Evidence map›Paper›PMID 27358401›Full record

ArticleThe Journal of biological chemistry2016

Dectin-2 Recognizes Mannosylated O-antigens of Human Opportunistic Pathogens and Augments Lipopolysaccharide Activation of Myeloid Cells.

Alexandra Wittmann, Dimitra Lamprinaki, Kristian M Bowles, Ewa Katzenellenbogen, Yuriy A Knirel, Chris Whitfield, Takashi Nishimura, Naoki Matsumoto, Kazuo Yamamoto, Yoichiro Iwakura and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  8. The Molecular Weaponry Produced by the BacteriumMolecules (Basel, Switzerland) · 2022
    Review
  9. From structure to function - Ligand recognition by myeloid C-type lectin receptors.Computational and structural biotechnology journal · 2022
    Review
  10. Article
  11. Pattern recognition receptors in health and diseases.Signal transduction and targeted therapy · 2021
    Review
  12. Article
  13. Article
  14. Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020
    Review
  15. C-Type Lectin Receptors in Host Defense Against Bacterial Pathogens.Frontiers in cellular and infection microbiology · 2020
    Review
  16. Article
  17. Molecular basis for intestinal mucin recognition by galectin-3 and C-type lectins.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  18. Article
  19. Mechanism of pathogen recognition by human dectin-2.The Journal of biological chemistry · 2017
    Article
  20. 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

12 authors at 8 institutions in 5 countries.

Alexandra WittmannFrom the Food and Health Institute Strategic Programme, Institute of Food Research, Norwich NR4 7UA, United Kingdom.
Dimitra LamprinakiFrom the Food and Health Institute Strategic Programme, Institute of Food Research, Norwich NR4 7UA, United Kingdom.
Kristian M BowlesNorwich Medical School, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
Ewa Katzenellenbogenthe Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw 53-114, Poland.
Yuriy A Knirelthe N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow 119991, Russia.
Chris Whitfieldthe Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Takashi Nishimurathe Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan.
Naoki Matsumotothe Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan.
Kazuo Yamamotothe Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan.
Yoichiro Iwakurathe Center for Animal Disease Models, Research Institute for Biomedical Sciences, Tokyo University of Science, Chiba 278-0022, Japan, and.
Shinobu Saijothe Department of Molecular Immunology, Medical Mycology Research Center, Chiba University, Chiba 260-8673, Japan.
Norihito KawasakiFrom the Food and Health Institute Strategic Programme, Institute of Food Research, Norwich NR4 7UA, United Kingdom, the Department of Integrated Biosciences, Graduate School of Frontier Sciences, University of Tokyo, Chiba 277-8562, Japan, norihito.kawasaki@ifr.ac.uk.
Quadram Institute · GBThe University of Tokyo · JPChiba University · JPLudwik Hirszfeld Institute of Immunology and Experimental Therapy · PLN.D. Zelinsky Institute of Organic Chemistry · RUTokyo University of Science · JPUniversity of East Anglia · GBUniversity of Guelph · CA

Funding

Biotechnology and Biological Sciences Research Council BBS/E/F/00044486
6 · The paper itself

Abstract

LPS consists of a relatively conserved region of lipid A and core oligosaccharide and a highly variable region of O-antigen polysaccharide. Whereas lipid A is known to bind to the Toll-like receptor 4 (TLR4)-myeloid differentiation factor 2 (MD2) complex, the role of the O-antigen remains unclear. Here we report a novel molecular interaction between dendritic cell-associated C-type lectin-2 (Dectin-2) and mannosylated O-antigen found in a human opportunistic pathogen, Hafnia alvei PCM 1223, which has a repeating unit of [-Man-α1,3-Man-α1,2-Man-α1,2-Man-α1,2-Man-α1,3-]. H. alvei LPS induced higher levels of TNFα and IL-10 from mouse bone marrow-derived dendritic cells (BM-DCs), when compared with Salmonella enterica O66 LPS, which has a repeat of [-Gal-α1,6-Gal-α1,4-[Glc-β1,3]GalNAc-α1,3-GalNAc-β1,3-]. In a cell-based reporter assay, Dectin-2 was shown to recognize H. alvei LPS. This binding was inhibited by mannosidase treatment of H. alvei LPS and by mutations in the carbohydrate-binding domain of Dectin-2, demonstrating that H. alvei LPS is a novel glycan ligand of Dectin-2. The enhanced cytokine production by H. alvei LPS was Dectin-2-dependent, because Dectin-2 knock-out BM-DCs failed to do so. This receptor cross-talk between Dectin-2 and TLR4 involved events including spleen tyrosine kinase (Syk) activation and receptor juxtaposition. Furthermore, another mannosylated LPS from Escherichia coli O9a also bound to Dectin-2 and augmented TLR4 activation of BM-DCs. Taken together, these data indicate that mannosylated O-antigens from several Gram-negative bacteria augment TLR4 responses through interaction with Dectin-2.

Indexed as

AnimalsGram-Negative BacteriaHEK293 CellsHumansInterleukin-10Lectins, C-TypeMaleMiceMice, KnockoutMyeloid CellsO AntigensToll-Like Receptor 4Tumor Necrosis Factor-alphaCLEC6A protein, humandectin-2, mouseIL10 protein, humanIL10 protein, mouseInterleukin-10Lectins, C-TypeO AntigensTLR4 protein, humanTlr4 protein, mouseToll-Like Receptor 4Tumor Necrosis Factor-alphaimmunologylectinlipopolysaccharide (LPS)polysaccharideToll-like receptor 4 (TLR4)

Identifiers

PMID27358401
PMCPMC5016159
OpenAlexW2465950145

What OpenQuestion holds

Textmetadata
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.