Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells.

Toxins - 27 Sept 2020

Lam Kwok-Ho, Perry Kay, Shoemaker Charles B, Jin Rongsheng

Abstract excerpt

Botulinum neurotoxin serotype E (BoNT/E) is one of the major causes of human botulism, which is a life-threatening disease caused by flaccid paralysis of muscles. After receptor-mediated toxin internalization into motor neurons, the translocation domain (HN) of BoNT/E transforms into a protein channel upon vesicle acidification in endosomes and delivers its protease domain (LC) across membrane to enter the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antibodies, Neutralizing
Share to Antibody Specificity
Share to Biological Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Botulinum Toxins

Share to Epitopes

Share to Host-Pathogen Interactions

Share to Membranes, Artificial

Share to Single-Domain Antibodies

Source

Open in PubMed Open full text

Identifiers

PMID: 32992561
DOI: 10.3390/toxins12100616
PMCID: PMC7599855

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells.PMID 32992561Read ↗

Probing the structure and function of the protease domain of botulinum neurotoxins using single-domain antibodiesSemantic proximity Read ↗

Structural Insights into Rational Design of Single-Domain Antibody-Based Antitoxins against Botulinum NeurotoxinsSemantic proximity Read ↗

A Comprehensive Structural Analysis of Clostridium botulinum Neurotoxin A Cell-Binding Domain from Different SubtypesSemantic proximity Read ↗

New Engineered-Chimeric Botulinum Neurotoxin Mutant Acts as an Effective Bivalent Vaccine Against Botulinum Neurotoxin Serotype A and E.Semantic proximity Read ↗

Fully Human Monoclonal Antibodies Effectively Neutralizing Botulinum Neurotoxin Serotype BSemantic proximity Read ↗

The Light Chain Defines the Duration of Action of Botulinum Toxin Serotype A SubtypesSemantic proximity Read ↗

Botulinum Toxin: A Comprehensive Review of Its Molecular Architecture and Mechanistic ActionSemantic proximity Read ↗

Characterization of a membrane binding loop leads to engineering botulinum neurotoxin B with improved therapeutic efficacy.Semantic proximity Read ↗

Light Chain Diversity among the Botulinum NeurotoxinsSemantic proximity Read ↗

Challenges in searching for therapeutics against Botulinum NeurotoxinsSemantic proximity Read ↗

Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions.Semantic proximity Read ↗

Embracing the Versatility of Botulinum Neurotoxins in Conventional and New Therapeutic ApplicationsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.