Evidence map›Paper›PMID 24923446›Full record

ArticleThe Journal of biological chemistry2014

The calcium-induced conformation and glycosylation of scavenger-rich cysteine repeat (SRCR) domains of glycoprotein 340 influence the high affinity interaction with antigen I/II homologs.

Sangeetha Purushotham, Champion Deivanayagam

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 11% 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, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.

  1. Pooled it
  2. TargetingACS medicinal chemistry letters · 2026
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  3. α2-3-Sialylated Glycoproteins AttenuateInternational journal of molecular sciences · 2026
    Article
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  5. The structure ofInfection and immunity · 2026
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  6. Article
  7. Article
  8. The catalytic domains of Streptococcus mutans glucosyltransferases: a structural analysis.Acta crystallographica. Section F, Structural biology communications · 2023
    Article
  9. Article
  10. Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.Acta crystallographica. Section D, Structural biology · 2021
    Article
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  12. Review
  13. Article
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  15. 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

2 authors at 1 institution in 1 country.

Sangeetha PurushothamFrom the Department of Vision Sciences/Center for Structural Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294-4400.
Champion DeivanayagamFrom the Department of Vision Sciences/Center for Structural Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294-4400 champy@uab.edu.
University of Alabama at Birmingham · US

Funding

Determination of the SAG Binding Motif on AgI/II of Streptococcus MutansR01DE017737 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DEIVANAYAGAM, CHAMPION CHRISTDOSS SELVAKUMAR · 2007 to 2011
$1.8M
NIDCR NIH HHS R01 DE017737NIDCR NIH HHS R01DE017737
6 · The paper itself

Abstract

Oral streptococci adhere to tooth-immobilized glycoprotein 340 (GP340) via the surface protein antigen I/II (AgI/II) and its homologs as the first step in pathogenesis. Studying this interaction using recombinant proteins, we observed that calcium increases the conformational stability of the scavenger-rich cysteine repeat (SRCRs) domains of GP340. Our results also show that AgI/II adheres specifically with nanomolar affinity to the calcium-induced SRCR conformation in an immobilized state and not in solution. This interaction is significantly dependent on the O-linked carbohydrates present on the SRCRs. This study also establishes that a single SRCR domain of GP340 contains the two surfaces to which the apical and C-terminal regions of AgI/II noncompetitively adhere. Compared with the single SRCR domain, the three tandem SRCR domains displayed a collective/cooperative increase in their bacterial adherence and aggregation. The previously described SRCRP2 peptide that was shown to aggregate several oral streptococci displayed limited aggregation and also nonspecific adherence compared to SRCR domains. Finally, we show distinct species-specific adherence/aggregation between Streptococcus mutans AgI/II and Streptococcus gordonii SspB in their interaction with the SRCRs. This study concludes that identification of the metal ion and carbohydrate adherence motifs on both SRCRs and AgI/II homologs could lead to the development of anti-adhesive inhibitors that could deter the adherence of pathogenic oral streptococci and thereby prevent the onset of infections.

Indexed as

Antigens, BacterialBacterial AdhesionCalciumCalcium-Binding ProteinsDNA-Binding ProteinsGlycosylationHumansModels, MolecularMouthProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein StabilityReceptors, Cell SurfaceRecombinant ProteinsStreptococcus gordoniiAntigens, BacterialCalciumCalcium-Binding ProteinsDMBT1 protein, humanDNA-Binding ProteinsReceptors, Cell SurfaceRecombinant ProteinsTumor Suppressor ProteinsBacterial Adherence, Antigen I/II, Streptococcus mutans, Streptococcus gordonii, Oral StreptococciBacterial AdhesionBacterial PathogenesisCalciumCell Surface ProteinCell Surface ReceptorGlycosylationInnate ImmunitySurface Plasmon Resonance (SPR)

Identifiers

PMID24923446
PMCPMC4139206
OpenAlexW2335530470

What OpenQuestion holds

Textmetadata
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.