Evidence map›Paper›PMID 36382179›Full record

ReviewComputational and structural biotechnology journal2022

From structure to function - Ligand recognition by myeloid C-type lectin receptors.

Swantje Fischer, Felix Stegmann, Vinayaga Srinivasan Gnanapragassam, Bernd Lepenies

Open access · goldAbstract readReview
In one paragraph

Review in Computational and structural biotechnology journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Synthetic Ligands of Myeloid C-Type Lectin Receptors.Chembiochem : a European journal of chemical biology · 2026
    Review
  3. Article
  4. Infection and immunity · 2026
    Article
  5. Antiviral Role of Surface Layer Protein A (SlpA) ofPathogens (Basel, Switzerland) · 2026
    Article
  6. Review
  7. Article
  8. Review
  9. The Immune Microenvironment in Liver Cancer: From Analysis to Targeting.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  10. Article
  11. Review
  12. Review
  13. Implications of Mucin-TypeMolecules (Basel, Switzerland) · 2025
    Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. New insights into SYK targeting in solid tumors.Trends in pharmacological sciences · 2024
    Review
  19. iScience · 2024
    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

4 authors at 1 institution in 1 country.

Swantje FischerInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany.
Felix StegmannInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany.
Vinayaga Srinivasan GnanapragassamInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany.
Bernd LepeniesInstitute for Immunology, University of Veterinary Medicine Hannover, 30559 Hannover, Germany.
University of Veterinary Medicine Hannover, Foundation · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The relevance of protein-glycan interactions in immunity has long been underestimated. Yet, the immune system possesses numerous classes of glycan-binding proteins, so-called lectins. Of specific interest is the group of myeloid C-type lectin receptors (CLRs) as they are mainly expressed by myeloid cells and play an important role in the initiation of an immune response. Myeloid CLRs represent a major group amongst pattern recognition receptors (PRRs), placing them at the center of the rapidly growing field of glycoimmunology. CLRs have evolved to encompass a wide range of structures and functions and to recognize a large number of glycans and many other ligands from different classes of biopolymers. This review aims at providing the reader with an overview of myeloid CLRs and selected ligands, while highlighting recent insights into CLR-ligand interactions. Subsequently, methodological approaches in CLR-ligand research will be presented. Finally, this review will discuss how CLR-ligand interactions culminate in immunological functions, how glycan mimicry favors immune escape by pathogens, and in which way immune responses can be affected by CLR-ligand interactions in the long term.

Indexed as

BCG, Bacillus Calmette-GuérinCLR, C-type lectin receptorCRD, Carbohydrate recognition domainCTL, C-type lectinCTLD, C-type lectin-like domainC-type lectin receptorsDAMP, Danger-associated molecular patternDAP12, DNAX-activation protein 12DCAR, Dendritic cell immunoactivating receptorDC, Dendritic cellDCIR, Dendritic cell immunoreceptorDC-SIGN, Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrinDectin, Dendritic cell-associated C-type lectin receptorDLS, Dynamic light scatteringDNGR, Dendritic cell natural killer lectin group receptorECD, Extracellular domainECM, Experimental cerebral malariaELISA, Enzyme-linked-immunosorbent-assayFc, Fragment crystallizableFcRγ, Fragment crystallizable receptor γFRET, Förster resonance energy transferFuc, FucoseGal, GalactoseGalNAc, N-acetylgalactosamineGlc, GlucoseGlcNAc, N-acetylglucosamineGTfs, GlycosyltransferasesHIV-1, Human immunodeficiency virus 1HLA, Human leukocyte antigenHost-pathogen interactionHSPC, Hematopoietic stem and progenitor cellsIg, ImmunoglobulinIL, InterleukinImmune modulationITAM, Immunoreceptor tyrosine-based activating motifITC, Isothermal titration calorimetryITIM, Immunoreceptor tyrosine-based inhibitory motifLac, Lactose (Gal-β1,4-Glc)LacNAc, N-acetyllactosamine (Gal-β1,4-GlcNAc)Le, LewisLigand identificationLPS, LipopolysaccharideMan, MannoseMBP, Mannan-binding proteinMCL, Macrophage C-type lectinMDL, Myeloid DAP12-associating lectinMD, Molecular dynamicsMGDG, MonoglucosyldiacylglycerolMGL, Macrophage galactose-type lectinMHC, Major histocompatibility complexMICL, Myeloid inhibitory C type-like lectinMincle, Macrophage inducible Ca2+-dependent lectin receptorMMR, Macrophage mannose receptorMSU, Monosodium uratemTOR, Mammalian target of rapamycinMφ, MacrophagesNFAT, Nuclear factor of activated T-cellsNF-κB, Nuclear factor kappa BNK, Natural killer (cells)NMR, Nuclear magnet resonancePAMP, Pathogen-associated molecular patternPDPN, PodoplaninPRR, Pattern recognition receptorQCM, Quartz crystal microbalanceRaf-1, Rapidly accelerated fibrosarcoma 1RIA, RadioimmunoassaysROS, Reactive oxygen speciesSAMP, Self-associated molecular patternSAP130, Spliceosome-associated protein 130SARS-CoV, SARS coronavirusSelf-non-self-discriminationSH2, Src-homology 2SHP, Src homology region 2 domain-containing phosphataseSignaling flexibilitySIGNR, Specific intracellular adhesion molecule-3 grabbing non-integrin homolog-relatedSPR, Surface plasmon resonanceSYK, Spleen tyrosine kinaseTCA, Tricarboxylic acidTDM, Trehalose-6,6′-dimycolateTLC, Thin-layer chromatographyTLR, Toll-like receptorTNF, Tumor necrosis factorWTA, Wall teichoic acid

Identifiers

PMID36382179
PMCPMC9630629
OpenAlexW4306893982

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.