Evidence map›Paper›PMID 16882658›Full record

ArticleThe Journal of biological chemistry2006

A subfamily of Dr adhesins of Escherichia coli bind independently to decay-accelerating factor and the N-domain of carcinoembryonic antigen.

Natalia Korotkova, Ernesto Cota, Yuri Lebedin, Severine Monpouet, Julie Guignot, Alain L Servin, Steve Matthews, Steve L Moseley

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. The role of adhesins ofGut microbes · 2026
    Review
  2. Review
  3. Article
  4. Interactions of pathogenicFrontiers in immunology · 2023
    Review
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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 3 countries.

Natalia KorotkovaDepartment of Microbiology, University of Washington, Seattle, Washington 98195-7242, USA.
Ernesto Cota
Yuri Lebedin
Severine Monpouet
Julie Guignot
Alain L Servin
Steve Matthews
Steve L Moseley
Imperial College London · GBUniversité Paris-Saclay · FRUniversity of Washington · US

Funding

Structure, Function, and Evolution of Dr adhesinsR01DK064229 · NIDDK · UNIVERSITY OF WASHINGTON · PI MOSELEY, STEPHEN L. · 2004 to 2007
$1.3M
NIDDK NIH HHS DK-064229NIDDK NIH HHS R01 DK064229Wellcome Trust 079819
6 · The paper itself

Abstract

Escherichia coli expressing the Dr family of adhesins adheres to epithelial cells by binding to decay-accelerating factor (DAF) and carcinoembryonic antigen (CEA)-related cell surface proteins. The attachment of bacteria expressing Dr adhesins to DAF induces clustering of DAF around bacterial cells and also recruitment of CEA-related cell adhesion molecules. CEA, CEACAM1, and CEACAM6 have been shown to serve as receptors for some Dr adhesins (AfaE-I, AfaE-III, DraE, and DaaE). We demonstrate that AfaE-I, AfaE-V, DraE, and DaaE adhesins bind to the N-domain of CEA. To identify the residues involved in the N-CEA/DraE interaction, we performed SPR binding analyses of naturally occurring variants and a number of randomly generated mutants in DraE and N-CEA. Additionally, we used chemical shift mapping by NMR to determine the surface of DraE involved in N-CEA binding. These results show a distinct CEA binding site located primarily in the A, B, E, and D strands of the Dr adhesin. Interestingly, this site is located opposite to the beta-sheet encompassing the previously determined binding site for DAF, which implies that the adhesin can bind simultaneously to both receptors on the epithelial cell surface. The recognition of CEACAMs from a highly diverse DrCEA subfamily of Dr adhesins indicates that interaction with these receptors plays an important role in niche adaptation of E. coli strains expressing Dr adhesins.

Indexed as

Adhesins, BacterialAnimalsCarcinoembryonic AntigenCD55 AntigensCell AdhesionCHO CellsCricetinaeEscherichia coliFimbriae, BacterialHumansProtein BindingProtein Structure, TertiaryAdhesins, BacterialCarcinoembryonic AntigenCD55 Antigens

Identifiers

PMID16882658
PMCPMC2629542
OpenAlexW2038419256

What OpenQuestion holds

Textmetadata
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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.