Evidence map›Paper›PMID 28714909›Full record

ReviewInternational journal of molecular sciences2017

The Interplay between the Host Receptor and Influenza Virus Hemagglutinin and Neuraminidase.

Lauren Byrd-Leotis, Richard D Cummings, David A Steinhauer

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
13.6field-weighted citation impact, top 1% 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

107 citing papers in PubMed, 210 citations in OpenAlex.

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  19. Human Riboviruses: A Comprehensive Study.Journal of molecular evolution · 2025
    Review
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47 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Lauren Byrd-LeotisDepartment Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30307, USA. labyrd@emory.edu.
Richard D CummingsDepartment of Surgery, Harvard Medical School Beth Israel Deaconess Medical Center, Boston, MA 02215, USA. rcummin1@bidmc.harvard.edu.
David A SteinhauerDepartment Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30307, USA. dsteinh@emory.edu.
Emory University · USBeth Israel Deaconess Medical Center · US

Funding

The role of NA in virus receptor interaction and HA:NA functional balanceF31AI115968 · NIAID · EMORY UNIVERSITY · PI BYRD-LEOTIS, LAUREN · 2015 to 2016
$79k
NIAID NIH HHS F31 AI115968NIAID NIH HHS HHSN272201400004C
6 · The paper itself

Abstract

The hemagglutinin (HA) and neuraminidase (NA) glycoproteins of influenza A virus are responsible for the surface interactions of the virion with the host. Entry of the virus is mediated by functions of the HA: binding to cellular receptors and facilitating fusion of the virion membrane with the endosomal membrane. The HA structure contains receptor binding sites in the globular membrane distal head domains of the trimer, and the fusion machinery resides in the stem region. These sites have specific characteristics associated with subtype and host, and the differences often define species barriers. For example, avian viruses preferentially recognize α2,3-Sialic acid terminating glycans as receptors and mammalian viruses recognize α2,6-Sialic acid. The neuraminidase, or the receptor-destroying protein, cleaves the sialic acid from cellular membrane constituents and viral glycoproteins allowing for egress of nascent virions. A functional balance of activity has been demonstrated between the two glycoproteins, resulting in an optimum level of HA affinity and NA enzymatic cleavage to allow for productive infection. As more is understood about both HA and NA, the relevance for functional balance between HA and NA continues to expand, with potential implications for interspecies transmission, host adaptation, and pathogenicity.

Indexed as

AnimalsHemagglutinin Glycoproteins, Influenza VirusHost-Pathogen InteractionsHumansInfluenza A virusMembrane ProteinsNeuraminidaseViral ProteinsVirus InternalizationHemagglutinin Glycoproteins, Influenza VirusMembrane ProteinsNeuraminidaseViral Proteinsglycan bindinghemagglutinininfluenza A virusneuraminidasevirus-host interactions

Identifiers

PMID28714909
PMCPMC5536029
OpenAlexW2735191928

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.