Evidence map›Paper›PMID 39037231›Full record

ArticlemBio2024

Exploiting the Affimer platform against influenza A virus.

Oliver Debski-Antoniak, Alex Flynn, David P Klebl, Moisés H Rojas Rechy, Christian Tiede, Ian A Wilson, Stephen P Muench, Darren Tomlinson, Juan Fontana

Abstract read
In one paragraph

Article in mBio, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–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

2 citing papers in PubMed.

  1. Article
  2. 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

9 authors.

Oliver Debski-AntoniakSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0001-8239-2738
Alex Flynn *Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, United Kingdom.
David P Klebl *Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, United Kingdom.
Moisés H Rojas Rechy *School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Christian TiedeSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Ian A WilsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Stephen P MuenchAstbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, United Kingdom.
Darren TomlinsonSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Juan FontanaSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-9084-2927

Funding

Academy of Medical Sciences (The Academy of Medical Sciences) SBF002\1029Consejo Nacional de Ciencia y Tecnología (CONACYT) 773992Rosetrees Trust (Rosetrees) A1618University of Leeds University Academic Fellow schemeWellcome TrustWellcome Trust (WT) 090932/Z/09/ZWellcome Trust (WT) 108466/Z/15/ZWellcome Trust (WT) 221524/Z/20/Z
6 · The paper itself

Abstract

Influenza A virus (IAV) is well known for its pandemic potential. While current surveillance and vaccination strategies are highly effective, therapeutic approaches are often short-lived due to the high mutation rates of IAV. Recently, monoclonal antibodies (mAbs) have emerged as a promising therapeutic approach, both against current strains and future IAV pandemics. In addition to mAbs, several antibody-like alternatives exist, which aim to improve upon mAbs. Among these, Affimers stand out for their short development time, high expression levels in IMPORTANCE: Influenza A virus is one of the few viruses that can cause devastating pandemics. Due to the high mutation rates of this virus, annual vaccination is required, and antivirals are short-lived. Monoclonal antibodies present a promising approach to tackle influenza virus infections but are associated with some limitations. To improve on this strategy, we explored the Affimer platform, which are antibody-like proteins made in bacteria. By performing phage-display against a monomeric version of influenza virus fusion protein, an established viral target, we were able to isolate Affimers that inhibit influenza virus infection

Indexed as

Cryoelectron MicroscopyHemagglutinin Glycoproteins, Influenza VirusInfluenza A virusAnimalsAntiviral AgentsDogsHumansInfluenza, HumanMadin Darby Canine Kidney CellsRecombinant Fusion ProteinsAntiviral AgentsHemagglutinin Glycoproteins, Influenza VirusRecombinant Fusion ProteinsAffimercryo-electron microscopy sample preparationinfluenza A virusmAb

Identifiers

PMID39037231
PMCPMC11323568

What OpenQuestion holds

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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.