Evidence map›Paper›PMID 27752100›Full record

ArticleScientific reports2016

Viral fusion efficacy of specific H3N2 influenza virus reassortant combinations at single-particle level.

Hung-Lun Hsu, Jean K Millet, Deirdre A Costello, Gary R Whittaker, Susan Daniel

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
  5. Membrane-tethered mucin-like polypeptides sterically inhibit binding and slow fusion kinetics of influenza A virus.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  7. Review
  8. 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 1 institution in 1 country.

Hung-Lun HsuSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.
Jean K MilletDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY, USA.
Deirdre A CostelloSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.
Gary R WhittakerDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY, USA.
Susan DanielSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA.
Cornell University · US

Funding

NIAID NIH HHS HHSN272201400005C
6 · The paper itself

Abstract

Virus pseudotyping is a useful and safe technique for studying entry of emerging strains of influenza virus. However, few studies have compared different reassortant combinations in pseudoparticle systems, or compared entry kinetics of native viruses and their pseudotyped analogs. Here, vesicular stomatitis virus (VSV)-based pseudovirions displaying distinct influenza virus envelope proteins were tested for fusion activity. We produced VSV pseudotypes containing the prototypical X-31 (H3) HA, either alone or with strain-matched or mismatched N2 NAs. We performed single-particle fusion assays using total internal reflection fluorescence microscopy to compare hemifusion kinetics among these pairings. Results illustrate that matching pseudoparticles behaved very similarly to native virus. Pseudoparticles harboring mismatched HA-NA pairings fuse at significantly slower rates than native virus, and NA-lacking pseudoparticles exhibiting the slowest fusion rates. Relative viral membrane HA density of matching pseudoparticles was higher than in mismatching or NA-lacking pseudoparticles. An equivalent trend of HA expression level on cell membranes of HA/NA co-transfected cells was observed and intracellular trafficking of HA was affected by NA co-expression. Overall, we show that specific influenza HA-NA combinations can profoundly affect the critical role played by HA during entry, which may factor into viral fitness and the emergence of new pandemic influenza viruses.

Indexed as

Virus InternalizationAmino Acid SequenceAnimalsCell LineHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A Virus, H3N2 SubtypeKineticsMicroscopy, FluorescenceNeuraminidasePhylogenyReassortant VirusesSubcellular FractionsTransfectionVirionHemagglutinin Glycoproteins, Influenza VirusNeuraminidase

Identifiers

PMID27752100
PMCPMC5067655
OpenAlexW2533102129

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.