Evidence map›Paper›PMID 27070150›Full record

ArticlePloS one2016

Binding Cooperativity Matters: A GM1-Like Ganglioside-Cholera Toxin B Subunit Binding Study Using a Nanocube-Based Lipid Bilayer Array.

Nolan C Worstell, Pratik Krishnan, Joshua D Weatherston, Hung-Jen Wu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Cholera toxin as a model ABArchives of toxicology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Advances in Mass Spectrometry of Gangliosides Expressed in Brain Cancers.International journal of molecular sciences · 2024
    Review
  9. Article
  10. Article
  11. ABToxins · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Structured clustering of the glycosphingolipid GM1 is required for membrane curvature induced by cholera toxin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  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

4 authors at 1 institution in 1 country.

Nolan C WorstellDepartment of Chemical Engineering, Texas A&M University, College Station, Texas, United States of America.
Pratik KrishnanDepartment of Chemical Engineering, Texas A&M University, College Station, Texas, United States of America.
Joshua D WeatherstonDepartment of Chemical Engineering, Texas A&M University, College Station, Texas, United States of America.
Hung-Jen WuDepartment of Chemical Engineering, Texas A&M University, College Station, Texas, United States of America.ORCID http://orcid.org/0000-0003-3082-7431
Texas A&M University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-glycan recognition is often mediated by multivalent binding. These multivalent bindings can be further complicated by cooperative interactions between glycans and individual glycan binding subunits. Here we have demonstrated a nanocube-based lipid bilayer array capable of quantitatively elucidating binding dissociation constants, maximum binding capacity, and binding cooperativity in a high-throughput format. Taking cholera toxin B subunit (CTB) as a model cooperativity system, we studied both GM1 and GM1-like gangliosides binding to CTB. We confirmed the previously observed CTB-GM1 positive cooperativity. Surprisingly, we demonstrated fucosyl-GM1 has approximately 7 times higher CTB binding capacity than GM1. In order to explain this phenomenon, we hypothesized that the reduced binding cooperativity of fucosyl-GM1 caused the increased binding capacity. This was unintuitive, as GM1 exhibited higher binding avidity (16 times lower dissociation constant). We confirmed the hypothesis using a theoretical stepwise binding model of CTB. Moreover, by taking a mixture of fucosyl-GM1 and GM2, we observed the mild binding avidity fucosyl-GM1 activated GM2 receptors enhancing the binding capacity of the lipid bilayer surface. This was unexpected as GM2 receptors have negligible binding avidity in pure GM2 bilayers. These unexpected discoveries demonstrate the importance of binding cooperativity in multivalent binding mechanisms. Thus, quantitative analysis of multivalent protein-glycan interactions in heterogeneous glycan systems is of critical importance. Our user-friendly, robust, and high-throughput nanocube-based lipid bilayer array offers an attractive method for dissecting these complex mechanisms.

Indexed as

Cholera ToxinCryoelectron MicroscopyG(M1) GangliosideG(M2) GangliosideIn Vitro TechniquesKineticsLipid BilayersMetal NanoparticlesModels, BiologicalNanotechnologyProtein BindingSilicon DioxideSilverSurface Plasmon ResonanceCholera Toxinfucosyl GM1 gangliosideG(M1) GangliosideG(M2) GangliosideLipid BilayersSilicon DioxideSilver

Identifiers

PMID27070150
PMCPMC4829222
OpenAlexW2336169204

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.