Evidence map›Paper›PMID 8617231›Full record

ArticleThe EMBO journal1996

FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5.

M Bonhivers, A Ghazi, P Boulanger, L Letellier

Abstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structural basis for host recognition and superinfection exclusion by bacteriophage T5.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  15. Article
  16. Redesign of a plugged beta-barrel membrane protein.The Journal of biological chemistry · 2011
    Article
  17. Article
  18. Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  19. FhuA (TonA), the career of a protein.Journal of bacteriology · 2009
    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

4 authors at 1 institution in 1 country.

M BonhiversLaboratoire des Biomembranes, URA CNRS 1116, Université Paris Sud, Orsay, France.
A Ghazi
P Boulanger
L Letellier
Université Paris-Sud · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Escherichia coli outer membrane protein FhuA catalyzes the transport of Fe3+(-)ferrichrome and is the receptor of phage T5 and phi 80. The purified protein inserted into planar lipid bilayers showed no channel activity. Binding of phage T5 and FhuA resulted in the appearance of high conductance ion channels. The electrophysiological characteristics of the channels (conductance, kinetic behavior, substates, ion selectivity including the effect of ferrichrome) showed similarities with those of the channel formed by a FhuA derivative from which the 'gating loop' (delta 322-355) had been removed. binding of phage T5 to FhuA in E.coli cells conferred SDS sensitivity to the bacteria, suggesting that such channels also exist in vivo. These data suggest that binding of T5 to loop 322-355 of FhuA, which constitutes the T5 binding site, unmasks an inner channel in FhuA. Both T5 and ferrichrome bind to the closed state of the channel but only T5 can trigger its opening.

Indexed as

Escherichia coli ProteinsBacterial Outer Membrane ProteinsBacteriophagesBinding SitesEscherichia coliFerrichromeIon Channel GatingIon ChannelsLipid BilayersReceptors, VirusSodium Dodecyl SulfateT-PhagesBacterial Outer Membrane ProteinsEscherichia coli ProteinsFerrichromeFhuA protein, E coliIon ChannelsLipid BilayersReceptors, VirusSodium Dodecyl Sulfate

Identifiers

PMID8617231
PMCPMC450102
OpenAlexW66814248

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.