Evidence map›Paper›PMID 30028591›Full record

ArticleACS nano2018

Engineering a Rugged Nanoscaffold To Enhance Plug-and-Display Vaccination.

Theodora U J Bruun, Anne-Marie C Andersson, Simon J Draper, Mark Howarth

Abstract read
In one paragraph

Article in ACS nano, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 174 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
174citing papers in PubMed, 1 pooled it
–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

174 citing papers in PubMed, 1 synthesis or guideline pooled it.

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

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

4 authors.

Theodora U J BruunDepartment of Biochemistry , University of Oxford , South Parks Road , Oxford OX1 3QU , United Kingdom.
Anne-Marie C AnderssonDepartment of Biochemistry , University of Oxford , South Parks Road , Oxford OX1 3QU , United Kingdom.
Simon J DraperJenner Institute , University of Oxford , Oxford OX3 7DQ , United Kingdom.
Mark HowarthDepartment of Biochemistry , University of Oxford , South Parks Road , Oxford OX1 3QU , United Kingdom.ORCID 0000-0001-8870-7147

Funding

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

Abstract

Nanoscale organization is crucial to stimulating an immune response. Using self-assembling proteins as multimerization platforms provides a safe and immunogenic system to vaccinate against otherwise weakly immunogenic antigens. Such multimerization platforms are generally based on icosahedral viruses and have led to vaccines given to millions of people. It is unclear whether synthetic protein nanoassemblies would show similar potency. Here we take the computationally designed porous dodecahedral i301 60-mer and rationally engineer this particle, giving a mutated i301 (mi3) with improved particle uniformity and stability. To simplify the conjugation of this nanoparticle, we employ a SpyCatcher fusion of mi3, such that an antigen of interest linked to the SpyTag peptide can spontaneously couple through isopeptide bond formation (Plug-and-Display). SpyCatcher-mi3 expressed solubly to high yields in Escherichia coli, giving more than 10-fold greater yield than a comparable phage-derived icosahedral nanoparticle, SpyCatcher-AP205. SpyCatcher-mi3 nanoparticles showed high stability to temperature, freeze-thaw, lyophilization, and storage over time. We demonstrate approximately 95% efficiency coupling to different transmission-blocking and blood-stage malaria antigens. Plasmodium falciparum CyRPA was conjugated to SpyCatcher-mi3 nanoparticles and elicited a high avidity antibody response, comparable to phage-derived virus-like particles despite their higher valency and RNA cargo. The simple production, precise derivatization, and exceptional ruggedness of this nanoscaffold should facilitate broad application for nanobiotechnology and vaccine development.

Indexed as

NanoparticlesNanotechnologyParticle SizePeptidesPlasmodium falciparumPorositySurface PropertiesVaccinationPeptidesSpyTag peptidebioconjugationbionanotechnologynanomedicineprotein engineeringself-assemblyvaccinationvirus-like particle

Identifiers

PMID30028591
PMCPMC6158681

What OpenQuestion holds

Textmetadata
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.