Foodborne Botulism: Clinical Diagnosis and Medical Treatment

Lonati, Davide; Schicchi, Azzurra; Crevani, Marta; Buscaglia, Eleonora; Scaravaggi, Giulia; Maida, Francesca; Cirronis, Marco; Petrolini, Valeria Margherita; Locatelli, Carlo

doi:10.3390/toxins12080509

Cited by 66 publications

(54 citation statements)

References 60 publications

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“…It probably shows a similar pattern than in experimental animals, notably supporting the long persistence of BoNT in the serum of certain patients. BoNT detection in serum is the most direct way to confirm a diagnosis of botulism [ 41 , 42 , 191 ]. However, the presence of BoNT in the blood circulation depends on the time between serum sampling and the symptom onset, the initial amount of toxin involved in the disease, which has been ingested or produced locally, and probably of individual host factors related to toxin absorption and/or elimination which remain to be defined.…”

Section: Discussionmentioning

confidence: 99%

“…BoNT amino acid sequences deduced from bont gene sequencing revealed that each toxinotype is subdivided into an increasing number of subtypes defined as >2.6% amino acid variation. Thus, 41 BoNT subtypes and multiple variants have been reported [5][6][7]. More recently, genome comparison showed the presence of bont related sequences in a few non-clostridial strains such as bont/Wo or bont/I from Weisenella oryzae, a bacterium of fermented rice, bont/J (ebont/F or bont/En) from an Enterococcus faecalis strain in a cow, and Cp1 from Chryseobacterium piperi from sediment [1,[8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

“…Botulism cases are suspected on the basis of clinical symptoms and epidemiological aspects. Botulism confirmation is supported by laboratory tests that are required for botulism typing [ 41 , 42 ]. Initially, food-borne botulism was confirmed by BoNT detection in suspected food samples using experimental animals [ 40 ].…”

Section: Introductionmentioning

confidence: 99%

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Toxemia in Human Naturally Acquired Botulism

Rasetti-Escargueil

Lemichez

Popoff

2020

Toxins

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Human botulism is a severe disease characterized by flaccid paralysis and inhibition of certain gland secretions, notably salivary secretions, caused by inhibition of neurotransmitter release. Naturally acquired botulism occurs in three main forms: food-borne botulism by ingestion of preformed botulinum neurotoxin (BoNT) in food, botulism by intestinal colonization (infant botulism and intestinal toxemia botulism in infants above one year and adults), and wound botulism. A rapid laboratory confirmation of botulism is required for the appropriate management of patients. Detection of BoNT in the patient’s sera is the most direct way to address the diagnosis of botulism. Based on previous published reports, botulinum toxemia was identified in about 70% of food-borne and wound botulism cases, and only in about 28% of infant botulism cases, in which the diagnosis is mainly confirmed from stool sample investigation. The presence of BoNT in serum depends on the BoNT amount ingested with contaminated food or produced locally in the intestine or wound, and the timeframe between serum sampling and disease onset. BoNT levels in patient’s sera are most frequently low, requiring a highly sensitive method of detection. Mouse bioassay is still the most used method of botulism identification from serum samples. However, in vitro methods based on BoNT endopeptidase activity with detection by mass spectrometry or immunoassay have been developed and depending on BoNT type, are more sensitive than the mouse bioassay. These new assays show high specificity for individual BoNT types and allow more accurate differentiation between positive toxin sera from botulism and autoimmune neuropathy patients.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Toxemia in Human Naturally Acquired Botulism

Rasetti-Escargueil

Lemichez

Popoff

2020

Toxins

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“…Clostridium botulinum , an anaerobic, rod-shaped bacterium, produces a neurotoxin called botulinum toxin (BoNT) during sporulation [ 1 , 2 , 3 ]. BoNT is the most potent biological toxin, as it causes botulism manifested by paralysis of muscles and eventual fatal respiratory failure [ 4 , 5 ]. When an action potential arrives at the cholinergic presynaptic nerve terminal, there is an influx of calcium into the presynaptic terminal, which then facilitates acetylcholine vesicle fusion with the presynaptic membrane; this fusion is facilitated by a group of proteins referred to as SNARE (soluble N-ethylmaleimide-sensitive factor attachment receptor) proteins, which include SNAP 25 (25 kD synaptosomal-associated protein) and Syntaxin [ 6 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

Botulinum Toxin in Movement Disorders: An Update

Anandan

Jankovic

2021

Toxins

106

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Since its initial approval in 1989 by the US Food and Drug Administration for the treatment of blepharospasm and other facial spasms, botulinum toxin (BoNT) has evolved into a therapeutic modality for a variety of neurological and non-neurological disorders. With respect to neurologic movement disorders, BoNT has been reported to be effective for the treatment of dystonia, bruxism, tremors, tics, myoclonus, restless legs syndrome, tardive dyskinesia, and a variety of symptoms associated with Parkinson’s disease. More recently, research with BoNT has expanded beyond its use as a powerful muscle relaxant and a peripherally active drug to its potential central nervous system applications in the treatment of neurodegenerative disorders. Although BoNT is the most potent biologic toxin, when it is administered by knowledgeable and experienced clinicians, it is one of the safest therapeutic agents in clinical use. The primary aim of this article is to provide an update on recent advances in BoNT research with a focus on novel applications in the treatment of movement disorders. This comprehensive review of the literature provides a critical review of evidence-based clinical trials and highlights recent innovative pilot studies.

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“…Four distinct phenotypic groups (I-IV) of C. botulinum are recognized. C. botulinum Groups I and II are primarily responsible for human botulism, the most frequent form of botulism in the European Union [5]. C. botulinum Group I has minimum and optimum growth temperatures of 12 • C and 37 • C, respectively.…”

Section: Introductionmentioning

confidence: 99%

Novel Lytic Enzyme of Prophage Origin from Clostridium botulinum E3 Strain Alaska E43 with Bactericidal Activity against Clostridial Cells

Morzywolek

Plotka

Kaczorowska

et al. 2021

IJMS

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Clostridium botulinum is a Gram-positive, anaerobic, spore-forming bacterium capable of producing botulinum toxin and responsible for botulism of humans and animals. Phage-encoded enzymes called endolysins, which can lyse bacteria when exposed externally, have potential as agents to combat bacteria of the genus Clostridium. Bioinformatics analysis revealed in the genomes of several Clostridium species genes encoding putative N-acetylmuramoyl-l-alanine amidases with anti-clostridial potential. One such enzyme, designated as LysB (224-aa), from the prophage of C. botulinum E3 strain Alaska E43 was chosen for further analysis. The recombinant 27,726 Da protein was expressed and purified from E. coli Tuner(DE3) with a yield of 37.5 mg per 1 L of cell culture. Size-exclusion chromatography and analytical ultracentrifugation experiments showed that the protein is dimeric in solution. Bioinformatics analysis and results of site-directed mutagenesis studies imply that five residues, namely H25, Y54, H126, S132, and C134, form the catalytic center of the enzyme. Twelve other residues, namely M13, H43, N47, G48, W49, A50, L73, A75, H76, Q78, N81, and Y182, were predicted to be involved in anchoring the protein to the lipoteichoic acid, a significant component of the Gram-positive bacterial cell wall. The LysB enzyme demonstrated lytic activity against bacteria belonging to the genera Clostridium, Bacillus, Staphylococcus, and Deinococcus, but did not lyse Gram-negative bacteria. Optimal lytic activity of LysB occurred between pH 4.0 and 7.5 in the absence of NaCl. This work presents the first characterization of an endolysin derived from a C. botulinum Group II prophage, which can potentially be used to control this important pathogen.

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Foodborne Botulism: Clinical Diagnosis and Medical Treatment

Cited by 66 publications

References 60 publications

Toxemia in Human Naturally Acquired Botulism

Toxemia in Human Naturally Acquired Botulism

Botulinum Toxin in Movement Disorders: An Update

Novel Lytic Enzyme of Prophage Origin from Clostridium botulinum E3 Strain Alaska E43 with Bactericidal Activity against Clostridial Cells

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