Evidence map›Paper›PMID 17697132›Full record

ArticleCellular microbiology2008

The bundlin pilin protein of enteropathogenic Escherichia coli is an N-acetyllactosamine-specific lectin.

Romney M Hyland, Jiangxiao Sun, Thomas P Griener, George L Mulvey, John S Klassen, Michael S Donnenberg, Glen D Armstrong

Open access · bronzeAbstract read
In one paragraph

Article in Cellular microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

34 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Type IV pili ofEcoSal Plus · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Lectins ofBeilstein journal of organic chemistry · 2019
    Review
  10. Review
  11. Self-Conjugation of the EnteropathogenicBioMed research international · 2017
    Article
  12. Diarrheagenic Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2016
    Review
  13. Article
  14. Review
  15. Editorial.FEMS microbiology reviews · 2015
    Article
  16. [Acute diarrheal disease caused by enteropathogenic Escherichia coli in Colombia].Revista chilena de infectologia : organo oficial de la Sociedad Chilena de Infectologia · 2014
    Review
  17. Article
  18. Article
  19. Article
  20. Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012
    Review
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

7 authors at 2 institutions in 2 countries.

Romney M HylandUniversity of Calgary, Calgary, AB, Canada.
Jiangxiao Sun
Thomas P Griener
George L Mulvey
John S Klassen
Michael S Donnenberg
Glen D Armstrong
University of Calgary · CAUniversity of Maryland, Baltimore · US

Funding

MOLECULAR BASIS OF LOCALIZED ADHERENCE IN E. COLIR01AI037606 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DONNENBERG, MICHAEL S · 1995 to 2009
$2.5M
NIAID NIH HHS R01 AI037606NIAID NIH HHS R01 AI-37606
6 · The paper itself

Abstract

Synthetic N-acetyllactosamine (LacNAc) glycoside sequences coupled to BSA competitively inhibit enteropathogenic Escherichia coli (EPEC) localized adherence (LA) to human intestinal biopsy specimens and tissue culture cell monolayers. The LacNAc-specific adhesin appears to be associated with the bundle-forming pili (BFP) expressed by EPEC during the early stages of colonization. Herein, we report that recombinant bundlin inhibits EPEC LA to HEp-2 cells and binds to HEp-2 cells. Recombinant bundlin also binds, with millimolar association constants (K(assoc)), to synthetic LacNAc-Benzene and LacNAc-O(CH(2))(8)CONH(2) glycosides as assessed in the gas phase by nanoelectrospray ionization mass spectrometry. Furthermore, LacNAc-BSA inhibits LA only of EPEC strains that express alpha bundlin alleles, suggesting putative locations for the LacNAc-binding pocket in the alpha bundlin monomer. Collectively, these results suggest that alpha bundlin possesses lectin-like properties that are responsible for LacNAc-specific initial adherence of alpha bundlin-expressing EPEC strains to host intestinal epithelial cells.

Indexed as

Amino SugarsBacterial AdhesionCell LineEnteropathogenic Escherichia coliEscherichia coli ProteinsFimbriae ProteinsHumansKineticsLectinsProtein BindingRecombinant ProteinsSpectrometry, Mass, Electrospray IonizationAmino SugarsEscherichia coli ProteinsFimbriae ProteinsLectinsN-acetyllactosamineRecombinant Proteins

Identifiers

PMID17697132
PMCPMC3809902
OpenAlexW2092934126

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.