Relevant bibliographies by topics / Botulinum neurotoxin inactivation

Academic literature on the topic 'Botulinum neurotoxin inactivation'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Botulinum neurotoxin inactivation"

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Zhang, Zhen, Elias Dahlsten, Hannu Korkeala, and Miia Lindström. "Positive Regulation of Botulinum Neurotoxin Gene Expression by CodY in Clostridium botulinum ATCC 3502." Applied and Environmental Microbiology 80, no. 24 (October 3, 2014): 7651–58. http://dx.doi.org/10.1128/aem.02838-14.

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ABSTRACTBotulinum neurotoxin, produced mainly by the spore-forming bacteriumClostridium botulinum, is the most poisonous biological substance known. Here, we show that CodY, a global regulator conserved in low-G+C Gram-positive bacteria, positively regulates the botulinum neurotoxin gene expression. Inactivation ofcodYresulted in decreased expression ofbotA, encoding the neurotoxin, as well as in reduced neurotoxin synthesis. Complementation of thecodYmutation intransrescued neurotoxin synthesis, and overexpression ofcodYintranscaused elevated neurotoxin production. Recombinant CodY was found to bind to a 30-bp region containing thebotAtranscription start site, suggesting regulation of the neurotoxin gene transcription through direct interaction. GTP enhanced the binding affinity of CodY to thebotApromoter, suggesting that CodY-dependent neurotoxin regulation is associated with nutritional status.
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SKINNER, GUY E., GREGORY J. FLEISCHMAN, FRAN BALSTER, KARL REINEKE, N. RUKMA REDDY, and JOHN W. LARKIN. "Effect of Fill Temperature on Clostridium botulinum Type A Toxin Activity during the Hot Filling of Juice Bottles." Journal of Food Protection 78, no. 8 (August 1, 2015): 1506–11. http://dx.doi.org/10.4315/0362-028x.jfp-14-378.

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The potential threat of terrorist attacks against the United States food supply using neurotoxin produced by Clostridium botulinum (BoNT) has resulted in the need for studying the effect of various food process operations on the bioavailability of this toxin. The objective of this study was to evaluate C. botulinum type A neurotoxin bioavailability after a simulated hot fill juice bottling operation. C. botulinum type A acid mud toxin (∼106 mouse lethal dose [MLD50]/ml) was deposited into juice bottles at an experimentally determined fastest cooling spot. Bottles (12 or 20 oz [355 and 592 ml]) were filled with either apple juice or an orange drink, at 80 or 85°C, in either upright or inverted orientations. Toxicity of the juice was evaluated as a function of holding time (1 to 2 min) by the mouse bioassay. The fastest cooling point in the upright orientation was determined to be at a bottle's bottom rim. In the inverted orientation, the fastest cooling point was in the bottle cap region. With respect to these two points, the upright bottle cooled faster than the inverted bottle, which was reflected in a higher inactivation of BoNT in the latter. For the orange drink (pH 2.9) toxicity was reduced by 0.5 × 106 MLD50/ml to a nondetectable level after 1 min in all bottle sizes, orientations, and temperatures as measured by the mouse bioassay. This indicates that there was at least a 0.5 × 106 MLD50/ml reduction in activity. Inactivation in apple juice (pH 4.0), to the same degree as in the orange drink, was found only for the inverted orientation at 85°C. Complete inactivation in apple juice for all conditions was found at a lower added toxin level of 0.25 × 105 MLD50/ml. In general, bottle inversion and filling at 85°C provided complete inactivation of BoNT to the 0.5 × 106 MLD50/ml level. All experiments resulted in the inactivation of 2.5 × 104 MLD50/ml of BoNT regardless of juice type, fill temperature, or bottle orientation and size.
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Weingart, Oliver G., Tanja Schreiber, Conny Mascher, Diana Pauly, Martin B. Dorner, Thomas F. H. Berger, Charlotte Egger, et al. "The Case of Botulinum Toxin in Milk: Experimental Data." Applied and Environmental Microbiology 76, no. 10 (April 2, 2010): 3293–300. http://dx.doi.org/10.1128/aem.02937-09.

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ABSTRACT Botulinum neurotoxin (BoNT) is the most toxic substance known to man and the causative agent of botulism. Due to its high toxicity and the availability of the producing organism Clostridium botulinum, BoNT is regarded as a potential biological warfare agent. Because of the mild pasteurization process, as well as rapid product distribution and consumption, the milk supply chain has long been considered a potential target of a bioterrorist attack. Since, to our knowledge, no empirical data on the inactivation of BoNT in milk during pasteurization are available at this time, we investigated the activities of BoNT type A (BoNT/A) and BoNT/B, as well as their respective complexes, during a laboratory-scale pasteurization process. When we monitored milk alkaline phosphatase activity, which is an industry-accepted parameter of successfully completed pasteurization, our method proved comparable to the industrial process. After heating raw milk spiked with a set amount of BoNT/A or BoNT/B or one of their respective complexes, the structural integrity of the toxin was determined by enzyme-linked immunosorbent assay (ELISA) and its functional activity by mouse bioassay. We demonstrated that standard pasteurization at 72°C for 15 s inactivates at least 99.99% of BoNT/A and BoNT/B and at least 99.5% of their respective complexes. Our results suggest that if BoNTs or their complexes were deliberately released into the milk supply chain, standard pasteurization conditions would reduce their activity much more dramatically than originally anticipated and thus lower the threat level of the widely discussed “BoNT in milk” scenario.
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Held, Daniel M., Amy C. Shurtleff, Scott Fields, Christopher Green, Julie Fong, Russell G. A. Jones, Dorothea Sesardic, Roland Buelow, and Rae Lyn Burke. "Vaccination of Rabbits with an Alkylated Toxoid Rapidly Elicits Potent Neutralizing Antibodies against Botulinum Neurotoxin Serotype B." Clinical and Vaccine Immunology 17, no. 6 (April 21, 2010): 930–36. http://dx.doi.org/10.1128/cvi.00493-09.

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ABSTRACT New Zealand White (NZW) rabbits were immunized with several different nontoxic botulinum neurotoxin serotype B (BoNT/B) preparations in an effort to optimize the production of a rapid and highly potent, effective neutralizing antibody response. The immunogens included a recombinant heavy chain (rHc) protein produced in Escherichia coli, a commercially available formaldehyde-inactivated toxoid, and an alkylated toxoid produced by urea-iodoacetamide inactivation of the purified active toxin. All three immunogens elicited an antibody response to BoNT/B, detected by enzyme-linked immunosorbent assay (ELISA) and by toxin neutralization assay, by the use of two distinct mouse toxin challenge models. The induction period and the ultimate potency of the observed immune response varied for each immunogen, and the ELISA titer was not reliably predictive of the potency of toxin neutralization. The kinetics of the BoNT/B-specific binding immune response were nearly identical for the formaldehyde toxoid and alkylated toxoid immunogens, but immunization with the alkylated toxoid generated an approximately 10-fold higher neutralization potency that endured throughout the study, and after just 49 days, each milliliter of serum was capable of neutralizing 107 50% lethal doses of the toxin. Overall, the immunization of rabbits with alkylated BoNT/B toxoid appears to have induced a neutralizing immune response more rapid and more potent than the responses generated by vaccination with formaldehyde toxoid or rHc preparations.
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Palan, Shilpa, Imran Mir, Nick Thorn Martin, Iwona Ziomkiewicz, and Matthias Ehebauer. "Non-Destructive Catalytic Inactivation of Novel Recombinant Botulinum Neurotoxin Type A Variants Facilitates Safe Mass Spectrometry Analysis, Outside of Containment." Toxicon 214 (July 2022): S45. http://dx.doi.org/10.1016/j.toxicon.2021.11.098.

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SHONE, Clifford C., Peter HAMBLETON, and Jack MELLING. "Inactivation of Clostridium botulinum type A neurotoxin by trypsin and purification of two tryptic fragments. Proteolytic action near the COOH-terminus of the heavy subunit destroys toxin-binding activity." European Journal of Biochemistry 151, no. 1 (August 1985): 75–82. http://dx.doi.org/10.1111/j.1432-1033.1985.tb09070.x.

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Chapeton-Montes, Diana, Lucile Plourde, Cecile Deneve, Dominique Garnier, Fabien Barbirato, Vincent Colombié, Sandy Demay, et al. "Tetanus Toxin Synthesis is Under the Control of A Complex Network of Regulatory Genes in Clostridium tetani." Toxins 12, no. 5 (May 15, 2020): 328. http://dx.doi.org/10.3390/toxins12050328.

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Clostridium tetani produces a potent neurotoxin, the tetanus toxin (TeNT), which is responsible for an often-fatal neurological disease (tetanus) characterized by spastic paralysis. Prevention is efficiently acquired by vaccination with the TeNT toxoid, which is obtained by C. tetani fermentation and subsequent purification and chemical inactivation. C. tetani synthesizes TeNT in a regulated manner. Indeed, the TeNT gene (tent) is mainly expressed in the late exponential and early stationary growth phases. The gene tetR (tetanus regulatory gene), located immediately upstream of tent, encodes an alternative sigma factor which was previously identified as a positive regulator of tent. In addition, the genome of C. tetani encodes more than 127 putative regulators, including 30 two-component systems (TCSs). Here, we investigated the impact of 12 regulators on TeNT synthesis which were selected based on their homology with related regulatory elements involved in toxin production in other clostridial species. Among nine TCSs tested, three of them impact TeNT production, including two positive regulators that indirectly stimulate tent and tetR transcription. One negative regulator was identified that interacts with both tent and tetR promoters. Two other TCSs showed a moderate effect: one binds to the tent promoter and weakly increases the extracellular TeNT level, and another one has a weak inverse effect. In addition, CodY (control of dciA (decoyinine induced operon) Y) but not Spo0A (sporulation stage 0) or the DNA repair protein Mfd (mutation frequency decline) positively controls TeNT synthesis by interacting with the tent promoter. Moreover, we found that inorganic phosphate and carbonate are among the environmental factors that control TeNT production. Our data show that TeNT synthesis is under the control of a complex network of regulators that are largely distinct from those involved in the control of toxin production in Clostridium botulinum or Clostridium difficile.
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KONAGAYA, YUKIFUMI, HIROSHI URAKAMI, JUN HOSHINO, ATSUSHI KOBAYASHI, AKIHIKO SASAGAWA, AKIRA YAMAZAKI, SHUNJI KOZAKI, and NOBUMASA TANAKA. "Change of Thermal Inactivation of Clostridium botulinum Spores during Rice Cooking." Journal of Food Protection 72, no. 11 (November 1, 2009): 2400–2406. http://dx.doi.org/10.4315/0362-028x-72.11.2400.

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Cooked and packed rice (CaPR), a popular rice product in Japan, is distributed with oxygen-absorbing agents and without refrigeration. When the final product was inoculated with spores of several strains of proteolytic Clostridium botulinum at a dose of 103 spores per g (2 × 105 spores per package) and incubated at 30°C, the bacteria grew and produced neurotoxins in 40 days. To simulate more realistic cases of contamination, the same dose of spores was inoculated before the cooking process. When cooked at 100°C for 30 min, a small number of spores survived and the toxins were detected in some of the samples after incubation for 180 days. However, when cooked at 100°C for 15 min immediately followed by 105°C for 15 min, neither survivors nor the toxins were detected during incubation for 270 days after cooking. Even when inoculated with 105 spores per g of one of the most heat-resistant strains, 213B, viable spores were not detected after cooking. The inactivation by these heating conditions in different media indicated that the spores were inactivated >1,000-fold more in rice suspension than in cooked meat medium or phosphate buffer. It was therefore suggested that rice contains component(s) that facilitates thermal inactivation of C. botulinum.
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Stecher, B., G. Ahnert-Hilger, U. Weller, T. P. Kemmer, and M. Gratzl. "Amylase release from streptolysin O-permeabilized pancreatic acinar cells. Effects of Ca2+, guanosine 5′-[γ-thio]triphosphate, cyclic AMP, tetanus toxin and botulinum A toxin." Biochemical Journal 283, no. 3 (May 1, 1992): 899–904. http://dx.doi.org/10.1042/bj2830899.

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The molecular requirements for amylase release and the intracellular effects of botulinum A toxin and tetanus toxin on amylase release were investigated using rat pancreatic acinar cells permeabilized with streptolysin O. Micromolar concentrations of free Ca2+ evoked amylase release from these cells. Maximal release was observed in the presence of 30 microM free Ca2+. Ca(2+)-stimulated, but not basal, amylase release was enhanced by guanosine 5′-[gamma-thio]triphosphate (GTP[S]) (3-4 fold) or cyclic AMP (1.5-2 fold). Neither the two-chain forms of botulinum A toxin and tetanus toxin, under reducing conditions, nor the light chains of tetanus toxin, inhibited amylase release triggered by Ca2+, or combinations of Ca2+ + GTP[S] or Ca2+ + cAMP. The lack of inhibition was not due to inactivation of botulinum A toxin or tetanus toxin by pancreatic acinar cell proteolytic enzymes, as toxins previously incubated with permeabilized pancreatic acinar cells inhibited Ca(2+)-stimulated [3H]noradrenaline release from streptolysin O-permeabilized adrenal chromaffin cells. These data imply that clostridial neurotoxins inhibit a Ca(2+)-dependent mechanism which promotes exocytosis in neural and endocrine cells, but not in exocrine cells.
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Band, Philip, Edwin Vazquez-Cintron, Philip Beske, Christopher Angeles, Aurelia Syngkon, Patrick McNutt, and Konstantin Ichtchenko. "13. Recombinant derivatives of botulinum neurotoxins: should derivatives with light chain inactivating mutations retain biological activity?" Toxicon 93 (January 2015): S5—S6. http://dx.doi.org/10.1016/j.toxicon.2014.11.016.

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Dissertations / Theses on the topic "Botulinum neurotoxin inactivation"

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Conti, Emilia. "In vivo optical imaging of cortical plasticity induced by rehabilitation after stroke." Doctoral thesis, 2019. http://hdl.handle.net/2158/1152568.

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In my PhD thesis I have studied the changes in functional and structural plasticity induced by a photothrombotic stroke in mouse primary motor cortex. In order to dissect the multiple aspects consequent to the damage we exploit fluorescent imaging techniques that allow to investigate the functional and structural rearrangement of the cortex at different scale, from the entire hemisphere, with wide-field calcium imaging, up to the single synapse with two-photon microscopy. To promote a functional recovery of the mouse forelimb we applied different rehabilitative strategies in order to both foster the stabilization of regions of the cortex linked to the stroke core, and stimulate the remodelling of peri-infarct areas. We took advantage of a robotic platform (M-Platform), developed by our collaborator in Pisa, to perform the rehabilitation of mouse forelimb through a repetitive motor training. Together with this approach we applied different strategies to mould cortical activity. We temporary inhibited the healthy primary motor cortex, with an intracortical injection of Botulin Neuro Toxin E, in order to counterbalance the iper-excitability of the healthy hemisphere and to promote the structural and functional remodelling of the peri-infarct cortex. This combined rehabilitative protocol promotes the recovery of cortical maps of activation during motor training and the rewiring of interhemispheric connectivity, both from functional and structural level. Then we applied an optogenetic approach as a pro-plasticizing treatment by stimulating with light the region of the cortex surrounding the damage. By coupling this treatment with an intense motor training on the M-Platform we observed a generalized recovery of forelimb functionality in terms of manual dexterity and cortical profiles of activation. In this study, we have shown that different rehabilitative protocols that combines repetitive motor training and neuronal modulation of specific cortical regions induce a synergic effect on neuronal plasticity that promotes the recovery of structural features of healthy neuronal networks.
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Book chapters on the topic "Botulinum neurotoxin inactivation"

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Shoemaker, Charles B., and George A. Oyler. "Persistence of Botulinum Neurotoxin Inactivation of Nerve Function." In Current Topics in Microbiology and Immunology, 179–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-662-45790-0_9.

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Bigalke, H., F. Bartels, T. Binscheck, E. Erdal, G. Erdmann, U. Weller, and A. Wever. "Activation and Inactivation of Tetanus Toxin in Chromaffin Cells." In Botulinum and Tetanus Neurotoxins, 241–50. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4757-9542-4_25.

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