Evidence map›Paper›PMID 26105055›Full record

ArticleThe Journal of biological chemistry2015

Structural Hot Spots Determine Functional Diversity of the Candida glabrata Epithelial Adhesin Family.

Rike Diderrich, Michael Kock, Manuel Maestre-Reyna, Petra Keller, Holger Steuber, Steffen Rupp, Lars-Oliver Essen, Hans-Ulrich Mösch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
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  7. Niacin Limitation PromotesPathogens (Basel, Switzerland) · 2022
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  8. Article
  9. The Flo Adhesin Family.Pathogens (Basel, Switzerland) · 2021
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Functional reprogramming ofThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. On Commensalism ofJournal of fungi (Basel, Switzerland) · 2020
    Review
  17. Article
  18. Article
  19. Microorganisms · 2019
    Review
  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

8 authors at 3 institutions in 1 country.

Rike DiderrichFrom the Departments of Genetics and.
Michael KockBiochemistry, Philipps-Universität, 35043 Marburg, Germany.
Manuel Maestre-ReynaBiochemistry, Philipps-Universität, 35043 Marburg, Germany.
Petra Kellerthe Fraunhofer-Institut für Grenzflächen und Bioverfahrenstechnik, 70569 Stuttgart, Germany, and.
Holger SteuberBiochemistry, Philipps-Universität, 35043 Marburg, Germany.
Steffen Ruppthe Fraunhofer-Institut für Grenzflächen und Bioverfahrenstechnik, 70569 Stuttgart, Germany, and the Institut für Grenzflächenverfahrenstechnik und Plasmatechnologie, Universität Stuttgart, 70569 Stuttgart, Germany.
Lars-Oliver EssenBiochemistry, Philipps-Universität, 35043 Marburg, Germany, essen@chemie.uni-marburg.de.
Hans-Ulrich MöschFrom the Departments of Genetics and moesch@staff.uni-marburg.de.
Philipps University of Marburg · DEFraunhofer Institute for Interfacial Engineering and Biotechnology · DEUniversity of Stuttgart · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For host colonization, the human fungal pathogen Candida glabrata is known to utilize a large family of highly related surface-exposed cell wall proteins, the lectin-like epithelial adhesins (Epas). To reveal the structure-function relationships within the entire Epa family, we have performed a large scale functional analysis of the adhesion (A) domains of 17 Epa paralogs in combination with three-dimensional structural studies of selected members with cognate ligands. Our study shows that most EpaA domains exert lectin-like functions and together recognize a wide variety of glycans with terminal galactosides for conferring epithelial cell adhesion. We further identify several conserved and variable structural features within the diverse Epa ligand binding pockets, which affect affinity and specificity. These features rationalize why mere phylogenetic relationships within the Epa family are weak indicators for functional classification and explain how Epa-like adhesins have evolved in C. glabrata and related fungal species.

Indexed as

Amino Acid SequenceBinding SitesBiological EvolutionCandida glabrataCell Adhesion MoleculesCrystallography, X-RayEscherichia coliFungal ProteinsGene ExpressionGenetic VariationLectinsModels, MolecularMolecular Sequence DataPhylogenyPolysaccharidesProtein BindingCell Adhesion MoleculesFungal ProteinsLectinsPolysaccharidesRecombinant ProteinsCandida glabratacell adhesioncell surfaceepithelial adhesinhost-pathogen interactionlectinPA14 domainstructure-functionyeast

Identifiers

PMID26105055
PMCPMC4528126
OpenAlexW2275145293

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.