Evidence map›Paper›PMID 22416226›Full record

ArticlePLoS pathogens2012

Identification of O-mannosylated virulence factors in Ustilago maydis.

Alfonso Fernández-Álvarez, Miriam Marín-Menguiano, Daniel Lanver, Alberto Jiménez-Martín, Alberto Elías-Villalobos, Antonio J Pérez-Pulido, Regine Kahmann, José I Ibeas

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

  1. Protein Extraction Methods for Ustilago maydis.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Induction of Ustilago maydis Appressorium and Filamentation.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Review
  4. Article
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  9. Transcriptome Comparison between Two Strains ofJournal of fungi (Basel, Switzerland) · 2022
    Article
  10. Insights into the Structure of the Highly Glycosylated Ffase fromInternational journal of molecular sciences · 2022
    Article
  11. Secreted Glycosyltransferase RsIA_GT ofPathogens (Basel, Switzerland) · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Biotrophic Development ofThe Plant cell · 2018
    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 4 institutions in 2 countries.

Alfonso Fernández-ÁlvarezCentro Andaluz de Biología del Desarrollo, Universidad Pablo de Olavide, Consejo Superior de Investigaciones Científicas, Sevilla, Spain.
Miriam Marín-Menguiano
Daniel Lanver
Alberto Jiménez-Martín
Alberto Elías-Villalobos
Antonio J Pérez-Pulido
Regine Kahmann
José I Ibeas
Consejo Superior de Investigaciones Científicas · ESMax Planck Institute for Terrestrial Microbiology · DEUniversidad Pablo de Olavide · ESCentro Andaluz de Biología del Desarrollo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The O-mannosyltransferase Pmt4 has emerged as crucial for fungal virulence in the animal pathogens Candida albicans or Cryptococcus neoformans as well as in the phytopathogenic fungus Ustilago maydis. Pmt4 O-mannosylates specific target proteins at the Endoplasmic Reticulum. Therefore a deficient O-mannosylation of these target proteins must be responsible for the loss of pathogenicity in pmt4 mutants. Taking advantage of the characteristics described for Pmt4 substrates in Saccharomyces cerevisiae, we performed a proteome-wide bioinformatic approach to identify putative Pmt4 targets in the corn smut fungus U. maydis and validated Pmt4-mediated glycosylation of candidate proteins by electrophoretic mobility shift assays. We found that the signalling mucin Msb2, which regulates appressorium differentiation upstream of the pathogenicity-related MAP kinase cascade, is O-mannosylated by Pmt4. The epistatic relationship of pmt4 and msb2 showed that both are likely to act in the same pathway. Furthermore, constitutive activation of the MAP kinase cascade restored appressorium development in pmt4 mutants, suggesting that during the initial phase of infection the failure to O-mannosylate Msb2 is responsible for the virulence defect of pmt4 mutants. On the other hand we demonstrate that during later stages of pathogenic development Pmt4 affects virulence independently of Msb2, probably by modifying secreted effector proteins. Pit1, a protein required for fungal spreading inside the infected leaf, was also identified as a Pmt4 target. Thus, O-mannosylation of different target proteins affects various stages of pathogenic development in U. maydis.

Indexed as

Computational BiologyFungal ProteinsIntracellular Signaling Peptides and ProteinsMannosyltransferasesMolecular StructureMycotoxinsPlant DiseasesPlant ProteinsProteomicsStructure-Activity RelationshipTranscription Factor Pit-1UstilagoVirulence FactorsZea maysFungal ProteinsIntracellular Signaling Peptides and ProteinsMannosyltransferasesMycotoxinsPlant Proteinsprotein O-mannosyltransferaseTranscription Factor Pit-1Virulence Factors

Identifiers

PMID22416226
PMCPMC3295589
OpenAlexW2046398075

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.