Evidence map›Paper›PMID 2030668›Full record

ReviewMicrobiological reviews1991

Adherence and receptor relationships of Candida albicans.

R A Calderone, P C Braun

Open access · diamondAbstract readReview
In one paragraph

Review in Microbiological reviews, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
21.5field-weighted citation impact, top 1% 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

132 citing papers in PubMed, 389 citations in OpenAlex.

  1. Article
  2. Development and Use of a Monoclonal Antibody Specific for theFrontiers in cellular and infection microbiology · 2022
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. The Mechanistic Targets of Antifungal Agents: An Overview.Mini reviews in medicinal chemistry · 2016
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Article
  19. Article
  20. Article

72 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

2 authors at 1 institution in 1 country.

R A CalderoneDepartment of Microbiology, Georgetown University School of Medicine, Washington, D.C. 20007.
P C Braun
Georgetown University · US

Funding

C3D COMPLEMENT RECEPTOR OF CANDIDA ALBICANSR01AI025738 · NIAID · GEORGETOWN UNIVERSITY · PI CALDERONE, RICHARD ARTHUR · 1987 to 1994
–
NIAID NIH HHS AI25738
6 · The paper itself

Abstract

The cell surface of Candida albicans is composed of a variety of polysaccharides such as glucan, chitin, and mannan. The first two components primarily provide structure, while the mannan, often covalently linked to protein, constitutes the major antigen of the organism. Mannoproteins also have enzymatic activity (acid protease) and ligand-receptor functions. The complement receptors of C. albicans appear to be mannoproteins that are required for the adherence of the organism to endothelial cells. This is certainly true of the CR3-like protein of C. albicans. Proof that the CR3 is the Candida receptor for endothelial cells is derived from two observations. First, mutants lacking CR3 activity are less adherent in vitro and, in fact, less virulent. Second, the ligand recognized by the CR3 receptor (C3bi) as well as anti-CR3 antibodies blocks adherence of the organism to endothelial cells. The CR2 of C. albicans appears to promote the adherence of the organism to plastic substrates. Unlike the CR2 of mammalian cells, the Candida CR2 recognizes ligands containing the RGD sequence of amino acids in addition to the C3d ligand, which does not contain the RGD sequence. There is uncertainty as to whether the Candida CR2 and CR3 are, in fact, different proteins. A mannoprotein has also been described as the adhesin for epithelial cells. In this case, the receptor has a lectinlike activity and recognizes fucose- or glucosamine-containing glycoproteins of epithelial cells, depending on the strain of C. albicans. The oligosaccharide component of the receptor is probably not involved in ligand recognition and may serve to stabilize the receptor. However, the oligosaccharide factor 6 epitope of mannan may also provide adhesin activity in the recognition of epithelial cells. Mannoproteins can be extracted from cells by a number of reagents. Zymolyase, for instance, tends to remove structural mannoproteins, which contain relatively little protein and are linked to glucan. Reagents such as dithiothreitol, on the other hand, tend to extract mannoproteins containing higher amounts of protein that appear to have receptor function. The mannoproteins of C. albicans are dynamically expressed and may be growth phase and growth form specific.

Indexed as

Candida albicansCell AdhesionCell WallLigandsMembrane GlycoproteinsReceptors, ComplementLigandsmannoproteinsMembrane GlycoproteinsReceptors, Complement

Identifiers

PMID2030668
PMCPMC372798
OpenAlexW1890684887

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.