Evidence map›Paper›PMID 27939608›Full record

ArticleBiochimica et biophysica acta. Proteins and proteomics2017

Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding.

Rie Jønsson, Bing Liu, Carsten Struve, Yi Yang, René Jørgensen, Yingqi Xu, Håvard Jenssen, Karen A Krogfelt, Steve Matthews

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Proteins and proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Characterization of UropathogenicMicroorganisms · 2022
    Article
  5. Adhesin related genes as potential markers for the enteroaggregativeFrontiers in cellular and infection microbiology · 2022
    Article
  6. 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

9 authors at 3 institutions in 2 countries.

Rie JønssonInstitute for Science and Environment, Roskilde University, Roskilde, Denmark; Department of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark.
Bing LiuCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
Carsten StruveDepartment of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark.
Yi YangCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
René JørgensenDepartment of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark.
Yingqi XuCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom.
Håvard JenssenInstitute for Science and Environment, Roskilde University, Roskilde, Denmark.
Karen A KrogfeltDepartment of Microbiology and Infection Control, Statens Serum Institut, Copenhagen, Denmark. Electronic address: kak@ssi.dk.
Steve MatthewsCentre for Structural Biology, Department of Life Sciences, Imperial College London, South Kensington, London, United Kingdom. Electronic address: s.j.matthews@imperial.ac.uk.
Imperial College London · GBStatens Serum Institut · DKRoskilde University · DK

Funding

Medical Research Council G1001664Wellcome Trust 100280Wellcome Trust 104933Wellcome Trust WT100280MA
6 · The paper itself

Abstract

Enteroaggregative Escherichia coli (EAEC) is an emerging cause of acute and persistent diarrhea worldwide. The pathogenesis of different EAEC stains is complicated, however, the early essential step begins with attachment of EAEC to intestinal mucosa via aggregative adherence fimbriae (AAFs). Currently, five different variants have been identified, which all share a degree of similarity in the gene organization of their operons and sequences. Here, we report the solution structure of Agg5A from the AAF/V variant. While preserving the major structural features shared by all AAF members, only Agg5A possesses an inserted helix at the beginning of the donor strand, which together with altered surface electrostatics, renders the protein unable to interact with fibronectin. Hence, here we characterize the first AAF variant with a binding mode that varies from previously described AAFs.

Indexed as

Adhesins, Escherichia coliAmino Acid SequenceBacterial AdhesionEscherichia coliEscherichia coli InfectionsEscherichia coli ProteinsExtracellular MatrixFibronectinsFimbriae, BacterialHumansSequence AlignmentAdhesins, Escherichia coliEscherichia coli ProteinsFibronectinsAgg5AAggregative adherence fimbriaeChaperone-usherDonor strand complementationE. coliFibronectinPilin

Identifiers

PMID27939608
PMCPMC5289312
OpenAlexW2560662032

What OpenQuestion holds

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LicenceCC BY
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.