Evidence map›Paper›PMID 23787694›Full record

ArticleNature2013

Receptor binding by an H7N9 influenza virus from humans.

Xiaoli Xiong, Stephen R Martin, Lesley F Haire, Stephen A Wharton, Rodney S Daniels, Michael S Bennett, John W McCauley, Patrick J Collins, Philip A Walker, John J Skehel and 1 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 196 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
196citing papers in PubMed, 1 pooled it
27.5field-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

196 citing papers in PubMed, 1 synthesis or guideline pooled it, 309 citations in OpenAlex.

  1. Pooled it
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  5. Review
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  11. Viral factors underlying the pandemic potential of influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025
    Review
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  13. Article
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136 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Xiaoli XiongMRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW71AA, UK.
Stephen R Martin
Lesley F Haire
Stephen A Wharton
Rodney S Daniels
Michael S Bennett
John W McCauley
Patrick J Collins
Philip A Walker
John J Skehel
Steven J Gamblin
National Institute for Health Research · GB

Funding

Medical Research Council MC_U117584222Medical Research Council MC_U117585868PHS HHS U117512723PHS HHS U117570592PHS HHS U117584222PHS HHS U117585868
6 · The paper itself

Abstract

Of the 132 people known to have been infected with H7N9 influenza viruses in China, 37 died, and many were severely ill. Infection seems to have involved contact with infected poultry. We have examined the receptor-binding properties of this H7N9 virus and compared them with those of an avian H7N3 virus. We find that the human H7 virus has significantly higher affinity for α-2,6-linked sialic acid analogues ('human receptor') than avian H7 while retaining the strong binding to α-2,3-linked sialic acid analogues ('avian receptor') characteristic of avian viruses. The human H7 virus does not, therefore, have the preference for human versus avian receptors characteristic of pandemic viruses. X-ray crystallography of the receptor-binding protein, haemagglutinin (HA), in complex with receptor analogues indicates that both human and avian receptors adopt different conformations when bound to human H7 HA than they do when bound to avian H7 HA. Human receptor bound to human H7 HA exits the binding site in a different direction to that seen in complexes formed by HAs from pandemic viruses and from an aerosol-transmissible H5 mutant. The human-receptor-binding properties of human H7 probably arise from the introduction of two bulky hydrophobic residues by the substitutions Gln226Leu and Gly186Val. The former is shared with the 1957 H2 and 1968 H3 pandemic viruses and with the aerosol-transmissible H5 mutant. We conclude that the human H7 virus has acquired some of the receptor-binding characteristics that are typical of pandemic viruses, but its retained preference for avian receptor may restrict its further evolution towards a virus that could transmit efficiently between humans, perhaps by binding to avian-receptor-rich mucins in the human respiratory tract rather than to cellular receptors.

Indexed as

AnimalsBinding SitesBirdsCrystallography, X-RayHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A virusInfluenza A Virus, H7N3 SubtypeInfluenza, HumanModels, MolecularMucinsN-Acetylneuraminic AcidProtein BindingProtein ConformationReceptors, VirusHemagglutinin Glycoproteins, Influenza VirusMucinsN-Acetylneuraminic AcidReceptors, Virus

Identifiers

PMID23787694
OpenAlexW2035546162

What OpenQuestion holds

Textmetadata
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.