Evidence map›Paper›PMID 29682888›Full record

ArticlePlant biotechnology journal2018

A polymeric immunoglobulin-antigen fusion protein strategy for enhancing vaccine immunogenicity.

Gina R Webster, Craig van Dolleweerd, Thais Guerra, Szymon Stelter, Sven Hofmann, Mi-Young Kim, Audrey Y-H Teh, Gil Reynolds Diogo, Alastair Copland, Mathew J Paul and 3 more

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
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  5. Review
  6. Production of Recombinant Proteins in Transgenic Tobacco Plants.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
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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

13 authors at 2 institutions in 2 countries.

Gina R WebsterInstitute for Infection and Immunity, St. George's University of London, London, UK.ORCID 0000-0001-9899-0855
Craig van DolleweerdUniversity of Canterbury, Christchurch, New Zealand.
Thais GuerraInstitute for Infection and Immunity, St. George's University of London, London, UK.
Szymon StelterInstitute for Infection and Immunity, St. George's University of London, London, UK.
Sven HofmannInstitute for Infection and Immunity, St. George's University of London, London, UK.
Mi-Young KimInstitute for Infection and Immunity, St. George's University of London, London, UK.
Audrey Y-H TehInstitute for Infection and Immunity, St. George's University of London, London, UK.
Gil Reynolds DiogoInstitute for Infection and Immunity, St. George's University of London, London, UK.
Alastair CoplandInstitute for Infection and Immunity, St. George's University of London, London, UK.
Mathew J PaulInstitute for Infection and Immunity, St. George's University of London, London, UK.
Peter HartInstitute for Infection and Immunity, St. George's University of London, London, UK.
Rajko ReljicInstitute for Infection and Immunity, St. George's University of London, London, UK.ORCID 0000-0003-4351-8355
Julian K-C MaInstitute for Infection and Immunity, St. George's University of London, London, UK.ORCID 0000-0003-0767-0042
St George's, University of London · GBUniversity of Canterbury · NZ

Funding

European Research Council Future-Pharma EC H2020 EMI-TBHotung Foundation
6 · The paper itself

Abstract

In this study, a strategy based on polymeric immunoglobulin G scaffolds (PIGS) was used to produce a vaccine candidate for Mycobacterium tuberculosis. A genetic fusion construct comprising genes encoding the mycobacterial Ag85B antigen, an immunoglobulin γ-chain fragment and the tailpiece from immunoglobulin μ chain was engineered. Expression was attempted in Chinese Hamster Ovary (CHO) cells and in Nicotiana benthamiana. The recombinant protein assembled into polymeric structures (TB-PIGS) in N. benthamiana, similar in size to polymeric IgM. These complexes were subsequently shown to bind to the complement protein C1q and FcγRs with increased affinity. Modification of the N-glycans linked to TB-PIGS by removal of xylose and fucose residues that are normally found in plant glycosylated proteins also resulted in increased affinity for low-affinity FcγRs. Immunization studies in mice indicated that TB-PIGS are highly immunogenic with and without adjuvant. However, they did not improve protective efficacy in mice against challenge with M. tuberculosis compared to conventional vaccination with BCG, suggesting that additional or alternative antigens may be needed to protect against this disease. Nevertheless, these results establish a novel platform for producing polymeric antigen-IgG γ-chain molecules with inherent functional characteristics that are desirable in vaccines.

Indexed as

AnimalsAntigens, BacterialCHO CellsCricetulusFemaleImmunoglobulin GMiceMice, Inbred BALB CMycobacterium tuberculosisNicotianaRecombinant Fusion ProteinsTuberculosis, PulmonaryTuberculosis VaccinesAntigens, BacterialImmunoglobulin GRecombinant Fusion ProteinsTuberculosis VaccinesAg85BFcγRfusion proteinimmune complexplant biotechnologytuberculosis

Identifiers

PMID29682888
PMCPMC6230950
OpenAlexW2800129484

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.