesis of R. solanacearum.

Indexed as

ProteomicsFimbriae ProteinsGlycoproteinsGlycosylationHexosyltransferasesMembrane ProteinsO AntigensRalstonia solanacearumSolanum lycopersicumdolichyl-diphosphooligosaccharide - protein glycotransferaseFimbriae ProteinsGlycoproteinsHexosyltransferasesMembrane ProteinsO Antigensbiofilmprotein O-glycosylationType IV pili

Identifiers

PMID26531228
PMCPMC4736539
OpenAlexW2267446635

What OpenQuestion holds

Textmetadata
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.