For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
18
views
67
references
 Top references
cited by
47
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      451
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      Pharmaceutical, Biological, and Clinical Properties of Botulinum Neurotoxin Type A Products

      research-article
      Author(s):
      Publication date (Electronic):
      Journal: Drugs in R&D
      Publisher: Springer International Publishing

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Botulinum neurotoxin injections are a valuable treatment modality for many therapeutic indications and have revolutionized the field of aesthetic medicine so that they are the leading cosmetic procedure performed worldwide. Studies show that onabotulinumtoxinA, abobotulinumtoxinA, and incobotulinumtoxinA are comparable in terms of clinical efficacy. Differences between the products relate to the botulinum neurotoxin complexes, specific biological potency, and their immunogenicity. Protein complex size and molecular weight have no effect on biological activity, stability, distribution, or side effect profile. Complexing proteins and inactive toxin (toxoid) content increase the risk of neutralizing antibody formation, which can cause secondary treatment failure, particularly in chronic disorders that require frequent injections and long-term treatment. These attributes could lead to differences in therapeutic outcomes, and, given the widespread aesthetic use of these three neurotoxin products, physicians should be aware of how they differ to ensure their safe and effective use.

          Related collections

          Most cited references67

          • Record: found
          • Abstract: found
          • Article: not found

          History of lectins: from hemagglutinins to biological recognition molecules.

          Nathan Sharon, Halina Lis (2004)
          The occurrence in nature of erythrocyte-agglutinating proteins has been known since the turn of the 19th century. By the 1960s it became apparent that such proteins also agglutinate other types of cells, and that many of them are sugar-specific. These cell-agglutinating and sugar-specific proteins have been named lectins. Although shown to occur widely in plants and to some extent also in invertebrates, very few lectins had been isolated until the early 1970s, and they had attracted little attention. This attitude changed with the demonstration that lectins are extremely useful tools for the investigation of carbohydrates on cell surfaces, in particular of the changes that the latter undergo in malignancy, as well as for the isolation and characterization of glycoproteins. In subsequent years numerous lectins have been isolated from plants as well as from microorganisms and animals, and during the past two decades the structures of hundreds of them have been established. Concurrently, it was shown that lectins function as recognition molecules in cell-molecule and cell-cell interactions in a variety of biological systems. Here we present a brief account of 100-plus years of lectin research and show how these proteins have become the focus of intense interest for biologists and in particular for the glycobiologists among them.
          Article 0 comments Cited 180 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.

            Shenyan Gu, N Shoemaker, Jasmin Strotmeier … (2012)
            Botulinum neurotoxins (BoNTs) are highly poisonous substances that are also effective medicines. Accidental BoNT poisoning often occurs through ingestion of Clostridium botulinum-contaminated food. Here, we present the crystal structure of a BoNT in complex with a clostridial nontoxic nonhemagglutinin (NTNHA) protein at 2.7 angstroms. Biochemical and functional studies show that NTNHA provides large and multivalent binding interfaces to protect BoNT from gastrointestinal degradation. Moreover, the structure highlights key residues in BoNT that regulate complex assembly in a pH-dependent manner. Collectively, our findings define the molecular mechanisms by which NTNHA shields BoNT in the hostile gastrointestinal environment and releases it upon entry into the circulation. These results will assist in the design of small molecules for inhibiting oral BoNT intoxication and of delivery vehicles for oral administration of biologics.
            Article 0 comments Cited 64 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Content of Botulinum Neurotoxin in Botox®/Vistabel®, Dysport®/Azzalure®, and Xeomin®/Bocouture®

              Jürgen Frevert (2010)
              Background: Botulinum neurotoxin type A (BoNT/A) is the active substance in preparations used for the highly effective treatment of neurologic disorders such as cervical dystonia, blepharospasm, or spasticity, as well as other indications such as axillary and palmar hyperhidrosis, and urologic disorders. Objective: To determine the amount of BoNT/A protein present in pharmaceutical preparations of Botox®, Dysport®, and Xeomin®, which are identical with Vistabel®, Azzalure®, and Bocouture®, respectively. Methods: Rabbit and guinea pig antibodies raised against the 150kD BoNT/A neurotoxin purified from Clostridium botulinum type A, strain ATCC 3502 (‘Hall strain’), were used in a sensitive sandwich ELISA to determine the overall mean concentration of the 150kD neurotoxin present in four batches of Botox® (C2344C3, C2384C3, C2419, and C2385), two batches of Dysport® (678F and 689X) and three batches of Xeomin® (61111, 70604, and 81 208). The specific neurotoxin potency, defined as the potency or biologic activity (units) per mass of neurotoxin protein (ng), was calculated based on the overall mean concentration of BoNT/A neurotoxin. Results: Overall, the mean concentration of BoNT/A neurotoxin in Botox® was 0.73 ng per 100 unit vial (coefficient of variation [CV] = 3.5%), 3.24 ng per 500 unit vial of Dysport®, corresponding to 0.65 ng in 100 units (CV = 11.4%), and 0.44 ng per 100 unit vial of Xeomin® (CV = 1.9%). The specific potency of the 150kD BoNT/A neurotoxin was calculated as 137 units/ng for Botox®, 154 units/ng Dysport®, and 227 units/ng Xeomin®. Conclusions: The current study has shown that of the three products, Xeomin® contains the highest specific neurotoxin activity, followed by Dysport®, with Botox® having the lowest specific activity. This result suggests that Xeomin® contains only active neurotoxin in contrast with Botox®, which is likely to contain additional denatured/inactive neurotoxin.
              Article 0 comments Cited 57 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Jürgen Frevert: 49-331-2300116 , juergen.Frevert@merz.de
                Journal
                Journal ID (nlm-ta): Drugs R D
                Journal ID (iso-abbrev): Drugs R D
                Title: Drugs in R&D
                Publisher: Springer International Publishing (Cham )
                ISSN (Print): 1174-5886
                ISSN (Electronic): 1179-6901
                Publication date (Electronic): 6 January 2015
                Publication date PMC-release: 6 January 2015
                Publication date (Print): March 2015
                Volume: 15
                Issue: 1
                Pages: 1-9
                Affiliations
                Head of Botulinum Toxin Research, Merz Pharmaceuticals GmbH, Hermannswerder 15, 14473 Potsdam, Germany
                Article
                Publisher ID: 77
                DOI: 10.1007/s40268-014-0077-1
                PMC ID: 4359186
                PubMed ID: 25559581
                SO-VID: 2c84d72f-fe51-4f7d-ac0d-94b046655837
                Copyright © © The Author(s) 2014
                License:

                Open AccessThis article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.

                History
                Categories
                Subject: Current Opinion
                Custom metadata
                issue-copyright-statement © Springer International Publishing Switzerland 2015

                Data availability:

                Comments

                Comment on this article

                scite_

                Similar content451

                See all similar

                Cited by47

                See all cited by

                Most referenced authors456

                See all reference authors