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Botulinum toxin, also referred to as BTX, is a neurotoxic protein created by the Clostridium botulinum bacterium. It is also present in similar bacteria related to clostridium botulinum, however, for the purpose of this paper, the focus will be on its correlation with the gram-positive anaerobic bacteria Clostridium botulinum. The botulinum neurotoxin is classified under eight antigenically and serologically distinguishable exotoxins including BoNT A, B, C1, C2, D, E, F, and G. While types C and D are toxic only in animals, types A, B, E, and F cause significant toxicity levels in human beings. Each exotoxin type possesses individual potencies, which further emphasizes the great care needed to ensure safe use.
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Extracted from the neurotoxigenic strains of anaerobic and spore forming bacteria Clostridium botulinum, botulinum toxin’s creation stems from four possible bacteria sources under the genus Clostridium. These include Clostridium botulinum, Clostridium butyrricum, Clostridium barati, and Clostridium argentinensis. (Smith 2015) Along with these strains of bacteria, the botulinum toxin was found to share similar genes among the Weissella oryzae genome. After much research, scientists found a link between this bacteria and Clostridia. (Mansfield 2015) The produced neurotoxins contain a high level of amino acid sequence which results in relatively inactive, single polypeptide chains including a heavy and light chain at the average level of 100 and 50 kDa connected through a disulfide bond. The neurotoxin complex also has a shared association with other nontoxic proteins which contributes to the hemagglutinating properties.
As stated previously, many different types of this bacteria have been identified. All of the
eight separate exotoxins vary in potency and toxicity. Out of the eight, type A, type B, and type F are the most potent toxins of the botulinum toxin respectively. Types A, B, and E are significant contributors to systemic botulism in humans. While these all contain the possibility of potentially fatal doses, certain variants are approved for human use. Researcher A.B. Scott first introduced type A botulinum toxin as an effective treatment of strabismus for human individuals. The neurotoxin protein has also proven successful in treating a number of conditions including disorders of spasticity, and is often found useful for a variety of medical purposes.
Most commonly found on plants, in soil, and the intestinal tract of many animals, botulinum toxin is found in many areas. Lack of proper food preparation and food storage can also increase the risk of the botulinum toxin developing. Referred to as food-borne botulism, this often occurs with foods canned at home, because there is no official regulation of the canned food. One should refrain from storing food for prolonged periods of time and in inadequate jars that allow bacteria to grow in order to prevent this potentially fatal bacteria. According to the Centers for Disease Control and Prevention, “Home-canned vegetables are the most common cause of botulism outbreaks in the United States. From 1996 to 2014, there were 210 outbreaks of foodborne botulism reported to the CDC. Of the 145 outbreaks that were caused by home-prepared foods, 43 outbreaks, or 30%, were from home-canned vegetables. These outbreaks often occurred because home canners did not follow canning instructions, did not use pressure canners, ignored signs of food spoilage, or did not know they could get botulism from improperly preserving vegetables.”
Once the bacterium has entered one’s system, symptoms typically present themselves 18 to 36 hours after ingesting contaminated food. This is the average time frame; however, symptoms may arise as early as 6 hours after contamination or even as late as 10 days. In humans, it presents itself through paralysis of the inhibiting neurotransmitter release at the peripheral cholinergic nerve terminals near the skeletal system and autonomic nervous system. The botulinum toxin blocks the neural transmission by inhibiting the release of acetylcholine from the presynaptic motor neurons. It preys on four separate receptor sites including the neuromuscular junction, autonomic ganglia, postganglionic parasympathetic nerve endings and postganglionic sympathetic nerve endings. All of these nerve endings supply acetylcholine to the body’s systems. The heavy 100 kDa single polypeptide chain binds to certain receptors at the presynaptic surface of the cholinergic neurons which radiate specifically towards high affinity receptors. As a result of this, the endocytosis restricts the toxin-receptor complex, and consequently, the disulphide bond is broken allowing the toxin to reach the cytoplasm. The light 50 kDa single polypeptide chain interacts differently from its heavier counterpart. The light single polypeptide chain is associated with the syntaxin, the vesicle associated membrane protein, and the synaptosomal associated protein (SNAP 25). When the bacteria hits an individual’s system, it directly impairs the function of these proteins.
Between the first four to seven days after exposure, the most extreme of the side effects are felt. Most individuals experience severe neurotransmitter paralysis during this time. In most cases, the botulinum toxin requires 24-72 hours for side effects to begin to show. During this time, the botulinum toxin is beginning to process through the synaptosomal associated protein. However, this time frame may fluctuate depending on the individual. In some cases, individuals may not feel the effects of the toxin until 5 days after exposure. While the botulinum toxin effects peak around 10 days, the lasting effects can be present up to 8-12 weeks. Since the botulinum toxin attacks the alpha motor neurones at the neuromuscular junction, the side effects include severe weakness of the striated muscles. It also has adverse reactions on the parasympathetic and sympathetic systems. By inhibiting the production of acetylcholine in the parasympathetic and cholinergic postganglionic sympathetic neurons, it further increases the likelihood of paralysis.
Despite its dangerous, and potentially deadly side effects, its use is quite broad, as it has been approved in almost every medical sub-specialty department. Most commonly used in cosmetic medicine, more than 1.5 million Botox® injection services were provided in the United States alone. According to the American Society for Aesthetic Plastic Surgery (ASAPS), “the popularity of Botox® in the U.S. has skyrocketed, with a 40.6 percent increase in procedures, and a 5.1 percent increase since 2017.” (Dermatol 2010) There are various formulations of the botulinum toxin for medical use. In clinical use currently Serotype A is the prominent commercially available formulation. While it is currently the only available botulinum serotype used in commercial production, serotypes B, C, and F are currently undergoing testing for potential use. Extracted from serotype A, researchers have created two formulations of medical grade Botox®. These include Dysport® and Botox®.
Officially approved by the Federal Drug and Food Administration (FDA) in December of 1989, it gained popularity in medical offices as an unofficial treatment for blepharospasm, hemifacial spasms, and strabismus. Now its uses have vastly expanded past these conditions, but it still is used as a treatment for the above conditions. In an effort to ensure safe procedures surrounding the use of BoNT, the substance undergoes a severe regulation process which filters the appropriate dosage and formula of the botulinum toxin.
When creating Botox® , a sterilized form of lyophilized botulinum toxin type A is produced by a Hall strain of C. botulinum. It endures a preparation process in which the toxin is filtered using a variety of acid precipitations to create a crystalline complex which holds the toxin with additional proteins. The Botox® formula has been adjusted throughout the years. Originally the concentration of the Clostridium botulinum was 5 to 6 times less potent than the current formulation. Currently, each Botox® vile contains 100 units of the Clostridium botulinum serotype A, 0.9 milligrams of sodium chloride, and 0.5 milligrams of Albumin, and has a much higher degree of potency than previous concoctions. Its storage requires a low temperature of -5 degrees Celsius, and it must be stored in a freezer to maintain its quality of concentration. It is recommended to refrain from using a sterile saline reconstitute which often contains preservatives. Instead, Botox® should be reconstituted using a preservative free sterile saline solution to preserve its freshness. Researchers also debate over the use of 0.9 percent benzyl alcohol as a useful reconstitute that also reduces the amount of microbial contamination and may provide a mild analgesic effect.
Once an individual is ready to use the preserved Botox® , it is sensitive to agitation or bubbling, and easily becomes a denatured solution. When it is reconstituted, it must be refrigerated and kept at a 2 to 8 degree Celsius level. Once it is in its reconstituted form, the Botox® requires use within 4 hours of its opening. Some studies have pushed this time up to 6 hours with no loss of potency, however, after a 12 hour day there was a 44 percent drop in potency. After refreezing the solution for a 1 to 2 week period, there was a significant loss of potency resulting in a 70 percent drop.
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When injecting Botox® into muscles or glands, a 30-gauge 1-inch needle is used to insert the solution. The Teflon coated needle is injected directly into the area of treatment. Depending on the sensitivity of the injection spot, the needle may be guided by a electromyography to ensure proper placement. The dose of the injection is dependent upon the individual’s size along with the size of the treatment spot. For instance, a larger quantity of the botulinum toxin is required in an area holding greater muscle mass. Whereas a smaller dose is needed for an area containing a smaller degree of muscle mass.
Dysport® , the second variation of the Clostridium botulinum toxin commonly used in cosmetic medicine, has gained popularity in Europe and its surrounding countries. In order to produce this product, it is put through extensive purification techniques including column based filtration, and stored in vials kept in controlled room temperature spaces. While both Botox® and Dysport® are similar in formulation, serious concern regarding their dosage potency has arisen. From extensive research, we have discovered Botox® to have 3 times stronger potency than Dysport®. A single unit of Botox contains 3 times more potency than 1 unit of Dysport® . Other differences between the two are the bacterium strain each is collected from, and the various methods of preparation, purification, and diffusion processes.
Aside from these two main variants of the botulinum toxin, researchers have been creating and testing derivatives from different serotypes including botulinum toxin B, and botulinum toxin F. These include Xeomin®, Neurobloc®, Myobloc®, and Elan®. Xeomin® is the third derivative of the botulinum toxin A. It is separate from its counterparts due to the differences in purification and the filtering process it experiences. The complexing proteins are removed through a process of extensive purification. It holds 150 kDa of the neurotoxin, and shares a similar makeup to that of Botox®. In comparison to its concentration to Botox® , 1 unit of Xeomin® is comparable to 1 unit of Botox® . Due to the lack of complexing proteins, it contains the lowest content of bacterial protein which effects its ability to neutralize the formation of anti-bodies.
Neurobloc® is another variant of the botulinum toxin. It is categorized under the Clostridium botulinum type B. It is popular in the United Kingdom, United States, and Canada; however, lack of sufficient testing has prevented its legal use thus far. Further testing must be done in order for this product to receive approval for cosmetic and medical use.
Myobloc®, also referred to as Elan®, shares a similar composition to Dysport® . It has reconstituted abilities, and has a shelf life which extends past 12 months. In comparison to Botox® , which expires in a single day, Myobloc®’s long lasting capability is especially useful for patient scheduling. One downside to Myobloc®, however, is the low concentration it has. An individual may require a higher volume of Myobloc® to reach the same effects of Botox® . Due to its high protein content, antibody formation is more likely to occur in this product as well.
As with any cosmetic or medical procedure, there are certain risks that accompany the use of the botulinum toxin. Consequences including muscle weakness near the injection site, trouble swallowing for several months after treatment, muscle stiffness, neck pain, blurred vision, puffiness, dry eyes, drooping skin, dry mouth, headache, and fatigue can be direct results of improper use or negative reactions to the treatment. If the toxin is properly injected at the correct concentration and dose, the side effects should be minimum, however, if the injection fails to meet the criteria authorized by the Federal Drug and Food Administration, possible more fatal side effects can occur.
As a general precaution, an individual should avoid any activity that may cause adverse reactions. In order to lower one’s risk for developing a negative side effect, the following recommendations are listed. After receiving a botulinum toxin injection, the individual should plan a restful day where strenuous activities or any trauma to the affected areas are avoided for a minimum of 2 weeks. This includes refraining from exercise, facials, massages, and laser treatments. Lack of proper aftercare may result in dislodged toxins floating to other areas of the body, developing bumps, or intense pressure of areas aside from the original injection site.
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