Evidence map›Paper›PMID 26172471›Full record

ArticleMolecular oral microbiology2016

Absence of capsule reveals glycan-mediated binding and recognition of salivary mucin MUC7 by Streptococcus pneumoniae.

S Thamadilok, H Roche-Håkansson, A P Håkansson, S Ruhl

Open access · greenAbstract read
In one paragraph

Article in Molecular oral microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
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  4. ThePolymers · 2024
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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

4 authors at 1 institution in 1 country.

S ThamadilokDepartment of Oral Biology, School of Dental Medicine, University at Buffalo, The State University of New York, Buffalo, NY, USA.
H Roche-HåkanssonDepartment of Microbiology and Immunology, School of Medicine and Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY, USA.
A P HåkanssonDepartment of Microbiology and Immunology, School of Medicine and Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY, USA.
S RuhlDepartment of Oral Biology, School of Dental Medicine, University at Buffalo, The State University of New York, Buffalo, NY, USA.
University at Buffalo, State University of New York · US

Funding

Microbial Recognition of Sialic Acid Diversity in the Salivary ProteomeR01DE019807 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI RUHL, STEFAN HANS-KLAUS · 2010 to 2022
$4.7M
Anesthesiology Research Training ProgramT32GM099607 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KNIGHT III, PAUL R · 2012 to 2021
$1.8M
Pneumococcal transition from nasopharyngeal biofilm carriage to otitis mediaR01DC013554 · NIDCD · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI CAMPAGNARI, ANTHONY A · 2014 to 2018
$1.7M
MINING THE ORAL MICROBIOME FOR NOVEL GLYCAN-BINDING MOLECULESR21DE025826 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI RUHL, STEFAN HANS-KLAUS, SULLAM, PAUL M. · 2015 to 2016
$638k
NIDCD NIH HHS DC013554NIDCD NIH HHS R01 DC013554NIDCR NIH HHS DE019807NIDCR NIH HHS R01 DE019807NIDCR NIH HHS R21 DE025826NIGMS NIH HHS T32 GM099607
6 · The paper itself

Abstract

Salivary proteins modulate bacterial colonization in the oral cavity and interact with systemic pathogens that pass through the oropharynx. An interesting example is the opportunistic respiratory pathogen Streptococcus pneumoniae that normally resides in the nasopharynx, but belongs to the greater Mitis group of streptococci, most of which colonize the oral cavity. Streptococcus pneumoniae also expresses a serine-rich repeat (SRR) adhesin, PsrP, which is a homologue to oral Mitis group SRR adhesins, such as Hsa of Streptococcus gordonii and SrpA of Streptococcus sanguinis. As the latter bind to salivary glycoproteins through recognition of terminal sialic acids, we wanted to determine whether S. pneumoniae also binds to salivary proteins through possibly the same mechanism. We found that only a capsule-free mutant of S. pneumoniae TIGR4 binds to salivary proteins, most prominently to mucin MUC7, but that this binding was not mediated through PsrP or recognition of sialic acid. We also found, however, that PsrP is involved in agglutination of human red blood cells (RBCs). After removal of PsrP, an additional previously masked lectin-like adhesin activity mediating agglutination of sialidase-treated RBCs becomes revealed. Using a custom-spotted glycoprotein and neoglycoprotein dot blot array, we identify candidate glycan motifs recognized by PsrP and by the putative S. pneumoniae adhesin that could perhaps be responsible for pneumococcal binding to salivary MUC7 and glycoproteins on RBCs.

Indexed as

Adhesins, BacterialAntigens, BacterialBacterial AdhesionBacterial CapsulesHemagglutinationHumansImmobilized ProteinsMembrane ProteinsMouthMucinsMutationN-Acetylneuraminic AcidNasopharynxSalivary Proteins and PeptidesStreptococcus pneumoniaeStreptococcus sanguisAdhesins, BacterialAntigens, BacterialImmobilized ProteinsMembrane ProteinsMUC7 protein, humanMucinsN-Acetylneuraminic AcidSalivary Proteins and Peptidesbacterial lectinssalivasalivary proteinsserine-rich repeat adhesins

Identifiers

PMID26172471
PMCPMC4713356
OpenAlexW1930057486

What OpenQuestion holds

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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.