Evidence map›Paper›PMID 24957618›Full record

ArticleJournal of bacteriology2014

Characterization of two UDP-Gal:GalNAc-diphosphate-lipid β1,3-galactosyltransferases WbwC from Escherichia coli serotypes O104 and O5.

Shuo Wang, Diana Czuchry, Bin Liu, Anna N Vinnikova, Yin Gao, Jason Z Vlahakis, Walter A Szarek, Lei Wang, Lu Feng, Inka Brockhausen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

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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

10 authors at 2 institutions in 2 countries.

Shuo WangDepartment of Medicine and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Diana CzuchryDepartment of Medicine and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Bin LiuTEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin, China.
Anna N VinnikovaDepartment of Medicine and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Yin GaoDepartment of Medicine and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
Jason Z VlahakisDepartment of Chemistry, Queen's University, Kingston, Ontario, Canada.
Walter A SzarekDepartment of Chemistry, Queen's University, Kingston, Ontario, Canada.
Lei WangTEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin, China.
Lu FengTEDA School of Biological Sciences and Biotechnology, Nankai University, Tianjin, China fenglu63@nankai.edu.cn brockhau@queensu.ca.
Inka BrockhausenDepartment of Medicine and Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada fenglu63@nankai.edu.cn brockhau@queensu.ca.
Queen's University · CANankai University · CN

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Escherichia coli displays O antigens on the outer membrane that play an important role in bacterial interactions with the environment. The O antigens of enterohemorrhagic E. coli O104 and O5 contain a Galβ1-3GalNAc disaccharide at the reducing end of the repeating unit. Several other O antigens contain this disaccharide, which is identical to the mammalian O-glycan core 1 or the cancer-associated Thomsen-Friedenreich (TF) antigen. We identified the wbwC genes responsible for the synthesis of the disaccharide in E. coli serotypes O104 and O5. To functionally characterize WbwC, an acceptor substrate analog, GalNAcα-diphosphate-phenylundecyl, was synthesized. WbwC reaction products were isolated by high-pressure liquid chromatography and analyzed by mass spectrometry, nuclear magnetic resonance, galactosidase and O-glycanase digestion, and anti-TF antibody. The results clearly showed that the Galβ1-3GalNAcα linkage was synthesized, confirming WbwCECO104 and WbwCECO5 as UDP-Gal:GalNAcα-diphosphate-lipid β1,3-Gal-transferases. Sequence analysis revealed a conserved DxDD motif, and mutagenesis showed the importance of these Asp residues in catalysis. The purified enzymes require divalent cations (Mn(2+)) for activity and are specific for UDP-Gal and GalNAc-diphosphate lipid substrates. WbwC was inhibited by bis-imidazolium salts having aliphatic chains of 18 to 22 carbons. This work will help to elucidate mechanisms of polysaccharide synthesis in pathogenic bacteria and provide technology for vaccine synthesis.

Indexed as

Amino Acid SequenceEnterohemorrhagic Escherichia coliEscherichia coli ProteinsGalactosyltransferasesGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicSerotypingEscherichia coli ProteinsGalactosyltransferasesWbwC protein, E coli

Identifiers

PMID24957618
PMCPMC4135647
OpenAlexW1984316809

What OpenQuestion holds

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Registered trials

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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.