Evidence map›Paper›PMID 20092352›Full record

ArticleBiochemistry2010

Comparison of binding platforms yields insights into receptor binding differences between shiga toxins 1 and 2.

Michael J Flagler, Sujit S Mahajan, Ashish A Kulkarni, Suri S Iyer, Alison A Weiss

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. The diverse landscape of AB5-type toxins.Engineering microbiology · 2023
    Review
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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

5 authors at 1 institution in 1 country.

Michael J FlaglerDepartment of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, Ohio 45267, USA.
Sujit S Mahajan
Ashish A Kulkarni
Suri S Iyer
Alison A Weiss
University of Cincinnati · US

Funding

Glycoconjugate based diagnostics for bacterial toxinsU01AI075498 · NIAID · UNIVERSITY OF CINCINNATI · PI WEISS, ALISON A. · 2007 to 2011
$2.0M
Shiga Toxin Production and Role in PathogenesisR01AI064893 · NIAID · UNIVERSITY OF CINCINNATI · PI WEISS, ALISON A. · 2007 to 2011
$1.9M
NIAID NIH HHS R01 AI 064893NIAID NIH HHS R01 AI064893NIAID NIH HHS U01 AI 075498NIAID NIH HHS U01 AI075498
6 · The paper itself

Abstract

Protein-glycan interactions are typically very weak, and avid binding is achieved when proteins express multiple glycan binding sites. Shiga toxin (Stx) uses glycan receptors to enter cells. Stx has five identical binding subunits, each with three nonidentical glycan binding sites. Previous studies examined binding to biantennary glycans expressing Pk trisaccharide mimics immobilized on streptavidin, resulting in display of four trisaccharides per streptavidin face. Stx1 preferred the Pk trisaccharide of its native receptor, globotriaosylceramide (Gb3), while the more potent and clinically relevant variant, Stx2, preferred the Pk trisaccharide with the terminal galactose replaced with N-acetylgalactosamine (NHAc-Pk). In the present study, binding of Stxs to Pk analogues was examined using two experimental platforms, ELISA and surface plasmon resonance (SPR). ELISA was more sensitive than SPR. Sensitivity in the ELISA was due to high streptavidin density, suggesting that avid binding may require engagement of more than four trisaccharides. Selectivity for the Pk analogues was maintained in both experimental platforms. Glycan preference was mapped to binding site 2, since reciprocal mutation of a single amino acid (asparagine 32 of Stx1 B-subunit/serine 31 of Stx2 B-subunit) reversed binding preference. However, native Stx1 bound well to plates loaded with a 50:50 mixture of Pk-NHAc-Pk, while Stx2 bound less efficiently, suggesting that one of the Stx1 binding sites may only engage Pk, while another may tolerate either Pk or NHAc-Pk. Varying glycan structure and density across different in vitro binding platforms revealed important differences in receptor binding properties between Stx1 and Stx2.

Indexed as

Amino Acid SequenceBinding SitesEnzyme-Linked Immunosorbent AssayMolecular Sequence DataProtein BindingProtein Structure, SecondarySequence Homology, Amino AcidShiga Toxin 1Shiga Toxin 2Surface Plasmon ResonanceTrihexosylceramidesTrisaccharidesglobotriaosylceramideShiga Toxin 1Shiga Toxin 2TrihexosylceramidesTrisaccharides

Identifiers

PMID20092352
PMCPMC2857392
OpenAlexW2078377431

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.