Evidence map›Paper›PMID 32987745›Full record

ArticleToxins2020

Camelid VHH Antibodies that Neutralize Botulinum Neurotoxin Serotype E Intoxication or Protease Function.

Jacqueline M Tremblay, Edwin Vazquez-Cintron, Kwok-Ho Lam, Jean Mukherjee, Daniela Bedenice, Celinia A Ondeck, Matthieu T Conroy, Skylar M L Bodt, Brittany M Winner, Robert P Webb and 4 more

Open access · goldAbstract read
In one paragraph

Article in Toxins, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Botulinum neurotoxin: from molecular pathogenesis to emerging countermeasures.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2026
    Review
  3. Article
  4. Article
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  8. Review
  9. Review
  10. The Degradation of Botulinum Neurotoxin Light Chains Using PROTACs.International journal of molecular sciences · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Structure-guided design of a potentFrontiers in microbiology · 2023
    Article
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  17. Review
  18. Article
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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

14 authors at 4 institutions in 1 country.

Jacqueline M TremblayDepartment of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA.
Edwin Vazquez-CintronThe United States Army Medical Research Institute of Chemical Defense, Fort Detrick, MD 21010, USA.ORCID 0000-0002-4397-3713
Kwok-Ho LamDepartment of Physiology & Biophysics, University of California, Irvine, CA 92697-4560, USA.
Jean MukherjeeDepartment of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA.
Daniela BedeniceDepartment of Clinical Sciences, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA.
Celinia A OndeckThe United States Army Medical Research Institute of Chemical Defense, Fort Detrick, MD 21010, USA.
Matthieu T ConroyThe United States Army Medical Research Institute of Chemical Defense, Fort Detrick, MD 21010, USA.
Skylar M L BodtThe United States Army Medical Research Institute of Chemical Defense, Fort Detrick, MD 21010, USA.ORCID 0000-0002-5794-6927
Brittany M WinnerThe United States Army Medical Research Institute of Chemical Defense, Fort Detrick, MD 21010, USA.
Robert P WebbBacteriology Division, U.S. Army Medical Research Institute of Infectious Diseases, Ft. Detrick, MD 21702-5011, USA.ORCID 0000-0001-8253-8979
Konstantin IchtchenkoDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA.ORCID 0000-0002-2198-1325
Rongsheng JinDepartment of Physiology & Biophysics, University of California, Irvine, CA 92697-4560, USA.ORCID 0000-0003-0348-7363
Patrick M McNuttThe United States Army Medical Research Institute of Chemical Defense, Fort Detrick, MD 21010, USA.ORCID 0000-0002-5703-4565
Charles B ShoemakerDepartment of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University, North Grafton, MA 01536, USA.ORCID 0000-0001-9738-1361
United States Army Medical Research Institute of Infectious Diseases · USTufts University · USUniversity of California, Irvine · USNew York University · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI CLARDY, JON · 2003 to 2013
$113.7M
Novel therapeutic approaches to treatment of botulinum neurotoxin poisoning.R01AI093504 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Konstantin Ichtchenko · 2011 to 2026
$13.9M
A platform for therapeutic agents that promote rapid recovery from botulismR01AI093467 · NIAID · TUFTS UNIVERSITY BOSTON · PI OYLER, GEORGE A., SHOEMAKER, CHARLES BIX · 2011 to 2015
$4.1M
Novel therapeutic approaches to treatment of botulinum neurotoxin poisoning.U01AI093504 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ICHTCHENKO, KONSTANTIN · 2019 to 2021
$3.4M
Molecular mechanisms of botulinum neurotoxin neutralizationR01AI125704 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI JIN, RONGSHENG, SHOEMAKER, CHARLES BIX · 2016 to 2020
$3.0M
Division of Intramural Research, National Institute of Allergy and Infectious Diseases R01AI093467Division of Intramural Research, National Institute of Allergy and Infectious Diseases R01AI125704Division of Intramural Research, National Institute of Allergy and Infectious Diseases RAI093504Division of Intramural Research, National Institute of Allergy and Infectious Diseases U54-AI057159NIAID NIH HHS R01 AI093504NIAID NIH HHS R01 AI125704NIAID NIH HHS U01 AI093504
6 · The paper itself

Abstract

Botulinum neurotoxin (BoNT) serotype E is one of three serotypes that cause the preponderance of human botulism cases and is a Tier 1 Select Agent. BoNT/E is unusual among BoNT serotypes for its rapid onset and short duration of intoxication. Here we report two large panels of unique, unrelated camelid single-domain antibodies (VHHs) that were selected for their ability to bind to BoNT/E holotoxin and/or to the BoNT/E light chain protease domain (LC/E). The 19 VHHs which bind to BoNT/E were characterized for their subunit specificity and 8 VHHs displayed the ability to neutralize BoNT/E intoxication of neurons. Heterodimer antitoxins consisting of two BoNT/E-neutralizing VHHs, including one heterodimer designed using structural information for simultaneous binding, were shown to protect mice against co-administered toxin challenges of up to 500 MIPLD

Indexed as

Peptide HydrolasesAnimalsAntibodies, NeutralizingAntibody SpecificityBinding Sites, AntibodyBotulinum ToxinsBotulismCamelids, New WorldCells, CulturedDisease Models, AnimalImmunizationMaleMiceNeuronsProtease InhibitorsRatsAntibodies, NeutralizingBotulinum Toxinsbotulinum toxin type EPeptide HydrolasesProtease InhibitorsSingle-Domain Antibodiesantitoxinbotulinum neurotoxinbotulismneutralizationproteasesingle-domain antibodytoxinVHH

Identifiers

PMID32987745
PMCPMC7598594
OpenAlexW3088928121

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.