Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
8.3
4.0
Journals
Toxins
Special Issues
The Neutralization Mechanism and Immunological Studies of Botulinum Neurotoxin
share announcement

The Neutralization Mechanism and Immunological Studies of Botulinum Neurotoxin

A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Bacterial Toxins".

Deadline for manuscript submissions: 31 July 2026 | Viewed by 787

Special Issue Editors

Dr. Shauna Farr-Jones

E-Mail Website
Guest Editor
Department of Anesthesia, University of California, San Francisco, CA, USA
Interests: botulinum neurotoxin; bacterial toxins; recombinant antibodies; antibody engineering
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. James D. Marks

E-Mail Website
Guest Editor
Department of Anesthesia, University of California, San Francisco, CA, USA
Interests: botulinum neurotoxin; bacterial toxins; recombinant antibodies; antibody engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Botulinum neurotoxins (BoNTs) comprise a structurally and functionally diverse family of proteins whose extreme potency and serotype variability continue to motivate intensive investigation into their mechanisms of neutralization. This Special Issue of Toxins, titled “The Neutralization Mechanism and Immunological Studies of Botulinum Neurotoxin,” invites contributions that elucidate the structural, biochemical, and molecular determinants governing BoNT binding, internalization, enzymatic activity, and inhibition across multiple serotypes and subtypes. Topics of interest include structure–function analyses of toxin domains, epitope–paratope interactions, and conformational dynamics underlying neutralization, antibody- and non-antibody-based countermeasures, spanning diverse immunologic formats (e.g., monoclonal, oligoclonal, bispecific, polyclonal, and single-domain binders); and small-molecule or peptide inhibitors targeting receptor engagement, translocation, or metalloprotease activity. Studies on the mechanism of neutralization of BoNT for therapeutic use by anti-drug antibodies are also suitable for inclusion in this Special Issue. Studies integrating high-resolution structural methods, biophysical characterization, and functional neutralization assays are particularly encouraged, with the aim of advancing mechanistic insight and informing the rational design of next-generation BoNT therapeutics and countermeasures.

Dr. Shauna Farr-Jones
Prof. Dr. James D. Marks
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • botulinum neurotoxin antitoxin
  • mechanism of action
  • botulinum neurotoxin neutralization mechanism

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Published Papers (1 paper)

Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

17 pages, 2110 KB  
Article
Intradermal and Subcutaneous Botulinum Toxin Type A Injections Do Not Differ in the Induction of Neutralizing Antibody Formation
by Stefanie Honndorf, Jessica Moser and Klaus Fink
Toxins 2026, 18(6), 245; https://doi.org/10.3390/toxins18060245 - 27 May 2026
Viewed by 517
Abstract
The neurotoxin botulinum toxin type A (BoNT/A), produced by the bacteria Clostridium botulinum, is commonly injected intramuscularly (IM) for the management of chronic muscle hyperactivity, such as post-stroke spasticity. New indications such as peripheral neuropathic pain require alternative routes of BoNT/A administration, [...] Read more.
The neurotoxin botulinum toxin type A (BoNT/A), produced by the bacteria Clostridium botulinum, is commonly injected intramuscularly (IM) for the management of chronic muscle hyperactivity, such as post-stroke spasticity. New indications such as peripheral neuropathic pain require alternative routes of BoNT/A administration, such as subcutaneous (SC) or intradermal (ID). While IM BoNT/A injections may elicit anti-drug-antibodies (ADAs), their occurrence following SC or ID administration is unknown. Therefore, we investigated whether repeated SC or ID injections of 150 kDa BoNT/A can elicit ADAs in a dose-dependent manner, and whether these differ depending upon the route of administration. Mice were injected 5 times ID or SC with 150 kDa BoNT/A or, for higher doses, inactive mutant BoNT/A (DRBoNT/A) or inactivated toxoid (IA-BoNT/A). Total ADAs were analyzed by an immunoassay and the subgroup of neutralizing ADAs by an in vivo digit abduction score (DAS) assay following a challenge of 0.6 U BoNT/A IM. DRBoNT/A and IA-BoNT/A injections elicit ADAs (22.7 U/mL vs. 460.5 U/mL for ID; 4.7 U/mL vs. 339.4 U/mL for SC), while therapeutic doses of 150 kDa BoNT/A do not. Whereas mice with repeated 150 kDa BoNT/A injections at therapeutic dose show an unrestricted DAS of 3.7 (ID) or 3.4 (SC), mice injected repeatedly with 1.8 µg/kg DRBoNT/A or 500 µg/kg IA-BoNT/A show only a minimal DAS of ≤0.7, indicating a high titer of neutralizing ADAs. No differences were observed between administration routes. Accordingly, repeated ID or SC injections of pure 150 kDa BoNT/A at therapeutic doses fail to induce ADA formation in mice. On the other hand, DRBoNT/A ID injections induce higher ADA concentrations than SC, but generate similar amounts of neutralizing ADAs. IA-BoNT/A injections induce ADAs and neutralizing ADAs similarly after ID and SC injections. ADA development at intermediate BoNT/A doses can be higher after ID injection, but does not lead to differences in neutralizing ADAs. Our data demonstrate that the antibody response to botulinum toxin depends predominantly on the protein load, and less on the administration route. Full article
(This article belongs to the Special Issue The Neutralization Mechanism and Immunological Studies of Botulinum Neurotoxin)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-1
Back to TopTop