Evidence map›Paper›PMID 22319443›Full record

ArticlePLoS pathogens2012

Msb2 shedding protects Candida albicans against antimicrobial peptides.

Eva Szafranski-Schneider, Marc Swidergall, Fabien Cottier, Denis Tielker, Elvira Román, Jesus Pla, Joachim F Ernst

Abstract 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 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Role ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  5. Review
  6. Mucin Glycans: A Target for Cancer Therapy.Molecules (Basel, Switzerland) · 2023
    Review
  7. Review
  8. Review
  9. Yeast biofilm in food realms: occurrence and control.World journal of microbiology & biotechnology · 2020
    Review
  10. Review
  11. New Insights inFrontiers in cellular and infection microbiology · 2020
    Review
  12. ThemSphere · 2019
    Article
  13. Pathogens (Basel, Switzerland) · 2019
    Review
  14. Nutrient and Stress Sensing in Pathogenic Yeasts.Frontiers in microbiology · 2019
    Review
  15. Review
  16. "Tissue barriers · 2019
    Review
  17. Article
  18. Review
  19. Article
  20. 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

7 authors.

Eva Szafranski-SchneiderDepartment Biologie, Molekulare Mykologie, Heinrich-Heine-Universität, Düsseldorf, Germany.
Marc Swidergall
Fabien Cottier
Denis Tielker
Elvira Román
Jesus Pla
Joachim F Ernst

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Msb2 is a sensor protein in the plasma membrane of fungi. In the human fungal pathogen C. albicans Msb2 signals via the Cek1 MAP kinase pathway to maintain cell wall integrity and allow filamentous growth. Msb2 doubly epitope-tagged in its large extracellular and small cytoplasmic domain was efficiently cleaved during liquid and surface growth and the extracellular domain was almost quantitatively released into the growth medium. Msb2 cleavage was independent of proteases Sap9, Sap10 and Kex2. Secreted Msb2 was highly O-glycosylated by protein mannosyltransferases including Pmt1 resulting in an apparent molecular mass of >400 kDa. Deletion analyses revealed that the transmembrane region is required for Msb2 function, while the large N-terminal and the small cytoplasmic region function to downregulate Msb2 signaling or, respectively, allow its induction by tunicamycin. Purified extracellular Msb2 domain protected fungal and bacterial cells effectively from antimicrobial peptides (AMPs) histatin-5 and LL-37. AMP inactivation was not due to degradation but depended on the quantity and length of the Msb2 glycofragment. C. albicans msb2 mutants were supersensitive to LL-37 but not histatin-5, suggesting that secreted rather than cell-associated Msb2 determines AMP protection. Thus, in addition to its sensor function Msb2 has a second activity because shedding of its glycofragment generates AMP quorum resistance.

Indexed as

Antimicrobial Cationic PeptidesCandida albicansCathelicidinsCell WallFungal ProteinsGene Expression Regulation, FungalHistatinsIntracellular Signaling Peptides and ProteinsMAP Kinase Signaling SystemMembrane ProteinsMitogen-Activated Protein KinasesPeptide HydrolasesSaccharomyces cerevisiae ProteinsTunicamycinAntimicrobial Cationic PeptidesCathelicidinsFungal ProteinsHistatinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsMitogen-Activated Protein KinasesMSB2 protein, S cerevisiaePeptide HydrolasesSaccharomyces cerevisiae ProteinsTunicamycin

Identifiers

PMID22319443
PMCPMC3271078

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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.