Evidence map›Paper›PMID 24277851›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Cross-neutralizing human anti-poliovirus antibodies bind the recognition site for cellular receptor.

Zhaochun Chen, Elizabeth R Fischer, Diana Kouiavskaia, Bryan T Hansen, Steven J Ludtke, Bella Bidzhieva, Michelle Makiya, Liane Agulto, Robert H Purcell, Konstantin Chumakov

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

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  6. Non-lytic spread of poliovirus requires the nonstructural protein 3CD.bioRxiv : the preprint server for biology · 2024
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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

10 authors at 5 institutions in 1 country.

Zhaochun ChenLaboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.
Elizabeth R Fischer
Diana Kouiavskaia
Bryan T Hansen
Steven J Ludtke
Bella Bidzhieva
Michelle Makiya
Liane Agulto
Robert H Purcell
Konstantin Chumakov
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · USUnited States Food and Drug Administration · USBaylor College of Medicine · USCenter for Biologics Evaluation and Research · US

Funding

Infectious Diseases Research Technologies Core - RMLZICAI001052 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI CHERRY, JAMES · 2009 to 2025
$133.3M
SUPPORT AND DEVELOPMENT OF EMAN FOR ELECTRON MICROSCOPY IMAGE PROCESSINGR01GM080139 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LUDTKE, STEVEN J · 2006 to 2022
$5.4M
Intramural NIH HHSNIGMS NIH HHS R01 GM080139NIGMS NIH HHS R01-GM080139
6 · The paper itself

Abstract

Most structural information about poliovirus interaction with neutralizing antibodies was obtained in the 1980s in studies of mouse monoclonal antibodies. Recently we have isolated a number of human/chimpanzee anti-poliovirus antibodies and demonstrated that one of them, MAb A12, could neutralize polioviruses of both serotypes 1 and 2. This communication presents data on isolation of an additional cross-neutralizing antibody (F12) and identification of a previously unknown epitope on the surface of poliovirus virions. Epitope mapping was performed by sequencing of antibody-resistant mutants and by cryo-EM of complexes of virions with Fab fragments. The results have demonstrated that both cross-neutralizing antibodies bind the site located at the bottom of the canyon surrounding the fivefold axis of symmetry that was previously shown to interact with cellular poliovirus receptor CD155. However, the same antibody binds to serotypes 1 and 2 through different specific interactions. It was also shown to interact with type 3 poliovirus, albeit with about 10-fold lower affinity, insufficient for effective neutralization. Antibody interaction with the binding site of the cellular receptor may explain its broad reactivity and suggest that further screening or antibody engineering could lead to a universal antibody capable of neutralizing all three serotypes of poliovirus.

Indexed as

Models, MolecularAntibodies, ViralAntibody SpecificityBase SequenceCapsidCell Surface Display TechniquesCross ReactionsCryoelectron MicroscopyDisease EradicationEnzyme-Linked Immunosorbent AssayHEK293 CellsHumansMolecular Sequence DataNeutralization TestsPoliovirusSequence Analysis, DNAAntibodies, Viralantiviral therapybroadly reactive antibodiespassive immunizationphage display

Identifiers

PMID24277851
PMCPMC3864303
OpenAlexW2080799466

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.