Evidence map›Paper›PMID 24050651›Full record

ArticleVirology2013

Changes in the hemagglutinin of H5N1 viruses during human infection--influence on receptor binding.

Martin Crusat, Junfeng Liu, Angelina S Palma, Robert A Childs, Yan Liu, Stephen A Wharton, Yi Pu Lin, Peter J Coombs, Stephen R Martin, Mikhail Matrosovich and 18 more

Open access · hybridAbstract read
In one paragraph

Article in Virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 35 citations in OpenAlex.

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  19. Deep sequencing: becoming a critical tool in clinical virology.Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology · 2014
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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

28 authors at 5 institutions in 6 countries.

Martin CrusatOxford University Clinical Research Unit, Hospital for Tropical Diseases, Ho Chi Minh City, Vietnam; Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
Junfeng Liu
Angelina S Palma
Robert A Childs
Yan Liu
Stephen A Wharton
Yi Pu Lin
Peter J Coombs
Stephen R Martin
Mikhail Matrosovich
Zi Chen
David J Stevens
Vo Minh Hien
Tran Tan Thanh
Le Nguyen Truc Nhu
Lam Anh Nguyet
Do Quang Ha
H Rogier van Doorn
Tran Tinh Hien
Harald S Conradt
Makoto Kiso
Steve J Gamblin
Wengang Chai
John J Skehel
Alan J Hay
Jeremy Farrar
Menno D de Jong
Ten Feizi
Hospital for Tropical Diseases · VNImperial College London · GBOxford University Clinical Research Unit · VNPhilipps University of Marburg · DERede de Química e Tecnologia · PT

Funding

Immunogenic sugar moieties of prostate cancersU01CA128416 · NCI · STANFORD UNIVERSITY · PI WANG, DENONG · 2007 to 2011
$2.3M
Biotechnology and Biological Sciences Research Council BB/G000735/1Intramural NIH HHSMedical Research Council G0600512Medical Research Council G0600522Medical Research Council MC_U117584222NCI NIH HHS U01 CA128416Wellcome Trust
6 · The paper itself

Abstract

As avian influenza A(H5N1) viruses continue to circulate in Asia and Africa, global concerns of an imminent pandemic persist. Recent experimental studies suggest that efficient transmission between humans of current H5N1 viruses only requires a few genetic changes. An essential step is alteration of the virus hemagglutinin from preferential binding to avian receptors for the recognition of human receptors present in the upper airway. We have identified receptor-binding changes which emerged during H5N1 infection of humans, due to single amino acid substitutions, Ala134Val and Ile151Phe, in the hemagglutinin. Detailed biological, receptor-binding, and structural analyses revealed reduced binding of the mutated viruses to avian-like receptors, but without commensurate increased binding to the human-like receptors investigated, possibly reflecting a receptor-binding phenotype intermediate in adaptation to more human-like characteristics. These observations emphasize that evolution in nature of avian H5N1 viruses to efficient binding of human receptors is a complex multistep process.

Indexed as

Mutation, MissenseVirus AttachmentAnimalsCrystallography, X-RayHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A Virus, H5N1 SubtypeInfluenza, HumanInfluenza in BirdsMutant ProteinsPoultryProtein BindingProtein ConformationReceptors, VirusRNA, ViralSequence Analysis, DNAhemagglutinin, avian influenza A virusHemagglutinin Glycoproteins, Influenza VirusMutant ProteinsReceptors, VirusRNA, ViralBiolayer interferometryCarbohydrate microarrayH5N1 influenza infectionHemagglutination assaysHemagglutininHemagglutinin X-ray crystal structurePyrosequencingReceptor bindingReceptor specificitySynthetic sialylglycopolymers

Identifiers

PMID24050651
PMCPMC3820038
OpenAlexW1990273710

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.