Evidence map›Paper›PMID 17933909›Full record

ArticleEukaryotic cell2007

Endoplasmic reticulum alpha-glycosidases of Candida albicans are required for N glycosylation, cell wall integrity, and normal host-fungus interaction.

Héctor M Mora-Montes, Steven Bates, Mihai G Netea, Diana F Díaz-Jiménez, Everardo López-Romero, Samuel Zinker, Patricia Ponce-Noyola, Bart Jan Kullberg, Alistair J P Brown, Frank C Odds and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2007. 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
4.4field-weighted citation impact, top 5% 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, 147 citations in OpenAlex.

  1. Article
  2. Compromising UDP-sugar nucleotide biosynthesis attenuatesCell surface (Amsterdam, Netherlands) · 2026
    Article
  3. Cell surface (Amsterdam, Netherlands) · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Cell surface (Amsterdam, Netherlands) · 2025
    Article
  11. Silencing ofJournal of fungi (Basel, Switzerland) · 2025
    Article
  12. Journal of fungi (Basel, Switzerland) · 2025
    Article
  13. Review
  14. Review
  15. Journal of fungi (Basel, Switzerland) · 2024
    Article
  16. Article
  17. Silencing ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  18. Review
  19. Article
  20. Article

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

12 authors at 4 institutions in 3 countries.

Héctor M Mora-MontesInstituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Apartado Postal 187, Guanajuato, Gto. CP 36000, México.
Steven Bates
Mihai G Netea
Diana F Díaz-Jiménez
Everardo López-Romero
Samuel Zinker
Patricia Ponce-Noyola
Bart Jan Kullberg
Alistair J P Brown
Frank C Odds
Arturo Flores-Carreón
Neil A R Gow
Universidad de Guanajuato · MXUniversity of Aberdeen · GBRadboud University Nijmegen · NLCenter for Research and Advanced Studies of the National Polytechnic Institute · MX

Funding

Wellcome TrustWellcome Trust 063204Wellcome Trust 080088
6 · The paper itself

Abstract

The cell surface of Candida albicans is enriched in highly glycosylated mannoproteins that are involved in the interaction with the host tissues. N glycosylation is a posttranslational modification that is initiated in the endoplasmic reticulum (ER), where the Glc(3)Man(9)GlcNAc(2) N-glycan is processed by alpha-glucosidases I and II and alpha1,2-mannosidase to generate Man(8)GlcNAc(2). This N-oligosaccharide is then elaborated in the Golgi to form N-glycans with highly branched outer chains rich in mannose. In Saccharomyces cerevisiae, CWH41, ROT2, and MNS1 encode for alpha-glucosidase I, alpha-glucosidase II catalytic subunit, and alpha1,2-mannosidase, respectively. We disrupted the C. albicans CWH41, ROT2, and MNS1 homologs to determine the importance of N-oligosaccharide processing on the N-glycan outer-chain elongation and the host-fungus interaction. Yeast cells of Cacwh41Delta, Carot2Delta, and Camns1Delta null mutants tended to aggregate, displayed reduced growth rates, had a lower content of cell wall phosphomannan and other changes in cell wall composition, underglycosylated beta-N-acetylhexosaminidase, and had a constitutively activated PKC-Mkc1 cell wall integrity pathway. They were also attenuated in virulence in a murine model of systemic infection and stimulated an altered pro- and anti-inflammatory cytokine profile from human monocytes. Therefore, N-oligosaccharide processing by ER glycosidases is required for cell wall integrity and for host-fungus interactions.

Indexed as

AnimalsCandida albicansCell WallCytokinesEndoplasmic ReticulumFemaleGlycoside HydrolasesGlycosylationHumansMiceMice, Inbred BALB CModels, BiologicalMonocytesSaccharomyces cerevisiaeVirulenceCytokinesGlycoside Hydrolases

Identifiers

PMID17933909
PMCPMC2168260
OpenAlexW2140209943

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.