Evidence map›Paper›PMID 28821267›Full record

ArticleVirology journal2017

Small-size recombinant adenoviral hexon protein fragments for the production of virus-type specific antibodies.

Martin Pacesa, Rodinde Hendrickx, Manuela Bieri, Justin W Flatt, Urs F Greber, Silvio Hemmi

Open access · goldAbstract read
In one paragraph

Article in Virology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.5field-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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Detection of novel adenovirus in sick pigeons.The Journal of veterinary medical science · 2018
    Article
  5. Review
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 2 institutions in 1 country.

Martin PacesaInstitute of Molecular Life Sciences, University of Zurich, CH-8057, Zurich, Switzerland.
Rodinde HendrickxInstitute of Molecular Life Sciences, University of Zurich, CH-8057, Zurich, Switzerland.
Manuela BieriInstitute of Molecular Life Sciences, University of Zurich, CH-8057, Zurich, Switzerland.
Justin W FlattInstitute of Molecular Life Sciences, University of Zurich, CH-8057, Zurich, Switzerland.
Urs F GreberInstitute of Molecular Life Sciences, University of Zurich, CH-8057, Zurich, Switzerland.
Silvio HemmiInstitute of Molecular Life Sciences, University of Zurich, CH-8057, Zurich, Switzerland. silvio.hemmi@imls.uzh.ch.
University of Zurich · CHBoard of the Swiss Federal Institutes of Technology · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAdenoviruses are common pathogens infecting animals and humans. They are classified based on serology, or genome sequence information. These methods have limitations due to lengthy procedures or lack of infectivity data. Adenoviruses are easy to produce and amenable to genetic and biochemical modifications, which makes them a powerful tool for biological studies, and clinical gene-delivery and vaccine applications. Antibodies directed against adenoviral proteins are important diagnostic tools for virus identification in vivo and in vitro, and are used to elucidate infection mechanisms, often in combination with genomic sequencing and type specific information from hyper-variable regions of structural proteins.

resultsHere we describe a novel and readily useable method for cloning, expressing and purifying small fragments of hyper-variable regions 1-6 of the adenoviral hexon protein. We used these polypeptides as antigens for generating polyclonal rabbit antibodies against human adenovirus 3 (HAdV-B3), mouse adenovirus 1 (MAdV-1) and MAdV-2 hexon. In Western immunoblots with lysates from cells infected from thirteen human and three mouse viruses, these antibodies bound to homologous full-length hexon protein and revealed variable levels of cross-reactivity to heterologous hexons. Results from immuno-fluorescence and electron microscopy studies indicated that HAdV-B3 and MAdV-2 hexon antibodies recognized native forms of hexon.

conclusionsThe procedure described here can in principle be applied to any adenovirus for which genome sequence information is available. It provides a basis for generating novel type-specific tools in diagnostics and research, and extends beyond the commonly used anti-viral antibodies raised against purified viruses or subviral components.

Indexed as

A549 CellsAdenoviridaeAdenoviridae InfectionsAdenoviruses, HumanAmino Acid SequenceAnimalsAntibodies, NeutralizingAntibodies, ViralAntigens, ViralBase SequenceBlotting, WesternCapsidCapsid ProteinsCell LineCross ReactionsDNA, ViralAntibodies, NeutralizingAntibodies, ViralAntigens, ViralCapsid ProteinsDNA, ViralEpitopeshexon capsid protein, AdenovirusRecombinant ProteinsAdenovirusAntibodiesElectron MicroscopyHexonImmunoblottingImmunofluorescenceNeutralizationProtein PurificationVirus Blocking

Identifiers

PMID28821267
PMCPMC5563037
OpenAlexW2745599348

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.