Evidence map›Paper›PMID 24631690›Full record

ArticleBiochemical and biophysical research communications2014

High-resolution crystal structure of HA33 of botulinum neurotoxin type B progenitor toxin complex.

Kwangkook Lee, Kwok-Ho Lam, Anna Magdalena Kruel, Kay Perry, Andreas Rummel, Rongsheng Jin

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Gut mucin fucosylation dictates the entry of botulinum toxin complexes.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Inhibiting oral intoxication of botulinum neurotoxin A complex by carbohydrate receptor mimics.Toxicon : official journal of the International Society on Toxinology · 2015
    Article
  15. Review
  16. Article
  17. 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

6 authors at 3 institutions in 2 countries.

Kwangkook LeeDepartment of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.
Kwok-Ho LamDepartment of Physiology and Biophysics, University of California, Irvine, CA 92697, USA.
Anna Magdalena KruelInstitut für Toxikologie, Medizinische Hochschule Hannover, Hannover, Germany.
Kay PerryNE-CAT and Department of Chemistry and Chemical Biology, Cornell University, Argonne National Laboratory, Argonne, IL, USA.
Andreas RummelInstitut für Toxikologie, Medizinische Hochschule Hannover, Hannover, Germany.
Rongsheng JinDepartment of Physiology and Biophysics, University of California, Irvine, CA 92697, USA. Electronic address: r.jin@uci.edu.
University of California, Irvine · USMedizinische Hochschule Hannover · DEArgonne National Laboratory · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Structural and functional studies of botulinum neurotoxinR01AI091823 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI JIN, RONGSHENG · 2012 to 2016
$2.0M
NIAID NIH HHS R01 AI091823NIAID NIH HHS R01AI091823NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

Botulinum neurotoxins (BoNTs) are produced as progenitor toxin complexes (PTCs) by Clostridium botulinum. The PTCs are composed of BoNT and non-toxic neurotoxin-associated proteins (NAPs), which serve to protect and deliver BoNT through the gastrointestinal tract in food borne botulism. HA33 is a key NAP component that specifically recognizes host carbohydrates and helps enrich PTC on the intestinal lumen preceding its transport across the epithelial barriers. Here, we report the crystal structure of HA33 of type B PTC (HA33/B) in complex with lactose at 1.46Å resolution. The structural comparisons among HA33 of serotypes A-D reveal two different HA33-glycan interaction modes. The glycan-binding pockets on HA33/A and B are more suitable to recognize galactose-containing glycans in comparison to the equivalent sites on HA33/C and D. On the contrary, HA33/C and D could potentially recognize Neu5Ac as an independent receptor, whereas HA33/A and B do not. These findings indicate that the different oral toxicity and host susceptibility observed among different BoNT serotypes could be partly determined by the serotype-specific interaction between HA33 and host carbohydrate receptors. Furthermore, we have identified a key structural water molecule that mediates the HA33/B-lactose interactions. It provides the structural basis for development of new receptor-mimicking compounds, which have enhanced binding affinity with HA33 through their water-displacing moiety.

Indexed as

Models, ChemicalModels, MolecularBinding SitesBotulinum ToxinsBotulinum Toxins, Type AComputer SimulationLactoseMolecular ConformationProtein BindingWaterBotulinum ToxinsBotulinum Toxins, Type ALactoserimabotulinumtoxinBWaterBotulinum neurotoxinsCarbohydrate receptorHemagglutininHost–pathogen interactionProgenitor toxin complex

Identifiers

PMID24631690
PMCPMC4020412
OpenAlexW2129708906

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Registered trials

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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.