Evidence map›Paper›PMID 28852068›Full record

ArticleScientific reports2017

Interaction of lipopolysaccharides at intermolecular sites of the periplasmic Lpt transport assembly.

Cedric Laguri, Paola Sperandeo, Kevin Pounot, Isabel Ayala, Alba Silipo, Catherine M Bougault, Antonio Molinaro, Alessandra Polissi, Jean-Pierre Simorre

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. TheInternational journal of molecular sciences · 2026
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  14. Border Control: Regulating LPS Biogenesis.Trends in microbiology · 2021
    Review
  15. Review
  16. Article
  17. Review
  18. Glycan structures and their interactions with proteins. A NMR view.Current opinion in structural biology · 2020
    Review
  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

9 authors at 6 institutions in 2 countries.

Cedric LaguriUniversité Grenoble Alpes, Institut de Biologie Structurale, 71 avenue des Martyrs - CS10090, 38044, Grenoble cedex 9, France. cedric.laguri@ibs.fr.
Paola SperandeoUniversity of Milano, Department of Pharmacological and Biomolecular Sciences, Via Balzaretti 9, Milano, Italy.
Kevin PounotUniversité Grenoble Alpes, Institut de Biologie Structurale, 71 avenue des Martyrs - CS10090, 38044, Grenoble cedex 9, France.
Isabel AyalaUniversité Grenoble Alpes, Institut de Biologie Structurale, 71 avenue des Martyrs - CS10090, 38044, Grenoble cedex 9, France.
Alba SilipoUniversity of Naples Federico II, Department of Chemical Sciences, via cinthia 4, Napoli, Italy.
Catherine M BougaultUniversité Grenoble Alpes, Institut de Biologie Structurale, 71 avenue des Martyrs - CS10090, 38044, Grenoble cedex 9, France.
Antonio MolinaroUniversity of Naples Federico II, Department of Chemical Sciences, via cinthia 4, Napoli, Italy.
Alessandra PolissiUniversity of Milano, Department of Pharmacological and Biomolecular Sciences, Via Balzaretti 9, Milano, Italy. alessandra.polissi@unimi.it.
Jean-Pierre SimorreUniversité Grenoble Alpes, Institut de Biologie Structurale, 71 avenue des Martyrs - CS10090, 38044, Grenoble cedex 9, France.
Université Grenoble Alpes · FRUniversity of Milan · ITUniversity of Naples Federico II · ITCEA Grenoble · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRInstitut de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transport of lipopolysaccharides (LPS) to the surface of the outer membrane is essential for viability of Gram-negative bacteria. Periplasmic LptC and LptA proteins of the LPS transport system (Lpt) are responsible for LPS transfer between the Lpt inner and outer membrane complexes. Here, using a monomeric E. coli LptA mutant, we first show in vivo that a stable LptA oligomeric form is not strictly essential for bacteria. The LptC-LptA complex was characterized by a combination of SAXS and NMR methods and a low resolution model of the complex was determined. We were then able to observe interaction of LPS with LptC, the monomeric LptA mutant as well as with the LptC-LptA complex. A LptC-LPS complex was built based on NMR data in which the lipid moiety of the LPS is buried at the interface of the two β-jellyrolls of the LptC dimer. The selectivity of LPS for this intermolecular surface and the observation of such cavities at homo- or heteromolecular interfaces in LptC and LptA suggests that intermolecular sites are essential for binding LPS during its transport.

Indexed as

Biological TransportIntracellular SpaceLipopolysaccharidesMagnetic Resonance SpectroscopyModels, BiologicalModels, MolecularMolecular ConformationPeriplasmic ProteinsProtein BindingStructure-Activity RelationshipLipopolysaccharidesPeriplasmic Proteins

Identifiers

PMID28852068
PMCPMC5575297
OpenAlexW2747423744

What OpenQuestion holds

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Registered trials

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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.