Evidence map›Paper›PMID 34868073›Full record

ReviewFrontiers in immunology2021

Influenza Neuraminidase Characteristics and Potential as a Vaccine Target.

Sarah Creytens, Mirte N Pascha, Marlies Ballegeer, Xavier Saelens, Cornelis A M de Haan

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 1 pooled it
6.9field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 1 synthesis or guideline pooled it, 81 citations in OpenAlex.

  1. Pooled it
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  7. Article
  8. mRNA Vaccines for Influenza: Hope for a Universal Vaccine?BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Oseltamivir aziridines are potent influenza neuraminidase inhibitors and imaging agents.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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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 3 institutions in 2 countries.

Sarah CreytensVlaams Instituut voor Biotechnologie (VIB)-UGent Center for Medical Biotechnology, VIB, Ghent, Belgium.
Mirte N PaschaSection Virology, Division Infectious Diseases & Immunology, Department of Biomolecular Health Sciences, Utrecht University, Utrecht, Netherlands.
Marlies BallegeerVlaams Instituut voor Biotechnologie (VIB)-UGent Center for Medical Biotechnology, VIB, Ghent, Belgium.
Xavier SaelensVlaams Instituut voor Biotechnologie (VIB)-UGent Center for Medical Biotechnology, VIB, Ghent, Belgium.
Cornelis A M de HaanSection Virology, Division Infectious Diseases & Immunology, Department of Biomolecular Health Sciences, Utrecht University, Utrecht, Netherlands.
Utrecht University · NLVIB-UGent Center for Medical Biotechnology · BEVlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuraminidase of influenza A and B viruses plays a critical role in the virus life cycle and is an important target of the host immune system. Here, we highlight the current understanding of influenza neuraminidase structure, function, antigenicity, immunogenicity, and immune protective potential. Neuraminidase inhibiting antibodies have been recognized as correlates of protection against disease caused by natural or experimental influenza A virus infection in humans. In the past years, we have witnessed an increasing interest in the use of influenza neuraminidase to improve the protective potential of currently used influenza vaccines. A number of well-characterized influenza neuraminidase-specific monoclonal antibodies have been described recently, most of which can protect in experimental challenge models by inhibiting the neuraminidase activity or by Fc receptor-dependent mechanisms. The relative instability of the neuraminidase poses a challenge for protein-based antigen design. We critically review the different solutions that have been proposed to solve this problem, ranging from the inclusion of stabilizing heterologous tetramerizing zippers to the introduction of inter-protomer stabilizing mutations. Computationally engineered neuraminidase antigens have been generated that offer broad, within subtype protection in animal challenge models. We also provide an overview of modern vaccine technology platforms that are compatible with the induction of robust neuraminidase-specific immune responses. In the near future, we will likely see the implementation of influenza vaccines that confront the influenza virus with a double punch: targeting both the hemagglutinin and the neuraminidase.

Indexed as

AlphainfluenzavirusAntibodies, ViralAntigenic Drift and ShiftAntigens, ViralBetainfluenzavirusCatalytic DomainCross ProtectionEvolution, MolecularHumansImmunogenicity, VaccineInfluenza, HumanInfluenza VaccinesMutationNanoparticlesNeuraminidaseVaccines, SyntheticAntibodies, ViralAntigens, ViralInfluenza VaccinesNeuraminidaseVaccines, SyntheticViral Proteinsantigenic driftcorrelate of protectioninfluenzamonoclonal antibodiesneuraminidasevaccines

Identifiers

PMID34868073
PMCPMC8635103
OpenAlexW3211739003

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.