Evidence map›Paper›PMID 30866786›Full record

ArticleEmerging microbes & infections2019

Neuraminidase activity and specificity of influenza A virus are influenced by haemagglutinin-receptor binding.

Jimmy Chun Cheong Lai, Herath M T K Karunarathna, Ho Him Wong, Joseph S M Peiris, John M Nicholls

Open access · goldAbstract read
In one paragraph

Article in Emerging microbes & infections, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 51 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

5 authors at 3 institutions in 2 countries.

Jimmy Chun Cheong Laia Department of Pathology , The University of Hong Kong , Hong Kong , Hong Kong SAR.
Herath M T K Karunarathnac School of Public Health , The University of Hong Kong , Hong Kong , Hong Kong SAR.
Ho Him Wonga Department of Pathology , The University of Hong Kong , Hong Kong , Hong Kong SAR.
Joseph S M Peirisb HKU-Pasteur Research Pole , The University of Hong Kong , Hong Kong , Hong Kong SAR.
John M Nichollsa Department of Pathology , The University of Hong Kong , Hong Kong , Hong Kong SAR.
HKU-Pasteur Research Pole · HKUniversity of Hong Kong · HKUniversity of Peradeniya · LK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Influenza virus haemagglutinin (HA) and neuraminidase (NA) are involved in the recognition and modulation of sialic acids on the cell surface as the virus receptor. Although the balance between two proteins functions has been found to be crucial for viral fitness, the interplay between the proteins has not been well established. Herein we present evidence for interplay between influenza HA and NA, which may affect the balance between two glycoprotein functions. NA enzymatic activities against sialoglycans were promoted by the presence of HA, which is in accordance with the level of co-existing HA. Such activity enhancement was lost when the HA-receptor binding properties were abolished by low-pH treatment or by mutations at the HA receptor binding domain. Sialidase activities of NA-containing virus-like particles and native influenza viruses were detected using different NA-assays and sialic acid substrates. Most pronounced HA-mediated NA enhancement was found when intact virions were confronted with multivalent surface-anchored substrates, which mimics the physiological conditions on cell membranes. Using recombinant viruses with altered HA bindings preference between α2,3- and α2,6-linked sialic acids, we also found that NA function against different substrates is correlated with the HA-receptor specificity. The effect of HA-receptor specificities on NA functions, together with the HA-mediated NA enhancement, may play a role in virus evasion of the mucus barrier, as well as in cross-species adaptation. Our data also indicate the importance of using multivalent substrates in future studies of NA functions.

Indexed as

AnimalsDogsHEK293 CellsHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A virusMadin Darby Canine Kidney CellsNeuraminidaseProtein BindingReceptors, Cell SurfaceSubstrate SpecificityViral ProteinsHemagglutinin Glycoproteins, Influenza VirusNA protein, influenza A virusNeuraminidaseReceptors, Cell Surfacesialic acid receptorViral ProteinsHemagglutininInfluenza virusneuraminidasereceptor interactionsialic acids

Identifiers

PMID30866786
PMCPMC6455212
OpenAlexW2920749181

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.