Evidence map›Paper›PMID 18644880›Full record

ArticleInfection and immunity2008

Beta-1,2 oligomannose adhesin epitopes are widely distributed over the different families of Candida albicans cell wall mannoproteins and are associated through both N- and O-glycosylation processes.

Chantal Fradin, Marie Christine Slomianny, Céline Mille, Annick Masset, Raymond Robert, Boualem Sendid, Joachim F Ernst, Jean Claude Michalski, Daniel Poulain

Abstract read
In one paragraph

Article in Infection and immunity, 2008. 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
1.9field-weighted citation impact, top 14% 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, 39 citations in OpenAlex.

  1. Antibodies as Models and Tools to DecipherJournal of fungi (Basel, Switzerland) · 2023
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  15. Reporters for the analysis of N-glycosylation in Candida albicans.Fungal genetics and biology : FG & B · 2013
    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

9 authors at 4 institutions in 2 countries.

Chantal FradinUMR Inserm 799, Laboratoire de Mycologie Fondamentale et Appliquée, Universitéde Lille 2, 59045 Lille cedex, France.
Marie Christine Slomianny
Céline Mille
Annick Masset
Raymond Robert
Boualem Sendid
Joachim F Ernst
Jean Claude Michalski
Daniel Poulain
Inserm · FRUnité de Glycobiologie Structurale et Fonctionnelle · FRHeinrich Heine University Düsseldorf · DEUniversité de Lille · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Beta-1,2-linked mannosides (beta-Mans) are believed to contribute to Candida albicans virulence. The presence of beta-Mans has been chemically established for two molecules (phosphopeptidomannan [PPM] and phospholipomannan) that are noncovalently linked to the cell wall, where they correspond to specific epitopes. However, a large number of cell wall mannoproteins (CWMPs) also express beta-Man epitopes, although their nature and mode of beta-mannosylation are unknown. We therefore used Western blotting to map beta-Man epitopes for the different families of mannoproteins gradually released from the cell wall according to their mode of anchorage (soluble, released by dithiothreitol, beta-1,3 glucan linked, and beta-1,6 glucan linked). Reduction of beta-Man epitope expression occurred after chemical and enzymatic deglycosylation of the different cell wall fractions, as well as in a secreted form of Hwp1, a representative of the CWMPs linked by glycosylphosphatidylinositol remnants. Enzyme-linked immunosorbent assay inhibition tests were performed to assess the presence of beta-Man epitopes in released oligomannosides. A comparison of the results obtained with CWMPs to the results obtained with PPM and the use of mutants with mutations affecting O and N glycosylation demonstrated that both O glycosylation and N glycosylation participate in the association of beta-Mans with the protein moieties of CWMPs. This process, which can alter the function of cell wall molecules and their recognition by the host, is therefore more important and more complex than originally thought, since it differs from the model established previously with PPM.

Indexed as

Antibodies, FungalAntibodies, MonoclonalBlotting, WesternCandida albicansCell WallEnzyme-Linked Immunosorbent AssayEpitope MappingEpitopesFungal ProteinsGlycosylationMannosidesMembrane GlycoproteinsProtein BindingVirulence FactorsAntibodies, FungalAntibodies, MonoclonalEpitopesFungal ProteinsmannoproteinsMannosidesMembrane GlycoproteinsVirulence Factors

Identifiers

PMID18644880
PMCPMC2546831
OpenAlexW2148894710

What OpenQuestion holds

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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.