Evidence map›Paper›PMID 23277582›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis.

Rui Bao, Manoj K M Nair, Wai-kwan Tang, Lothar Esser, Annapurna Sadhukhan, Robin L Holland, Di Xia, Dieter M Schifferli

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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, 41 citations in OpenAlex.

  1. The role of adhesins ofGut microbes · 2026
    Review
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  3. Review
  4. Article
  5. Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. The invasin D protein fromThe Journal of biological chemistry · 2018
    Article
  11. Structural basis forProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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 4 institutions in 1 country.

Rui BaoLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Manoj K M Nair
Wai-kwan Tang
Lothar Esser
Annapurna Sadhukhan
Robin L Holland
Di Xia
Dieter M Schifferli
University of Pennsylvania · USNational Cancer Institute · USCenter for Cancer Research · USNational Institutes of Health · US

Funding

Structural studies of fimbriae of enterotoxigenic E. coli (ETEC)ZIABC010735 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI XIA, DI S · 2009 to 2017
$1.2M
Infection Biology Training GrantT32AI078876 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI SLAUCH, JAMES M. · 2010 to 2014
$892k
The Psa fimbriae of Yersinia pestis, an adhesin with protective immunogenic propeR21AI076695 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI SCHIFFERLI, DIETER M. · 2009 to 2010
$447k
Intramural NIH HHSNIAID NIH HHS AI076695NIAID NIH HHS R21 AI076695NIAID NIH HHS T32 AI078876
6 · The paper itself

Abstract

The pH 6 antigen (Psa) of Yersinia pestis consists of fimbriae that bind to two receptors: β1-linked galactosyl residues in glycosphingolipids and the phosphocholine group in phospholipids. Despite the ubiquitous presence of either moiety on the surface of many mammalian cells, Y. pestis appears to prefer interacting with certain types of human cells, such as macrophages and alveolar epithelial cells of the lung. The molecular mechanism of this apparent selectivity is not clear. Site-directed mutagenesis of the consensus choline-binding motif in the sequence of PsaA, the subunit of the Psa fimbrial homopolymer, identified residues that abolish galactosylceramide binding, phosphatidylcholine binding, or both. The crystal structure of PsaA in complex with both galactose and phosphocholine reveals separate receptor binding sites that share a common structural motif, thus suggesting a potential interaction between the two sites. Mutagenesis of this shared structural motif identified Tyr126, which is part of the choline-binding consensus sequence but is found in direct contact with the galactose in the structure of PsaA, important for both receptor binding. Thus, this structure depicts a fimbrial subunit that forms a polymeric adhesin with a unique arrangement of dual receptor binding sites. These findings move the field forward by providing insights into unique types of multiple receptor-ligand interactions and should steer research into the synthesis of dual receptor inhibitor molecules to slow down the rapid progression of plague.

Indexed as

Amino Acid SequenceAnimalsAntigens, BacterialBacterial ProteinsBase SequenceBinding SitesCell LineCrystallography, X-RayDNA, BacterialFimbriae, BacterialGalactoseHost-Pathogen InteractionsHumansMiceModels, MolecularMolecular Sequence DataAntigens, BacterialBacterial ProteinsDNA, BacterialGalactosepH 6 antigen, YersiniaPhosphorylcholineReceptors, Cell Surface

Identifiers

PMID23277582
PMCPMC3549101
OpenAlexW2086977756

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.