Evidence map›Paper›PMID 24591200›Full record

ArticleInnate immunity2015

Soluble human TLR2 ectodomain binds diacylglycerol from microbial lipopeptides and glycolipids.

Maximiliano J Jiménez-Dalmaroni, Catherine M Radcliffe, David J Harvey, Mark R Wormald, Petra Verdino, Gary D Ainge, David S Larsen, Gavin F Painter, Richard Ulevitch, Bruce Beutler and 3 more

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

Article in Innate immunity, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. A two-step bioconjugation ofRSC chemical biology · 2026
    Article
  2. Anti-Inflammatory Efficacy of Human-DerivedJournal of microbiology and biotechnology · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Structural basis for inhibition of TLR2 by staphylococcal superantigen-like protein 3 (SSL3).Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Review
  11. 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

13 authors at 4 institutions in 3 countries.

Maximiliano J Jiménez-DalmaroniGlycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, UK Department of Integrative Structural and Computational Biology, and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA.
Catherine M RadcliffeGlycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, UK.
David J HarveyGlycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, UK.
Mark R WormaldGlycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, UK.
Petra VerdinoDepartment of Integrative Structural and Computational Biology, and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA.
Gary D AingeDepartment of Chemistry, University of Otago, Dunedin, New Zealand.
David S LarsenDepartment of Chemistry, University of Otago, Dunedin, New Zealand.
Gavin F PainterThe Ferrier Research Institute, Victoria University Of Wellington, Gracefield Research Centre, Lower Hutt, New Zealand.
Richard UlevitchDepartment of Immunology and Microbial Sciences, The Scripps Research Institute, La Jolla, CA, USA.
Bruce BeutlerDepartment of Genetics, The Scripps Research Institute, La Jolla, CA, USA.
Pauline M RuddGlycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, UK.
Raymond A DwekGlycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, UK.
Ian A WilsonDepartment of Integrative Structural and Computational Biology, and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA wilson@scripps.edu.
University of Oxford · GBScripps Research Institute · USUniversity of Otago · NZVictoria University of Wellington · NZ

Funding

Structural Basis of T Cell Receptor RecognitionR37AI042266 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2003 to 2012
$5.8M
Structural basis of TLR and NLR recognition and signalingR01AI042266 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 1998 to 2017
$3.7M
NIAID NIH HHS AI42266NIAID NIH HHS R01 AI042266NIAID NIH HHS R37 AI042266Wellcome Trust
6 · The paper itself

Abstract

TLRs are key innate immune receptors that recognize conserved features of biological molecules that are found in microbes. In particular, TLR2 has been reported to be activated by different kinds of microbial ligands. To advance our understanding of the interaction of TLR2 with its ligands, the recombinant human TLR2 ectodomain (hTLR2ED) was expressed using a baculovirus/insect cell expression system and its biochemical, as well as ligand binding, properties were investigated. The hTLR2ED binds synthetic bacterial and mycoplasmal lipopeptides, lipoteichoic acid from Staphylococcus aureus, and synthetic lipoarabinomannan precursors from Mycobacterium at extracellular physiological conditions, in the absence of its co-receptors TLR1 and TLR6. We also determined that lipopeptides and glycolipids cannot bind simultaneously to hTLR2ED and that the phosphatidyl inositol mannoside 2 (Pim2) is the minimal lipoarabinomannan structure for binding to hTLR2ED. Binding of hTLR2ED to Pim4, which contains a diacylglycerol group with one of its acyl chains containing 19 carbon atoms, indicates that hTLR2ED can bind ligands with acyl chains longer than 16 carbon atoms. In summary, our data indicate that diacylglycerol is the ligand moiety of microbial glycolipids and lipoproteins that bind to hTLR2ED and that both types of ligands bind to the same binding site of hTLR2ED.

Indexed as

AnimalsBacterial ProteinsBaculoviridaeDiglyceridesGlycolipidsHost-Pathogen InteractionsHumansInsectaLigandsLipopeptidesLipopolysaccharidesMycobacteriumMycoplasmaPhosphatidylinositolsProtein BindingProtein Structure, TertiaryBacterial ProteinsDiglyceridesGlycolipidsLigandsLipopeptidesLipopolysaccharideslipoteichoic acidphosphatidylinositol mannosidePhosphatidylinositolsTeichoic AcidsTLR2 protein, humanToll-Like Receptor 2Diacylglycerol ligandsFSL-1lipoarabinomannanlipoteichoic acidTLR2

Identifiers

PMID24591200
PMCPMC4392886
OpenAlexW1978781089

What OpenQuestion holds

Textmetadata
LicenceTDM
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.