Evidence map›Paper›PMID 25755271›Full record

ReviewJournal of dental research2015

Glycosyltransferase-mediated Sweet Modification in Oral Streptococci.

F Zhu, H Zhang, H Wu

Open access · greenAbstract readReview
In one paragraph

Review in Journal of dental research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Berberine, the major bioactive compound frombioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structural Determination of Glucosyltransferase C by Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The Current Strategies in Controlling Oral Diseases by Herbal and Chemical Materials.Evidence-based complementary and alternative medicine : eCAM · 2021
    Review
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

3 authors at 1 institution in 1 country.

F ZhuDepartments of Microbiology and Pediatric Dentistry, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, AL, USA.
H ZhangDepartments of Microbiology and Pediatric Dentistry, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, AL, USA.
H WuDepartments of Microbiology and Pediatric Dentistry, Schools of Dentistry and Medicine, University of Alabama at Birmingham, Birmingham, AL, USA hwu@uab.edu.
University of Alabama at Birmingham · US

Funding

Glycosylation & Function of an Oral Streptococcal AdhesinR01DE017954 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI WU, HUI · 2007 to 2022
$5.8M
SMALL MOLECULE INHIBITORS OF CARIOGENIC BIOFILMSR01DE022350 · NIDCR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Christian Corey Melander, Hui Wu · 2012 to 2026
$4.3M
NIDCR NIH HHS R01 DE017954NIDCR NIH HHS R01DE017954NIDCR NIH HHS R01 DE022350NIDCR NIH HHS R01DE022350
6 · The paper itself

Abstract

Bacterial glycosyltransferases play important roles in bacterial fitness and virulence. Oral streptococci have evolved diverse strategies to survive and thrive in the carbohydrate-rich oral cavity. In this review, we discuss 2 important biological processes mediated by 2 distinct groups of glycosyltransferases in oral streptococci that are important for bacterial colonization and virulence. The first process is the glycosylation of highly conserved serine-rich repeat adhesins by a series of glycosyltransferases. Using Streptococcus parasanguinis as a model, we highlight new features of several glycosyltransferases that sequentially modify the serine-rich glycoprotein Fap1. Distinct features of a novel glycosyltransferase fold from a domain of unknown function 1792 are contrasted with common properties of canonical glycosyltransferases. The second biological process we cover is involved in building sticky glucan matrix to establish cariogenic biofilms by an important opportunistic pathogen Streptococcus mutans through the action of a family of 3 glucosyltransferases. We focus on discussing the structural feature of this family as a glycoside hydrolase family of enzymes. While the 2 processes are distinct, they all produce carbohydrate-coated biomolecules, which enable bacteria to stick better in the complex oral microbiome. Understanding the making of the sweet modification presents a unique opportunity to develop novel antiadhesion and antibiofilm strategies to fight infections by oral streptococci and beyond.

Indexed as

Adhesins, BacterialBiofilmsGlucansGlycosylationGlycosyltransferasesHumansMouthPolysaccharides, BacterialStreptococcusAdhesins, BacterialGlucansGlycosyltransferasesPolysaccharides, Bacterial3D molecular structurebiofilmcarbohydrateglucansglycosylationserine-rich repeat glycoproteins

Identifiers

PMID25755271
PMCPMC4502785
OpenAlexW2079505151

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.