Evidence map›Paper›PMID 30874593›Full record

ArticleScientific reports2019

SnoopLigase peptide-peptide conjugation enables modular vaccine assembly.

Anne-Marie C Andersson, Can M Buldun, David J Pattinson, Simon J Draper, Mark Howarth

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  9. Aptamers as promising nanotheranostic tools in the COVID-19 pandemic era.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022
    Review
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  15. Article
  16. Overcoming Symmetry Mismatch in Vaccine Nanoassembly through Spontaneous Amidation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  17. Overcoming Symmetry Mismatch in Vaccine Nanoassembly through Spontaneous Amidation.Angewandte Chemie (International ed. in English) · 2021
    Article
  18. Review
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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

5 authors at 1 institution in 1 country.

Anne-Marie C AnderssonDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Can M BuldunDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID 0000-0002-4586-7201
David J PattinsonJenner Institute, University of Oxford, Oxford, OX3 7DQ, UK.
Simon J DraperJenner Institute, University of Oxford, Oxford, OX3 7DQ, UK.ORCID 0000-0002-9415-1357
Mark HowarthDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. mark.howarth@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Medical Research Council MR/P001351/1Wellcome TrustWellcome Trust 106917/Z/15/Z
6 · The paper itself

Abstract

For many infectious diseases there is still no vaccine, even though potential protective antigens have been identified. Suitable platforms and conjugation routes are urgently needed to convert the promise of such antigens into broadly protective and scalable vaccines. Here we apply a newly established peptide-peptide ligation approach, SnoopLigase, for specific and irreversible coupling of antigens onto an oligomerization platform. SnoopLigase was engineered from a Streptococcus pneumoniae adhesin and enables isopeptide bond formation between two peptide tags: DogTag and SnoopTagJr. We expressed in bacteria DogTag linked to the self-assembling coiled-coil nanoparticle IMX313. This platform was stable over months at 37 °C when lyophilized, remaining reactive even after boiling. IMX-DogTag was efficiently coupled to two blood-stage malarial proteins (from PfEMP1 or CyRPA), with SnoopTagJr fused at the N- or C-terminus. We also showed SnoopLigase-mediated coupling of a telomerase peptide relevant to cancer immunotherapy. SnoopLigase-mediated nanoassembly enhanced the antibody response to both malaria antigens in a prime-boost model. Including or depleting SnoopLigase from the conjugate had little effect on the antibody response to the malarial antigens. SnoopLigase decoration represents a promising and accessible strategy for modular plug-and-display vaccine assembly, as well as providing opportunities for robust nanoconstruction in synthetic biology.

Indexed as

Adhesins, BacterialAntigens, BacterialAntigens, ProtozoanImmunoconjugatesNanoparticlesPeptidesStreptococcus pneumoniaeVaccinationVaccinesAdhesins, BacterialAntigens, BacterialAntigens, ProtozoanImmunoconjugatesPeptidesVaccines

Identifiers

PMID30874593
PMCPMC6420506
OpenAlexW2921076844

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.