Evidence map›Paper›PMID 20971868›Full record

ArticleApplied and environmental microbiology2010

Purification and characterization of an active N-acetylglucosaminyltransferase enzyme complex from Streptococci.

Ren Wu, Meixian Zhou, Hui Wu

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2010. 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
1.8field-weighted citation impact, top 14% 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, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Defining the enzymatic pathway for polymorphicThe Journal of biological chemistry · 2017
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Structural and biochemical analysis of a bacterial glycosyltransferase.Methods in molecular biology (Clifton, N.J.) · 2013
    Article
  15. Article
  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

3 authors at 1 institution in 1 country.

Ren WuDepartment of Pediatric Dentistry, School of Dentistry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
Meixian Zhou
Hui Wu
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
NIDCR NIH HHS R01 DE017954
6 · The paper itself

Abstract

A new family of bacterial serine-rich repeat glycoproteins can function as adhesins required for biofilm formation and pathogenesis in streptococci and staphylococci. Biogenesis of these proteins depends on a gene cluster coding for glycosyltransferases and accessory secretion proteins. Previous studies show that Fap1, a member of this family from Streptococcus parasanguinis, can be glycosylated by a protein glycosylation complex in a recombinant heterogeneous host. Here we report a tandem affinity purification (TAP) approach used to isolate and study protein complexes from native streptococci. This method demonstrated that a putative glycosyltransferase (Gtf2), which is essential for Fap1 glycosylation, readily copurified with another glycosyltransferase (Gtf1) from native S. parasanguinis. This result and the similar isolation of a homologous two-protein complex from Streptococcus pneumoniae indicate the biological relevance of the complexes to the glycosylation in streptococci. Furthermore, novel N-acetylglucosaminyltransferase activity was discovered for the complexes. Optimal activity required heterodimer formation and appears to represent a novel type of glycosylation.

Indexed as

Amino Acid SequenceChromatography, AffinityDimerizationFimbriae ProteinsGlycosylationMolecular Sequence DataN-AcetylglucosaminyltransferasesStreptococcusfap1 protein, StreptococcusFimbriae ProteinsN-AcetylglucosaminyltransferasesN-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase

Identifiers

PMID20971868
PMCPMC3008268
OpenAlexW2119980812

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.