Evidence map›Paper›PMID 23633946›Full record

ArticlePLoS pathogens2013

The Mnn2 mannosyltransferase family modulates mannoprotein fibril length, immune recognition and virulence of Candida albicans.

Rebecca A Hall, Steven Bates, Megan D Lenardon, Donna M Maccallum, Jeanette Wagener, Douglas W Lowman, Michael D Kruppa, David L Williams, Frank C Odds, Alistair J P Brown and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

84 citing papers in PubMed, 121 citations in OpenAlex.

  1. Trial
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  9. Protein kinase A signaling regulates immune evasion by shaving and concealing fungal β-1,3-glucan.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  10. Dual function ofmBio · 2025
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  15. A COmBio · 2024
    Article
  16. Review
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24 more citing papers are in PubMed but not listed here.

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

11 authors at 3 institutions in 2 countries.

Rebecca A HallAberdeen Fungal Group, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, United Kingdom.
Steven Bates
Megan D Lenardon
Donna M Maccallum
Jeanette Wagener
Douglas W Lowman
Michael D Kruppa
David L Williams
Frank C Odds
Alistair J P Brown
Neil A R Gow
University of Aberdeen · GBEast Tennessee State University · USUniversity of Exeter · GB

Funding

AMELIORATION OF SEPSIS BY MACROPHAGE ACTIVATIONR01GM053522 · NIGMS · EAST TENNESSEE STATE UNIVERSITY · PI WILLIAMS, DAVID L. · 1996 to 2015
$3.4M
Biotechnology and Biological Sciences Research Council BB/F00513X/1Medical Research Council MR/J008230/1NIGMS NIH HHS R01 GM053522Wellcome TrustWellcome Trust 075470Wellcome Trust 080088Wellcome Trust 086827Wellcome Trust 099215
6 · The paper itself

Abstract

The fungal cell wall is the first point of interaction between an invading fungal pathogen and the host immune system. The outer layer of the cell wall is comprised of GPI anchored proteins, which are post-translationally modified by both N- and O-linked glycans. These glycans are important pathogen associated molecular patterns (PAMPs) recognised by the innate immune system. Glycan synthesis is mediated by a series of glycosyl transferases, located in the endoplasmic reticulum and Golgi apparatus. Mnn2 is responsible for the addition of the initial α1,2-mannose residue onto the α1,6-mannose backbone, forming the N-mannan outer chain branches. In Candida albicans, the MNN2 gene family is comprised of six members (MNN2, MNN21, MNN22, MNN23, MNN24 and MNN26). Using a series of single, double, triple, quintuple and sextuple mutants, we show, for the first time, that addition of α1,2-mannose is required for stabilisation of the α1,6-mannose backbone and hence regulates mannan fibril length. Sequential deletion of members of the MNN2 gene family resulted in the synthesis of lower molecular weight, less complex and more uniform N-glycans, with the sextuple mutant displaying only un-substituted α1,6-mannose. TEM images confirmed that the sextuple mutant was completely devoid of the outer mannan fibril layer, while deletion of two MNN2 orthologues resulted in short mannan fibrils. These changes in cell wall architecture correlated with decreased proinflammatory cytokine induction from monocytes and a decrease in fungal virulence in two animal models. Therefore, α1,2-mannose of N-mannan is important for both immune recognition and virulence of C. albicans.

Indexed as

AnimalsCandida albicansCandidiasisCell WallFemaleFungal ProteinsHumansMannansMannoseMannosyltransferasesMembrane GlycoproteinsMiceMice, Inbred BALB CPolysaccharidesReceptors, Pattern RecognitionSequence AlignmentFungal ProteinsMannansmannoproteinsMannoseMannosyltransferasesMembrane GlycoproteinsPolysaccharidesReceptors, Pattern Recognition

Identifiers

PMID23633946
PMCPMC3636026
OpenAlexW2086193922

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.