Evidence map›Paper›PMID 28482337›Full record

ReviewCurrent opinion in structural biology2017

Recognition of microbial glycans by soluble human lectins.

Darryl A Wesener, Amanda Dugan, Laura L Kiessling

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
–field-weighted citation impact
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

57 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Ficolin-1 in pediatricInfection and immunity · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Defined Glycan Ligands for Detecting Rare l-Sugar-Binding Proteins.Journal of the American Chemical Society · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024
    Review
  17. Molecular recognition ofiScience · 2024
    Article
  18. Article
  19. Article
  20. Human oral lectin ZG16B acts as a cell wall polysaccharide probe to decode host-microbe interactions with oral commensals.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

3 authors.

Darryl A WesenerCenter for Genome Sciences and Systems Biology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Amanda DuganDepartment of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, 53706, USA.
Laura L KiesslingDepartment of Biochemistry, University of Wisconsin-Madison, 433 Babcock Drive, 53706, USA; Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, 53706, USA. Electronic address: Kiessling@chem.wisc.edu.

Funding

Chemistry-Biology Interface Training ProgramT32GM008505 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BLACKWELL, HELEN E. · 1993 to 2023
$9.8M
Synthetic Ligands for Modulating Immune Cell ResponsesR01AI055258 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KIESSLING, LAURA L · 2003 to 2024
$7.8M
The Chemistry and Biology of Galactofuranose-Containing GlycansR01AI126592 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Laura L Kiessling · 2017 to 2026
$5.2M
WUSTL Transdisciplinary Pre- and Postdoctoral Training Program in Obesity and Cardiovascular DiseaseT32HL130357 · NHLBI · WASHINGTON UNIVERSITY · PI WILFLEY, DENISE ELLA · 2016 to 2025
$4.3M
MULTIVALENT PROTEIN CARBOHYDRATE INTERACTIONSR01GM055984 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KIESSLING, LAURA L · 1997 to 2014
$3.9M
The Chemistry and Biology of Galactofuranose ResiduesR01AI063596 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KIESSLING, LAURA L · 2005 to 2014
$3.0M
The Chemistry and Biology of Galactofuranose ResiduesR56AI063596 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI KIESSLING, LAURA L · 2009 to 2009
$338k
NHLBI NIH HHS T32 HL130357NIAID NIH HHS R01 AI055258NIAID NIH HHS R01 AI063596NIAID NIH HHS R01 AI126592NIAID NIH HHS R56 AI063596NIGMS NIH HHS R01 GM055984NIGMS NIH HHS T32 GM008505
6 · The paper itself

Abstract

Human innate immune lectins that recognize microbial glycans can conduct microbial surveillance and thereby help prevent infection. Structural analysis of soluble lectins has provided invaluable insight into how these proteins recognize their cognate carbohydrate ligands and how this recognition gives rise to biological function. In this opinion, we cover the structural features of lectins that allow them to mediate microbial recognition, highlighting examples from the collectin, Reg protein, galectin, pentraxin, ficolin and intelectin families. These analyses reveal how some lectins (e.g., human intelectin-1) can recognize glycan epitopes that are remarkably diverse, yet still differentiate between mammalian and microbial glycans. We additionally discuss strategies to identify lectins that recognize microbial glycans and highlight tools that facilitate these discovery efforts.

Indexed as

MicrobiologyAnimalsHumansLectinsPolysaccharidesProtein BindingSolubilityLectinsPolysaccharides

Identifiers

PMID28482337
PMCPMC6688470

What OpenQuestion holds

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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.