Evidence map›Paper›PMID 27626446›Full record

ArticleToxins2016

Neutralization of Botulinum Neurotoxin Type E by a Humanized Antibody.

Yağmur Derman, Katja Selby, Sebastian Miethe, André Frenzel, Yvonne Liu, Christine Rasetti-Escargueil, Arnaud Avril, Thibaut Pelat, Remi Urbain, Alexandre Fontayne and 5 more

Open access · goldAbstract readComparative Study
In one paragraph

Article in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2023
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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

15 authors at 5 institutions in 4 countries.

Yağmur DermanDepartment of Food Hygiene and Environmental Health, Faculty of Veterinary Medicine, University of Helsinki, Helsinki 00014, Finland. yagmur.derman@helsinki.fi.
Katja SelbyDepartment of Food Hygiene and Environmental Health, Faculty of Veterinary Medicine, University of Helsinki, Helsinki 00014, Finland. katja.selby@helsinki.fi.
Sebastian MietheInstitut für Biochemie, Biotechnologie, und Bioinformatik, Technische Universität Braunschweig, Abteilung Biotechnologie, Braunschweig 38106, Germany. s.miethe@tu-braunschweig.de.
André FrenzelInstitut für Biochemie, Biotechnologie, und Bioinformatik, Technische Universität Braunschweig, Abteilung Biotechnologie, Braunschweig 38106, Germany. andre.frenzel@tu-bs.de.
Yvonne LiuDivision of Bacteriology, National Institute for Biological Standards and Control (NIBSC), A centre of Medicine and Healthcare products Regulatory Agency, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, UK. yvonne.liu@nibsc.org.
Christine Rasetti-EscargueilDivision of Bacteriology, National Institute for Biological Standards and Control (NIBSC), A centre of Medicine and Healthcare products Regulatory Agency, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, UK. christine.escargueil@laposte.net.
Arnaud AvrilInstitut de Recherche Biomédicale des Armées (IRBA), Département des Maladies Infectieuses, Unité biothérapies anti-infectieuses et immunité, Brétigny-sur-Orge, 1 place du Général Valérie André 91220, France. arnaud.avril@irba.fr.
Thibaut PelatInstitut de Recherche Biomédicale des Armées (IRBA), Département des Maladies Infectieuses, Unité biothérapies anti-infectieuses et immunité, Brétigny-sur-Orge, 1 place du Général Valérie André 91220, France. thibaut.pelat@biotem.fr.
Remi UrbainLFB Biotechnologies, Therapeutic Innovation Department, 59 Rue de Trévise, Lille Cedex BP 62006-59011, France. remi.urbain@ecdysispharma.com.
Alexandre FontayneLFB Biotechnologies, Therapeutic Innovation Department, 59 Rue de Trévise, Lille Cedex BP 62006-59011, France. fontaynea@lfb.fr.
Philippe ThullierInstitut de Recherche Biomédicale des Armées (IRBA), Département des Maladies Infectieuses, Unité biothérapies anti-infectieuses et immunité, Brétigny-sur-Orge, 1 place du Général Valérie André 91220, France. pthullier@yahoo.com.
Dorothea SesardicDivision of Bacteriology, National Institute for Biological Standards and Control (NIBSC), A centre of Medicine and Healthcare products Regulatory Agency, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, UK. Thea.Sesardic@nibsc.org.
Miia LindströmDepartment of Food Hygiene and Environmental Health, Faculty of Veterinary Medicine, University of Helsinki, Helsinki 00014, Finland. miia.lindstrom@helsinki.fi.
Michael HustInstitut für Biochemie, Biotechnologie, und Bioinformatik, Technische Universität Braunschweig, Abteilung Biotechnologie, Braunschweig 38106, Germany. m.hust@tu-bs.de.
Hannu KorkealaDepartment of Food Hygiene and Environmental Health, Faculty of Veterinary Medicine, University of Helsinki, Helsinki 00014, Finland. hannu.korkeala@helsinki.fi.
University of Helsinki · FINational Institute for Biological Standards and Control · GBTechnische Universität Braunschweig · DEEurasanté · FRLFB (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Botulinum neurotoxins (BoNTs) cause botulism and are the deadliest naturally-occurring substances known to humans. BoNTs have been classified as one of the category A agents by the Centers for Disease Control and Prevention, indicating their potential use as bioweapons. To counter bio-threat and naturally-occurring botulism cases, well-tolerated antibodies by humans that neutralize BoNTs are relevant. In our previous work, we showed the neutralizing potential of macaque (Macaca fascicularis)-derived scFv-Fc (scFv-Fc ELC18) by in vitro endopeptidase immunoassay and ex vivo mouse phrenic nerve-hemidiaphragm assay by targeting the light chain of the botulinum neurotoxin type E (BoNT/E). In the present study, we germline-humanized scFv-Fc ELC18 into a full IgG hu8ELC18 to increase its immunotolerance by humans. We demonstrated the protection and prophylaxis capacity of hu8ELC18 against BoNT/E in a mouse model. A concentration of 2.5 ng/mouse of hu8ELC18 protected against 5 mouse lethal dose (MLD) in a mouse protection assay and complete neutralization of 1 LD50 of pure BoNT/E toxin was achieved with 8 ng of hu8ELC18 in mouse paralysis assay. Furthermore, hu8ELC18 protected mice from 5 MLD if injected up to 14 days prior to intraperitoneal BoNT/E administration. This newly-developed humanized IgG is expected to have high tolerance in humans.

Indexed as

AnimalsAntibodies, Monoclonal, HumanizedAntibodies, NeutralizingAntidotesAntitoxinsBotulinum ToxinsBotulismClostridium botulinumDisease Models, AnimalFemaleMiceSingle-Chain AntibodiesAntibodies, Monoclonal, HumanizedAntibodies, NeutralizingAntidotesAntitoxinsBotulinum Toxinsbotulinum toxin type ESingle-Chain Antibodiesantibodybotulinum neurotoxin type Ebotulism

Identifiers

PMID27626446
PMCPMC5037483
OpenAlexW2519988515

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.