Evidence map›Paper›PMID 25640475›Full record

ArticleMolecular plant pathology2015

The Penicillium digitatum protein O-mannosyltransferase Pmt2 is required for cell wall integrity, conidiogenesis, virulence and sensitivity to the antifungal peptide PAF26.

Eleonora Harries, Mónica Gandía, Lourdes Carmona, Jose F Marcos

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant pathology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
6.5field-weighted citation impact, top 4% 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

26 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Recent Advances in Pathogenicity and Biocontrol of PostharvestJournal of fungi (Basel, Switzerland) · 2026
    Review
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  17. Article
  18. Journal of fungi (Basel, Switzerland) · 2019
    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

4 authors at 1 institution in 1 country.

Eleonora HarriesDepartamento de Ciencia de los Alimentos, Instituto de Agroquímica y Tecnología de Alimentos (IATA), CSIC, Avda, Agustín Escardino-7, Paterna, 46980, Valencia, Spain.
Mónica GandíaDepartamento de Ciencia de los Alimentos, Instituto de Agroquímica y Tecnología de Alimentos (IATA), CSIC, Avda, Agustín Escardino-7, Paterna, 46980, Valencia, Spain.
Lourdes CarmonaDepartamento de Ciencia de los Alimentos, Instituto de Agroquímica y Tecnología de Alimentos (IATA), CSIC, Avda, Agustín Escardino-7, Paterna, 46980, Valencia, Spain.
Jose F MarcosDepartamento de Ciencia de los Alimentos, Instituto de Agroquímica y Tecnología de Alimentos (IATA), CSIC, Avda, Agustín Escardino-7, Paterna, 46980, Valencia, Spain.ORCID http://orcid.org/0000-0003-3339-2584
Instituto de Agroquímica y Tecnología de Alimentos · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The activity of protein O-mannosyltransferases (Pmts) affects the morphogenesis and virulence of fungal pathogens. Recently, PMT genes have been shown to determine the sensitivity of Saccharomyces cerevisiae to the antifungal peptide PAF26. This study reports the identification and characterization of the three Pdpmt genes in the citrus post-harvest pathogen Penicillium digitatum. The Pdpmt genes are expressed during fungal growth and fruit infection, with the highest induction for Pdpmt2. Pdpmt2 complemented the growth defect of the S. cerevisiae Δpmt2 strain. The Pdpmt2 gene mutation in P. digitatum caused pleiotropic effects, including a reduction in fungal growth and virulence, whereas its constitutive expression had no phenotypic effect. The Pdpmt2 null mutants also showed a distinctive colourless phenotype with a strong reduction in the number of conidia, which was associated with severe alterations in the development of conidiophores. Additional effects of the Pdpmt2 mutation were hyphal morphological alterations, increased sensitivity to cell wall-interfering compounds and a blockage of invasive growth. In contrast, the Pdpmt2 mutation increased tolerance to oxidative stress and to the antifungal activity of PAF26. These data confirm the role of protein O-glycosylation in the PAF26-mediated antifungal mechanism present in distantly related fungal species. Important to future crop protection strategies, this study demonstrates that a mutation rendering fungi more resistant to an antifungal peptide results in severe deleterious effects on fungal growth and virulence.

Indexed as

Antifungal AgentsCell WallMannosyltransferasesOligopeptidesPenicilliumVirulenceAntifungal AgentsMannosyltransferasesOligopeptidesPAF26 peptideantifungal peptidescell wallcitrus fruitPenicillium digitatumpost-harvest decayprotein glycosylation

Identifiers

PMID25640475
PMCPMC6638402
OpenAlexW1919103765

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.