Evidence map›Paper›PMID 33031770›Full record

ArticleCell host & microbe2020

Hemagglutinin Traits Determine Transmission of Avian A/H10N7 Influenza Virus between Mammals.

Sander Herfst, Jie Zhang, Mathilde Richard, Ryan McBride, Pascal Lexmond, Theo M Bestebroer, Monique I J Spronken, Dennis de Meulder, Judith M van den Brand, Miruna E Rosu and 10 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell host & microbe, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

  1. Pooled it
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  10. The prefusion structure of the HERV-K (HML-2) Env spike complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Viral factors underlying the pandemic potential of influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors at 4 institutions in 4 countries.

Sander HerfstDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Jie ZhangStructural Biology of Disease Processes Laboratory, the Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Mathilde RichardDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Ryan McBrideDepartments of Molecular Medicine, Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA 92037, USA.
Pascal LexmondDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Theo M BestebroerDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Monique I J SpronkenDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Dennis de MeulderDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Judith M van den BrandDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Miruna E RosuDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Stephen R MartinStructural Biology of Disease Processes Laboratory, the Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Steve J GamblinStructural Biology of Disease Processes Laboratory, the Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Xiaoli XiongStructural Biology of Disease Processes Laboratory, the Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Wenjie PengDepartments of Molecular Medicine, Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA 92037, USA.
Rogier BodewesDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Erhard van der VriesDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands.
Albert D M E OsterhausResearch Centre for Emerging Infections and Zoonoses, University of Veterinary Medicine, 30559, Hannover, Germany.
James C PaulsonDepartments of Molecular Medicine, Immunology and Microbiology, the Scripps Research Institute, La Jolla, CA 92037, USA.
John J SkehelStructural Biology of Disease Processes Laboratory, the Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Ron A M FouchierDepartment of Viroscience, Postgraduate School of Molecular Medicine, Erasmus MC University Medical Center, 3015GE, Rotterdam, the Netherlands. Electronic address: r.fouchier@erasmusmc.nl.
Erasmus MC · NLThe Francis Crick Institute · GBScripps Research Institute · USUniversity of Veterinary Medicine Hannover, Foundation · DE

Funding

Influenza virus receptors on human airway epithelial cellsR01AI114730 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI PAULSON, JAMES C · 2015 to 2023
$5.1M
NIAID NIH HHS HHSN272201400008CNIAID NIH HHS R01 AI114730Wellcome Trust FC001078Wellcome Trust FC001143
6 · The paper itself

Abstract

In 2014, an outbreak of avian A/H10N7 influenza virus occurred among seals along North-European coastal waters, significantly impacting seal populations. Here, we examine the cross-species transmission and mammalian adaptation of this influenza A virus, revealing changes in the hemagglutinin surface protein that increase stability and receptor binding. The seal A/H10N7 virus was aerosol or respiratory droplet transmissible between ferrets. Compared with avian H10 hemagglutinin, seal H10 hemagglutinin showed stronger binding to the human-type sialic acid receptor, with preferential binding to α2,6-linked sialic acids on long extended branches. In X-ray structures, changes in the 220-loop of the receptor-binding pocket caused similar interactions with human receptor as seen for pandemic strains. Two substitutions made seal H10 hemagglutinin more stable than avian H10 hemagglutinin and similar to human hemagglutinin. Consequently, identification of avian-origin influenza viruses across mammals appears critical to detect influenza A viruses posing a major threat to humans and other mammals.

Indexed as

AerosolsAnimalsBinding SitesBirdsFerretsHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A virusInfluenza A Virus, H10N7 SubtypeInfluenza in BirdsMammalsMembrane FusionModels, MolecularOrthomyxoviridae InfectionsPolysaccharidesSialic AcidsAerosolsHemagglutinin Glycoproteins, Influenza VirusPolysaccharidesSialic AcidsaerosolA/H10N7glycan microarrayshemagglutinininfluenzareceptor-bindingrespiratory dropletstabilitytransmission

Identifiers

PMID33031770
PMCPMC7556738
OpenAlexW3092043506

What OpenQuestion holds

Textmetadata
LicenceTDM
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.