Evidence map›Paper›PMID 25593075›Full record

ArticleCarbohydrate research2015

A Photobacterium sp. α2-6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens.

Li Ding, Chao Zhao, Jingyao Qu, Yanhong Li, Go Sugiarto, Hai Yu, Junru Wang, Xi Chen

Abstract read
In one paragraph

Article in Carbohydrate research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
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  13. Synthesis ofFrontiers in immunology · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Glycosyltransferase engineering for carbohydrate synthesis.Biochemical Society transactions · 2016
    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

8 authors.

Li DingDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA; College of Science, Northwest A&F University, Yangling, Shaanxi 712100, China.
Chao ZhaoDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA; Department of Nutrition and Food Safety, Fujian Agriculture and Forestry University, Fuzhou, Fujian, China.
Jingyao QuDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Yanhong LiDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Go SugiartoDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Hai YuDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Junru WangCollege of Science, Northwest A&F University, Yangling, Shaanxi 712100, China. Electronic address: wangjunru@nwsuaf.edu.cn.
Xi ChenDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA. Electronic address: xiichen@ucdavis.edu.

Funding

Oligosaccharides as antimicrobials and prebioticsR01HD065122 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2010 to 2013
$1.8M
New chemoenzymatic methods for synthesizing complex carbohydratesR01GM094523 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2013 to 2016
$1.2M
NICHD NIH HHS R01 HD065122NICHD NIH HHS R01HD065122NIGMS NIH HHS R01 GM094523NIGMS NIH HHS R01GM094523
6 · The paper itself

Abstract

In order to improve the catalytic efficiency of recombinant Photobacterium sp. JT-ISH-224 α2-6-sialyltransferase Psp2,6ST(15-501)-His6 in sialylating α-GalNAc-containing acceptors for the synthesis of tumor-associated carbohydrate antigens sialyl Tn (STn), protein crystal structure-based mutagenesis studies were carried out. Among several mutants obtained by altering the residues close to the acceptor substrate binding pocket, mutant A366G was shown to improve the sialyltransferase activity of Psp2,6ST(15-501)-His6 toward α-GalNAc-containing acceptors by 21-115% without significantly affecting its sialylation activity to β-galactosides. Furthermore, the expression level was improved from 18-40 mg L(-1) for the wild-type enzyme to 72-110 mg L(-1) for the A366G mutant. In situ generation of CMP-sialic acid in a one-pot two-enzyme system was shown effective in overcoming the high donor hydrolysis of the enzyme. Mutant A366G performed better than the wild-type Psp2,6ST(15-501)-His6 for synthesizing Neu5Acα2-6GalNAcαOSer/Thr STn antigens.

Indexed as

MutationAntigens, Tumor-Associated, CarbohydrateBacterial Proteinsbeta-D-Galactoside alpha 2-6-SialyltransferaseBinding SitesCrystallographyModels, MolecularPhotobacteriumProtein Structure, TertiaryRecombinant ProteinsSialyltransferasesAntigens, Tumor-Associated, CarbohydrateBacterial Proteinsbeta-D-Galactoside alpha 2-6-SialyltransferaseRecombinant Proteinssialosyl-Tn antigenSialyltransferasesImproved protein expressionMutagenesisSialyltransferaseSialyltransferase mutantSTn antigen

Identifiers

PMID25593075
PMCPMC9416874

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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.