Evidence map›Paper›PMID 36071433›Full record

ArticleMicrobial cell factories2022

Modification of avian pathogenic Escherichia coli χ7122 lipopolysaccharide increases accessibility to glycoconjugate antigens.

Alexander A Smith, Ricardo Corona-Torres, Rachel E Hewitt, Mark P Stevens, Andrew J Grant, Glycoengineering of Veterinary Vaccines Consortium

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed, 1 pooled it
2.2field-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

2 citing papers in PubMed, 1 synthesis or guideline pooled it, 10 citations in OpenAlex.

  1. Pooled it
  2. 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

6 authors at 3 institutions in 1 country.

Alexander A SmithDepartment of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge, UK.
Ricardo Corona-TorresThe Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh, Easter Bush, Midlothian, UK.
Rachel E HewittDepartment of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge, UK.
Mark P StevensThe Roslin Institute and Royal (Dick) School of Veterinary Studies, University of Edinburgh, Easter Bush, Midlothian, UK.
Andrew J GrantDepartment of Veterinary Medicine, University of Cambridge, Madingley Road, Cambridge, UK. ajg60@cam.ac.uk.
Glycoengineering of Veterinary Vaccines Consortium
University of Cambridge · GBRoslin Institute · GBUniversity of Edinburgh · GB

Funding

BBSRC BBS/E/D/20002174Biotechnology and Biological Sciences Research Council BB/N001591/1
6 · The paper itself

Abstract

backgroundWorldwide, an estimated 70.7 billion broilers were produced in 2020. With the reduction in use of prophylactic antibiotics as a result of consumer pressure and regulatory oversight alternative approaches, such as vaccination, are required to control bacterial infections. A potential way to produce a multivalent vaccine is via the generation of a glycoconjugate vaccine which consists of an antigenic protein covalently linked to an immunogenic carbohydrate. Protein-glycan coupling technology (PGCT) is an approach to generate glycoconjugates using enzymes that can couple proteins and glycan when produced in bacterial cells. Previous studies have used PGCT to generate a live-attenuated avian pathogenic Escherichia coli (APEC) strain capable of N-glycosylation of target proteins using a chromosomally integrated Campylobacter jejuni pgl locus. However, this proved ineffective against C. jejuni challenge.

resultsIn this study we demonstrate the lack of surface exposure of glycosylated protein in APEC strain χ7122 carrying the pgl locus. Furthermore, we hypothesise that this may be due to the complex cell-surface architecture of E. coli. To this end, we removed the lipopolysaccharide O-antigen of APEC χ7122 pgl

conclusionsOur results demonstrate an increase in cell surface exposure and therefore accessibility of glycosylated antigens upon removal of lipopolysaccharide antigen from the APEC cell surface.

Indexed as

Escherichia coliEscherichia coli InfectionsAnimalsChickensGlycoconjugatesLipopolysaccharidesGlycoconjugatesLipopolysaccharidesGlycoconjugate lipopolysaccharidePoultryProtein glycan coupling technologyVaccine

Identifiers

PMID36071433
PMCPMC9449299
OpenAlexW4294991647

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.