Evidence map›Paper›PMID 30002445›Full record

ArticleNature communications2018

Single-pot glycoprotein biosynthesis using a cell-free transcription-translation system enriched with glycosylation machinery.

Thapakorn Jaroentomeechai, Jessica C Stark, Aravind Natarajan, Cameron J Glasscock, Laura E Yates, Karen J Hsu, Milan Mrksich, Michael C Jewett, Matthew P DeLisa

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 84 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed, 1 pooled it
11.0field-weighted citation impact, top 1% 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

84 citing papers in PubMed, 1 synthesis or guideline pooled it, 213 citations in OpenAlex.

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24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Thapakorn JaroentomeechaiRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.
Jessica C StarkDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL, 60208, USA.
Aravind NatarajanDepartment of Microbiology, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0003-2180-7842
Cameron J GlasscockRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.ORCID http://orcid.org/0000-0001-5223-6339
Laura E YatesRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA.
Karen J HsuDepartment of Mechanical Engineering, Northwestern University, 2145 Sheridan Rd Technological Institute B224, Evanston, IL, 60208-3120, USA.
Milan MrksichCenter for Synthetic Biology, Northwestern University, 2145 Sheridan Road, Evanston, IL, 60208-3120, USA.
Michael C JewettDepartment of Chemical and Biological Engineering, Northwestern University, Evanston, IL, 60208, USA. m-jewett@northwestern.edu.ORCID http://orcid.org/0000-0003-2948-6211
Matthew P DeLisaRobert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, 14853, USA. md255@cornell.edu.ORCID http://orcid.org/0000-0003-3226-1566
Cornell University · USNorthwestern University · US

Funding

DOD | Defense Threat Reduction Agency (DTRA) GRANT11631647National Science Foundation (NSF) CBET 1159581National Science Foundation (NSF) CBET 1264701National Science Foundation (NSF) MCB 1413563
6 · The paper itself

Abstract

The emerging discipline of bacterial glycoengineering has made it possible to produce designer glycans and glycoconjugates for use as vaccines and therapeutics. Unfortunately, cell-based production of homogeneous glycoproteins remains a significant challenge due to cell viability constraints and the inability to control glycosylation components at precise ratios in vivo. To address these challenges, we describe a novel cell-free glycoprotein synthesis (CFGpS) technology that seamlessly integrates protein biosynthesis with asparagine-linked protein glycosylation. This technology leverages a glyco-optimized Escherichia coli strain to source cell extracts that are selectively enriched with glycosylation components, including oligosaccharyltransferases (OSTs) and lipid-linked oligosaccharides (LLOs). The resulting extracts enable a one-pot reaction scheme for efficient and site-specific glycosylation of target proteins. The CFGpS platform is highly modular, allowing the use of multiple distinct OSTs and structurally diverse LLOs. As such, we anticipate CFGpS will facilitate fundamental understanding in glycoscience and make possible applications in on demand biomanufacturing of glycoproteins.

Indexed as

BiotechnologyEscherichia coliEscherichia coli ProteinsGlycoproteinsGlycosylationHexosyltransferasesLipopolysaccharidesMembrane ProteinsProtein BiosynthesisReproducibility of ResultsTranscription, Geneticdolichyl-diphosphooligosaccharide - protein glycotransferaseEscherichia coli ProteinsGlycoproteinsHexosyltransferaseslipid-linked oligosaccharidesLipopolysaccharidesMembrane Proteins

Identifiers

PMID30002445
PMCPMC6043479
OpenAlexW2868576343

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.