Evidence map›Paper›PMID 24751665›Full record

ArticleScientific reports2014

A high-performance thioredoxin-based scaffold for peptide immunogen construction: proof-of-concept testing with a human papillomavirus epitope.

Elena Canali, Angelo Bolchi, Gloria Spagnoli, Hanna Seitz, Ivonne Rubio, Thelma A Pertinhez, Martin Müller, Simone Ottonello

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-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

18 citing papers in PubMed, 31 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Elena Canali1] Department of Life Sciences, Biochemistry and Molecular Biology Unit, University of Parma, Italy [2].
Angelo Bolchi1] Department of Life Sciences, Biochemistry and Molecular Biology Unit, University of Parma, Italy [2].
Gloria SpagnoliDepartment of Life Sciences, Biochemistry and Molecular Biology Unit, University of Parma, Italy.
Hanna SeitzGerman Cancer Research Center, Heidelberg, Germany.
Ivonne RubioGerman Cancer Research Center, Heidelberg, Germany.
Thelma A PertinhezC.I.M. Laboratory, Technopole Parma, University of Parma, Italy.
Martin MüllerGerman Cancer Research Center, Heidelberg, Germany.
Simone OttonelloDepartment of Life Sciences, Biochemistry and Molecular Biology Unit, University of Parma, Italy.
University of Parma · ITHeidelberg University · DEGerman Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Escherichia coli thioredoxin has been previously exploited as a scaffold for the presentation/stabilization of peptide aptamers as well as to confer immunogenicity to peptide epitopes. Here we focused on other key features of thioredoxin that are of general interest for the production of safer and more effective peptide immunogens, such as a high thermal stability, lack of cross-reactivity and a low-cost of production. We identified thioredoxin from the archaebacterium Pyrococcus furiosus (PfTrx) as a novel scaffold meeting all the above criteria. PfTrx is a highly thermostable and protease-resistant scaffold with a strong (poly)peptide solubilisation capacity. Anti-PfTrx antibodies did not cross-react with mouse, nor human thioredoxin. Untagged PfTrx bearing a previously identified HPV16-L2 peptide epitope was obtained in a >90% pure form with a one-step thermal purification procedure and effectively elicited the production of neutralizing anti-HPV antibodies. We thus propose PfTrx as a superior, general-purpose scaffold for the construction of safe, stable, and low-cost peptide immunogens.

Indexed as

Amino Acid SequenceAnimalsAntibodiesAntigens, ViralBacterial ProteinsCapsid ProteinsCross ReactionsEpitope MappingEpitopesHumansMetalsMiceModels, MolecularMolecular Sequence DataOncogene Proteins, ViralPapillomaviridaeAntibodiesAntigens, ViralBacterial ProteinsCapsid ProteinsEpitopesL2 protein, Human papillomavirus type 16MetalsOncogene Proteins, ViralPeptidesRecombinant Fusion ProteinsThioredoxins

Identifiers

PMID24751665
PMCPMC3994442
OpenAlexW1972696932

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.