scholarly journals Botulinum Toxin Complex: A Delivery Vehicle of Botulinum Neurotoxin Traveling Digestive Tract

10.5772/46023 ◽  
2012 ◽  
Author(s):  
Yoshimasa Sagane ◽  
Ken Inui ◽  
Shin-Ichiro Miyashita ◽  
Keita Miyata ◽  
Tomonori Suzuki ◽  
...  
Keyword(s):  
Botulinum Toxin ◽  
Digestive Tract ◽  
Botulinum Neurotoxin ◽  
Delivery Vehicle ◽  
Toxin Complex

scholarly journals Primary Cultures of Embryonic Chicken Neurons for Sensitive Cell-Based Assay of Botulinum Neurotoxin: Implications for Therapeutic Discovery

2007 ◽  
Vol 12 (3) ◽  
pp. 370-377 ◽  
Author(s):  
Andrea M. Stahl ◽  
Gordon Ruthel ◽  
Edna Torres-Melendez ◽  
Tara A. Kenny ◽  
Rekha G. Panchal ◽  
...  
Keyword(s):  
Nervous System ◽  
Botulinum Toxin ◽  
Neutralizing Antibodies ◽  
Botulinum Neurotoxin ◽  
Potent Inhibitor ◽  
Primary Cultures ◽  
Embryonic Chick ◽  
Sensitive Cell ◽  
Botulinum Neurotoxin A ◽  
Therapeutic Compounds

Botulinum toxin is an exceedingly potent inhibitor of neurotransmission across the neuromuscular junction, causing flaccid paralysis and death. The potential for misuse of this deadly poison as a bioweapon has added a greater urgency to the search for effective therapeutics. The development of sensitive and efficient cell-based assays for the evaluation of toxin antagonists is crucial to the rapid and successful identification of therapeutic compounds. The authors evaluated the sensitivity of primary cultures from 4 distinct regions of the embryonic chick nervous system to botulinum neurotoxin A (BoNT/A) cleavage of synaptosomal-associated protein of 25 kD (SNAP-25). Although differences in sensitivity were apparent, SNAP-25 cleavage was detectable in neuronal cells from each of the 4 regions within 3 h at BoNT/A concentrations of 1 nM or lower. Co-incubation of chick neurons with BoNT/A and toxin-neutralizing antibodies inhibited SNAP-25 cleavage, demonstrating the utility of these cultures for the assay of BoNT/A antagonists. ( Journal of Biomolecular Screening 2007:370-377)

Crystal structures of botulinum neurotoxin X and Weissella oryzae botulinum toxin–like catalytic domains

Toxicon ◽  
2021 ◽  
Vol 190 ◽  
pp. S42
Author(s):  
Sara Košenina ◽  
Geoffrey Masuyer ◽  
Sicai Zhang ◽  
Min Dong ◽  
Pål Stenmark
Keyword(s):  
Botulinum Toxin ◽  
Crystal Structures ◽  
Botulinum Neurotoxin ◽  
Catalytic Domains

scholarly journals Looking for the X Factor in Bacterial Pathogenesis: Association of orfX-p47 Gene Clusters with Toxin Genes in Clostridial and Non-Clostridial Bacterial Species

Toxins ◽  
2019 ◽  
Vol 12 (1) ◽  
pp. 19 ◽  
Author(s):  
Maria B. Nowakowska ◽  
François P. Douillard ◽  
Miia Lindström
Keyword(s):  
Gene Cluster ◽  
In Silico ◽  
Botulinum Neurotoxin ◽  
Bacterial Species ◽  
Gene Clusters ◽  
Bacterial Pathogenesis ◽  
Toxin Gene ◽  
Toxin Complex ◽  
Analytical Tools ◽  
Bacillus Isolate

The botulinum neurotoxin (BoNT) has been extensively researched over the years in regard to its structure, mode of action, and applications. Nevertheless, the biological roles of four proteins encoded from a number of BoNT gene clusters, i.e., OrfX1-3 and P47, are unknown. Here, we investigated the diversity of orfX-p47 gene clusters using in silico analytical tools. We show that the orfX-p47 cluster was not only present in the genomes of BoNT-producing bacteria but also in a substantially wider range of bacterial species across the bacterial phylogenetic tree. Remarkably, the orfX-p47 cluster was consistently located in proximity to genes coding for various toxins, suggesting that OrfX1-3 and P47 may have a conserved function related to toxinogenesis and/or pathogenesis, regardless of the toxin produced by the bacterium. Our work also led to the identification of a putative novel BoNT-like toxin gene cluster in a Bacillus isolate. This gene cluster shares striking similarities to the BoNT cluster, encoding a bont/ntnh-like gene and orfX-p47, but also differs from it markedly, displaying additional genes putatively encoding the components of a polymorphic ABC toxin complex. These findings provide novel insights into the biological roles of OrfX1, OrfX2, OrfX3, and P47 in toxinogenesis and pathogenesis of BoNT-producing and non-producing bacteria.

Expression and stability of the nontoxic component of the botulinum toxin complex

2009 ◽  
Vol 384 (1) ◽  
pp. 126-130 ◽  
Author(s):  
Keita Miyata ◽  
Tohru Yoneyama ◽  
Tomonori Suzuki ◽  
Hirokazu Kouguchi ◽  
Ken Inui ◽  
...  
Keyword(s):  
Botulinum Toxin ◽  
Toxin Complex

scholarly journals Role of nontoxic components of serotype D botulinum toxin complex in permeation through a Caco-2 cell monolayer, a model for intestinal epithelium

2007 ◽  
Vol 49 (3) ◽  
pp. 346-352 ◽  
Author(s):  
Koichi Niwa ◽  
Kumiko Koyama ◽  
Shin-ichi Inoue ◽  
Tomonori Suzuki ◽  
Kimiko Hasegawa ◽  
...  
Keyword(s):  
Botulinum Toxin ◽  
Intestinal Epithelium ◽  
Cell Monolayer ◽  
Toxin Complex

scholarly journals New trends in botulinum toxin use in dermatology

2018 ◽  
pp. 277-282 ◽  
Author(s):  
Stefania Guida ◽  
Francesca Farnetani ◽  
Steven P. Nisticò ◽  
Caterina Giorgio Mariarosaria ◽  
Graziella Babino ◽  
...  
Keyword(s):  
Botulinum Toxin ◽  
Botulinum Neurotoxin ◽  
Current Knowledge ◽  
Hypertrophic Scars ◽  
Skin Disorders ◽  
Facial Flushing ◽  
Cutaneous Lesions ◽  
Raynaud Phenomenon ◽  
Skin Conditions ◽  
Review Current

Background: Recent studies have highlighted new botulinum neurotoxin (BoNT) applications in the field of dermatology. Objective: To review current knowledge of BoNT use in dermatology. Methods: The literature of the last 5 years has been reviewed. Results: We describe interesting protocols of BoNT treatment for hyperhidrosis (HH), hypertrophic scars and keloids, Raynaud phenomenon, facial flushing, oily skin, psoriasis, Hailey-Hailey disease, and cutaneous lesions like painful lesions and periorbital syringomas. Conclusions: Several skin conditions eligible for BoNT treatment have been described. After the wide application for HH treatment, scars as well as vascular and inflammatory skin disorders, oily skin and cutaneous lesions represent fields of application of BoNT.

scholarly journals Botulinum Toxin Use in the Lower Urinary Tract

2007 ◽  
Vol 7 ◽  
pp. 808-817
Author(s):  
Shelby N. Morrisroe ◽  
Michael B. Chancellor
Keyword(s):  
Botulinum Toxin ◽  
Urinary Tract ◽  
Overactive Bladder ◽  
Lower Urinary Tract ◽  
Botulinum Neurotoxin ◽  
Botulinum Toxins ◽  
Muscle Paralysis ◽  
Botulinum Neurotoxin A ◽  
Beneficial Effects ◽  
Lower Urinary

Botulinum toxins are well known for their ability to disrupt neurotransmission and cause muscle paralysis. Recently, urologists have discovered their beneficial effects in patients with neurogenic and overactive bladder conditions. This review is intended to provide a quick overview for urologists of the structure, function, and clinical uses of botulinum neurotoxin A in the lower urinary tract.

Identification of the interaction region between hemagglutinin components of the botulinum toxin complex

2014 ◽  
Vol 65 ◽  
pp. 284-288 ◽  
Author(s):  
Tomonori Suzuki ◽  
Shin-Ichiro Miyashita ◽  
Shintaro Hayashi ◽  
Keita Miyata ◽  
Ken Inui ◽  
...  
Keyword(s):  
Botulinum Toxin ◽  
Interaction Region ◽  
Toxin Complex

scholarly journals Holotoxin Activity of Botulinum Neurotoxin Subtype A4 Originating from a Nontoxigenic Clostridium botulinum Expression System

2014 ◽  
Vol 80 (23) ◽  
pp. 7415-7422 ◽  
Author(s):  
Marite Bradshaw ◽  
William H. Tepp ◽  
Regina C. M. Whitemarsh ◽  
Sabine Pellett ◽  
Eric A. Johnson
Keyword(s):  
Clostridium Botulinum ◽  
Botulinum Neurotoxin ◽  
Expression System ◽  
Single Amino Acid ◽  
Content Type ◽  
Expression Host ◽  
Toxin Complex ◽  
Human Neuronal Cells

ABSTRACTClostridium botulinumsubtype A4 neurotoxin (BoNT/A4) is naturally expressed in the dual-toxin-producingC. botulinumstrain 657Ba at 100× lower titers than BoNT/B. In this study, we describe purification of recombinant BoNT/A4 (rBoNT/A4) expressed in a nonsporulating and nontoxigenicC. botulinumexpression host strain. The rBoNT/A4 copurified with nontoxic toxin complex components provided intransby the expression host and was proteolytically cleaved to the active dichain form. Activity of the recombinant BoNT/A4 in mice and in human neuronal cells was about 1,000-fold lower than that of BoNT/A1, and the recombinant BoNT/A4 was effectively neutralized by botulism heptavalent antitoxin. A previous report using recombinant truncated BoNT/A4 light chain (LC) expressed inEscherichia colihas indicated reduced stability and activity of BoNT/A4 LC compared to BoNT/A1 LC, which was surmounted by introduction of a single-amino-acid substitution, I264R. In order to determine whether this mutation would also affect the holotoxin activity of BoNT/A4, a recombinant full-length BoNT/A4 carrying this mutation as well as a second mutation predicted to increase solubility (L260F) was produced in the clostridial expression system. Comparative analyses of thein vitro, cellular, andin vivoactivities of rBoNT/A4 and rBoNT/A4-L260F I264R showed 1,000-fold-lower activity than BoNT/A1 in both the mutated and nonmutated BoNT/A4. This indicates that these mutations do not alter the activity of BoNT/A4 holotoxin. In summary, a recombinant BoNT from a dual-toxin-producing strain was expressed and purified in an endogenous clostridial expression system, allowing analysis of this toxin.

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