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Journal articles on the topic 'Tetanus-Toxin'

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Published: 4 June 2021

Last updated: 17 June 2025

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Matsuda, Morihiro, and Nakaba Sugimoto. "Tetanus Toxin." Journal of Toxicology: Toxin Reviews 16, no. 4 (1997): 241–52. http://dx.doi.org/10.3109/15569549709016459.

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Demotz, S., A. Lanzavecchia, U. Eisel, H. Niemann, C. Widmann, and G. Corradin. "Delineation of several DR-restricted tetanus toxin T cell epitopes." Journal of Immunology 142, no. 2 (1989): 394–402. http://dx.doi.org/10.4049/jimmunol.142.2.394.

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Abstract We have characterized five human T cell clones specific for tetanus toxin. The combination of different techniques allowed us to precisely map two T cell epitopes within fragments 830-843 and 1273-1284 of tetanus toxin, as formally demonstrated by the use of corresponding synthetic peptides. The three other T cell clones were specific for regions 2-602, 604-742, and 865-1315 of tetanus toxin, respectively. The five T cell clones were shown to be restricted to HLA-DR Ag. Furthermore, the allele of HLA-DR utilized by the various epitopes has been determined. The use of HLA-DR-transfected L cells as APC directly demonstrated that two epitopes, one of which represented by fragment 1273-1284, were recognized in association with HLA-DRw52a. For the other three T cell epitopes, the data strongly suggested they were recognized in association with HLA-DR5. Finally, a sixth T cell clone was shown to be specific for tetanus toxoid, the vaccinal preparation of tetanus toxin, and not for other tetanus toxin fragments. This indicated that immunization with tetanus toxoid probably elicits a T cell response directed only in part against native tetanus toxin.

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Chawla, Dr Anil Kumar, Chandrani Das, Paramdeep Singh, Mansha Tiwari, and Dr Seema Chaudhary. "Production of tetanus toxin by using media substantially free from meat and blood." Asian Journal of Pharmaceutical and Clinical Research 9, no. 6 (2016): 284. http://dx.doi.org/10.22159/ajpcr.2016.v9i6.14410.

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The present study was to redesign the conventional Mueller and Miller medium to produce tetanus toxin from Clostridium tetani. Meat based ingredients (such as Bovine Heart/ Brain/ Liver Infusion) were replaced with vegetable peptone & alternate casein hydrolysate and scaled up from 100mL to 1000mL. Modified Mueller and Miller Medium containing vegetable peptone (substitute of BHI) and alternate casein hydrolysate were used for production and scale -up of tetanus toxin. Detoxification of tetanus toxin was carried out by using formaldehyde to produce tetanus toxoid. Purification of tetanus toxoid was achieved by fractional precipitation. It was found that under optimum conditions, use of meat free media leads to production of tetanus toxin with equal limes flocculation (Lf) titer and high antigenic content at par with conventional meat based media without any post vaccination infections. The yield of toxin was improved during scale-up of the process. The present study provides a method for growth of Clostridium tetani that maximizes tetanus toxin production without any use of animal-derived components.

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Critchley, D. R., P. G. Nelson, W. H. Habig, and P. H. Fishman. "Fate of tetanus toxin bound to the surface of primary neurons in culture: evidence for rapid internalization." Journal of Cell Biology 100, no. 5 (1985): 1499–507. http://dx.doi.org/10.1083/jcb.100.5.1499.

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We examined the nature of the tetanus toxin receptor in primary cultures of mouse spinal cord by ligand blotting techniques. Membrane components were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to nitrocellulose sheets, which were overlaid with 125I-labeled tetanus toxin. The toxin bound only to material at or near the dye front, which was lost when the cells were delipidated before electrophoresis. Gangliosides purified from the lipid extract were separated by thin-layer chromatography and the chromatogram was overlaid with 125I-toxin. The toxin bound to gangliosides corresponding to GD1b and GT1b. Similar results were obtained with brain membranes; thus, gangliosides rather than glycoproteins appear to be the toxin receptors both in vivo and in neuronal cell cultures. To follow the fate of tetanus toxin bound to cultured neurons, we developed an assay to measure cell-surface and internalized toxin. Cells were incubated with tetanus toxin at 0 degree C, washed, and sequentially exposed to antitoxin and 125I-labeled protein A. Using this assay, we found that much of the toxin initially bound to cell surface disappeared rapidly when the temperature was raised to 37 degrees C but not when the cells were kept at 0 degree C. Some of the toxin was internalized and could only be detected by our treating the cells with Triton X-100 before adding anti-toxin. Experiments with 125I-tetanus toxin showed that a substantial amount of the toxin bound at 0 degree C dissociated into the medium upon warming of the cells. Using immunofluorescence, we confirmed that some of the bound toxin was internalized within 15 min and accumulated in discrete structures. These structures did not appear to be lysosomes, as the cell-associated toxin had a long half-life and 90% of the radioactivity released into the medium was precipitated by trichloroacetic acid. The rapid internalization of tetanus toxin into a subcellular compartment where it escapes degradation may be important for its mechanism of action.

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Qazi, Omar, Dorothea Sesardic, Robert Tierney, et al. "Reduction of the Ganglioside Binding Activity of the Tetanus Toxin HC Fragment Destroys Immunogenicity: Implications for Development of Novel Tetanus Vaccines." Infection and Immunity 74, no. 8 (2006): 4884–91. http://dx.doi.org/10.1128/iai.00500-06.

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ABSTRACT In this study, the immunogenicities of the nontoxic HC fragment of tetanus toxin and derivatives lacking ganglioside binding activity were compared with that of tetanus toxoid after subcutaneous immunization of mice. Wild-type HC (HCWT) protein and tetanus toxoid both elicited strong antibody responses against toxoid and HC antigens and provided complete protection against toxin challenge. Mutants of HC containing deletions essential for ganglioside binding elicited lower responses than HCWT. HCM115, containing two amino acid substitutions within the ganglioside binding site, provided reduced protection against tetanus toxin challenge compared with HCWT, consistent with lower anti-HC and anti-toxoid antibody titers. Circular-dichroism spectroscopy and intrinsic fluorescence spectroscopy showed minimal structural perturbation in HCM115. We conclude that the presence of the ganglioside binding site within HC may be essential for induction of a fully protective anti-tetanus response comparable to that induced by tetanus toxoid by subcutaneous injection.

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Stecher, B., G. Ahnert-Hilger, U. Weller, T. P. Kemmer та 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, № 3 (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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Bergey, G. K., H. Bigalke, and P. G. Nelson. "Differential effects of tetanus toxin on inhibitory and excitatory synaptic transmission in mammalian spinal cord neurons in culture: a presynaptic locus of action for tetanus toxin." Journal of Neurophysiology 57, no. 1 (1987): 121–31. http://dx.doi.org/10.1152/jn.1987.57.1.121.

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Tetanus toxin reduces monosynaptic inhibitory and excitatory synaptic transmission in mouse spinal cord neurons in culture. Inhibitory transmission is preferentially reduced by the toxin; however, excitatory transmission is also ultimately reduced and blocked by the concentrations of toxin used in these studies. Recordings from monosynaptically connected cell pairs revealed a marked diminution in amplitude of evoked monosynaptic inhibitory postsynaptic potentials coincident with the onset of convulsant action at a time when evoked monosynaptic EPSPs were relatively unaffected. Increased polysynaptic excitation occurred as a result of diminished inhibition. This supports the reduction of inhibition as an important mechanism in the convulsant action of tetanus toxin. Quantal analysis of the late effects of tetanus toxin on the monosynaptic excitatory postsynaptic potential revealed a reduction in quantal number with no reduction in quantal size, thus demonstrating a presynaptic locus of action for the toxin on spinal neurons.

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Galli, T., T. Chilcote, O. Mundigl, T. Binz, H. Niemann, and P. De Camilli. "Tetanus toxin-mediated cleavage of cellubrevin impairs exocytosis of transferrin receptor-containing vesicles in CHO cells." Journal of Cell Biology 125, no. 5 (1994): 1015–24. http://dx.doi.org/10.1083/jcb.125.5.1015.

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Cellubrevin is a member of the synaptobrevin/VAMP family of SNAREs, which has a broad tissue distribution. In fibroblastic cells it is concentrated in the vesicles which recycle transferrin receptors but its role in membrane trafficking and fusion remains to be demonstrated. Cellubrevin, like the synaptic vesicle proteins synaptobrevins I and II, can be cleaved by tetanus toxin, a metallo-endoprotease which blocks neurotransmitter release. However, nonneuronal cells are unaffected by the toxin due to lack of cell surface receptors for its heavy chain. To determine whether cellubrevin cleavage impairs exocytosis of recycling vesicles, we tested the effect of tetanus toxin light chain on the release of preinternalized transferrin from streptolysin-O-perforated CHO cells. The release was found to be temperature and ATP dependent as well as NEM sensitive. Addition of tetanus toxin light chain, but not of a proteolytically inactive form of the toxin, resulted in a partial inhibition of transferrin release which correlated with the toxin-mediated cleavage of cellubrevin. The residual release of transferrin occurring after complete cellubrevin degradation was still ATP dependent. Our results indicate that cellubrevin plays an important role in the constitutive exocytosis of vesicles which recycle plasmalemma receptors. The incomplete inhibition of transferrin release produced by the toxin suggests the existence of a cellubrevin-independent exocytotic mechanism, which may involve tetanus toxin-insensitive proteins of the synaptobrevin/VAMP family.

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Mitchell, John. "Tetanus Toxin-enhanced GABA Immunoreactivity in Living Neurons." Journal of Histochemistry & Cytochemistry 46, no. 3 (1998): 321–26. http://dx.doi.org/10.1177/002215549804600305.

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Analysis of the connectivity between different neuronal cell types is dependent on an appreciation of their dendritic and axonal arborizations. A detailed study of the dendrites and axons of GABAergic neurons has been thwarted by the lack of a suitable technique for enhancing GABA immunoreactivity. This article describes a procedure using tetanus toxin which, when applied to organotypic hippocampal cultures, considerably enhances the immunoreactivity in the dendrites and axons of the GABA- and somatostatin-containing neurons and clearly demonstrates the co-localization of GABA and somatostatin immunoreactivities in the same neuron. Tetanus toxin was applied to the culture medium on Day 14 for a 24-hr period and the cultures were fixed at the end of Day 18. Tetanus toxin-treated cultures ( n = 30) or untreated cultures ( n = 40) were incubated for either GABA or somatostatin immunoreactivity. Tetanus toxin-treated cultures used for co-localization studies ( n = 20) were incubated for both GABA and somatostatin immunoreactivity.

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Mujezinovic, Indira, Ahmed Smajlovic, and Vitomir Cupic. "The effect of haloperidol, aminooxyacetic acid and (-)-nuciferine on prolonging survival time of mice with tetanus." Veterinarski glasnik 72, no. 2 (2018): 122–28. http://dx.doi.org/10.2298/vetgl171023005m.

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Introduction. Tetanus, also known as lockjaw, is a very dangerous, infectious, acute, usually afebrile disease characterised by muscle spasms. The causative agent of the disease is the bacterium Clostridium tetani. This pathogen produces a specific neurotoxin, termed tetanus toxin, with two components: tetanospasmin and tetanolysin. Light chains of tetanospasmin cleavage synaptobrevin, which in turn prevent release of the inhibitory neurotransmitter GABA into the synaptic cleft. The ?-motor neurons are, therefore, under no inhibitory control, as a result of which they undergo sustained excitatory discharge causing the characteristic motor spasms of tetanus. Materials and Methods. In this research, we attempted to normalise disorders caused by tetanus toxin by using haloperidol (at doses of 4, 5, 6, 7 and 8 mg/kg b.w.), alone and in combination with (-)-nuciferine (at a dose of 5 mg/kg b.w.) or aminooxyacetic acid (at a dose of 20 mg/kg b.w.). Experiments were conducted on albino mice. Experimental tetanus was induced by application of tetanus toxin. Results and Conclusions. Application of haloperidol (alone and in combination with (-)-nuciferine and aminooxyacetic acid) was carried out 24 h following the application of tetanus toxin. It was found that haloperidol, given alone in a dose of 4 mg/kg, prolonged the average survival time of mice with experimental tetanus by 24.35 h compared to the control animals. Additionally, the combination of haloperidol with (-)-nuciferine slightly, but non-significantly, extended survival time , while the combination of haloperidol with aminooxyacetic acid produced the best effect on extension of survival time (mice survived on average 27.74 h longer than control mice).

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Randhawa, Varinder K., Philip J. Bilan, Zayna A. Khayat, et al. "VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts." Molecular Biology of the Cell 11, no. 7 (2000): 2403–17. http://dx.doi.org/10.1091/mbc.11.7.2403.

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Like neuronal synaptic vesicles, intracellular GLUT4-containing vesicles must dock and fuse with the plasma membrane, thereby facilitating insulin-regulated glucose uptake into muscle and fat cells. GLUT4 colocalizes in part with the vesicle SNAREs VAMP2 and VAMP3. In this study, we used a single-cell fluorescence-based assay to compare the functional involvement of VAMP2 and VAMP3 in GLUT4 translocation. Transient transfection of proteolytically active tetanus toxin light chain cleaved both VAMP2 and VAMP3 proteins in L6 myoblasts stably expressing exofacially myc-tagged GLUT4 protein and inhibited insulin-stimulated GLUT4 translocation. Tetanus toxin also caused accumulation of the remaining C-terminal VAMP2 and VAMP3 portions in Golgi elements. This behavior was exclusive to these proteins, because the localization of intracellular myc-tagged GLUT4 protein was not affected by the toxin. Upon cotransfection of tetanus toxin with individual vesicle SNARE constructs, only toxin-resistant VAMP2 rescued the inhibition of insulin-dependent GLUT4 translocation by tetanus toxin. Moreover, insulin caused a cortical actin filament reorganization in which GLUT4 and VAMP2, but not VAMP3, were clustered. We propose that VAMP2 is a resident protein of the insulin-sensitive GLUT4 compartment and that the integrity of this protein is required for GLUT4 vesicle incorporation into the cell surface in response to insulin.

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Inic-Kanada, Aleksandra, Marijana Stojanovic, Irena Zivkovic, Vladimir Petrusic та Ljiljana Dimitrijevic. "The monoclonal antibody 26 raised against tetanus toxoid also recognizes tetanus toxin and β2-glycoprotein I - its binding properties in vitro and potential applications". Journal of the Serbian Chemical Society 74, № 3 (2009): 245–57. http://dx.doi.org/10.2298/jsc0903245i.

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A murine monoclonal IgG1 antibody, marked as MAb26, specific for tetanus toxoid has been immunochemically characterized. By performing enzyme-linked immunosorbent assays (ELISAs) and western blot analyses, it was demonstrated that MAb26 reacted with tetanus toxoid, tetanus toxin and ?2-glycoprotein I (?2GPI). According to the results, MAb26 recognized the sequential epitope on the tetanus heavy chain. The affinity constant, calculated from Scatchard plots of MAb26 binding to tetanus toxoid, was 1.145?108 M-1 and the measurement of the relative affinity of MAb26 by ELISA using thiocyanate elution showed a significantly higher affinity of MAb26 to the toxoid (p = 0.0012) in comparison to the toxin. Additionally, the reactivity of MAb26 toward the toxoid forms increased when the tetanus toxin was detoxified using 8 mM and higher formaldehyde concentrations. The similarity of the tetanus toxoid to several sera proteins, either at the level of its conformation (IL-1?) or at the level of peptide sequences (?2GPI, laminin) favors its role in autoimmunity by the mechanism of molecular mimicry. As the induction of an autoimmune disease is dependent on the breakdown of tolerance, which could be the result of an overt hyperstimulation, the control of the presence and concentration of self-reactive epitopes in vaccine preparations is a prerequisite. In this study, it was shown that MAb26 can: 1) discriminate between the tetanus toxin and different toxoid forms, which makes it a good candidate for antibody control during vaccine preparation; 2) due to its cross-reactivity with ?2GPI, it could provide information on the presence of a potentially dangerous sequential epitope expressed at the protein surface.

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Johnston, Louise, Fatme Mawas, Rob Tierney, Omar Qazi, Neil Fairweather, and Dorothea Sesardic. "Transcutaneous delivery of tetanus toxin Hc fragment induces superior tetanus toxin neutralizing antibody response compared to tetanus toxoid." Human Vaccines 5, no. 4 (2009): 230–36. http://dx.doi.org/10.4161/hv.5.4.6877.

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Simpson, L. L. "Molecular Pharmacology of Botulinum Toxin and Tetanus Toxin." Annual Review of Pharmacology and Toxicology 26, no. 1 (1986): 427–53. http://dx.doi.org/10.1146/annurev.pa.26.040186.002235.

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Reboul, A., J. Arvieux, J. F. Wright, and M. G. Colomb. "Proteolytic fragmentation of tetanus toxin by subcellular fractions of JY, a B lymphoblastoid cell line." Biochemical Journal 277, no. 1 (1991): 47–51. http://dx.doi.org/10.1042/bj2770047.

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Proteolysis of 125I-labelled tetanus toxin by subcellular fractions from an Epstein-Barr-virus-transformed B lymphoblastoid cell line, JY, was investigated. Fractions enriched in lysosomes and plasma membranes cleaved the toxin molecule at several sites, with a pH optimum of 5.5. N-Terminal sequence analysis of Mr-81,000, -45,000 and -35,000 proteolytic fragments indicated cleavage of the Asp-460-Leu-461, Asp-872-Glu-873 and Ile-1013-Thr-1014 peptide bonds, all sites located within the heavy chain of the toxin molecule. Additional sites near the C-terminus of the heavy chain, giving rise to low-Mr peptides, were implicated. The toxin light chain was more resistant to proteolysis. A similar pattern of fragmentation was observed with tetanus toxin biosynthetically radiolabelled with 14C-labelled amino acids, showing that the proteolysis was not an artifact caused by iodination. The proteolytic activity was inhibited by the serine proteinase inhibitor di-isopropyl phosphorofluoridate, thiol-blocking proteinase inhibitors N-ethylmaleimide and iodoacetamide, and by EDTA. These results represent a preliminary characterization of the processing in vitro of tetanus toxin by an antigen-presenting cell line.

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Aktories, Klaus. "Botulinum neurotoxin and tetanus toxin." Trends in Pharmacological Sciences 11, no. 1 (1990): 45. http://dx.doi.org/10.1016/0165-6147(90)90042-7.

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GUSTAFSSON, B., E. WHITMORE, and M. TIRU. "Neutralization of Tetanus Toxin by Human Monoclonal Antibodies Directed Against Tetanus Toxin Fragment C." Hybridoma 12, no. 6 (1993): 699–708. http://dx.doi.org/10.1089/hyb.1993.12.699.

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Dong, Min, Geoffrey Masuyer, and Pål Stenmark. "Botulinum and Tetanus Neurotoxins." Annual Review of Biochemistry 88, no. 1 (2019): 811–37. http://dx.doi.org/10.1146/annurev-biochem-013118-111654.

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Botulinum neurotoxins (BoNTs) and tetanus neurotoxin (TeNT) are the most potent toxins known and cause botulism and tetanus, respectively. BoNTs are also widely utilized as therapeutic toxins. They contain three functional domains responsible for receptor-binding, membrane translocation, and proteolytic cleavage of host proteins required for synaptic vesicle exocytosis. These toxins also have distinct features: BoNTs exist within a progenitor toxin complex (PTC), which protects the toxin and facilitates its absorption in the gastrointestinal tract, whereas TeNT is uniquely transported retrogradely within motor neurons. Our increasing knowledge of these toxins has allowed the development of engineered toxins for medical uses. The discovery of new BoNTs and BoNT-like proteins provides additional tools to understand the evolution of the toxins and to engineer toxin-based therapeutics. This review summarizes the progress on our understanding of BoNTs and TeNT, focusing on the PTC, receptor recognition, new BoNT-like toxins, and therapeutic toxin engineering.

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Reder, Sabine, Marion Riffelmann, Christian Becker, and Carl Heinz Wirsing von König. "Measuring Immunoglobulin G Antibodies to Tetanus Toxin, Diphtheria Toxin, and Pertussis Toxin with Single-Antigen Enzyme-Linked Immunosorbent Assays and a Bead-Based Multiplex Assay." Clinical and Vaccine Immunology 15, no. 5 (2008): 744–49. http://dx.doi.org/10.1128/cvi.00225-07.

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ABSTRACT Bead-based assay systems offer the possibility of measuring several specific antibodies in one sample simultaneously. This study evaluated a vaccine panel of a multianalyte system that measures antibodies to tetanus toxin, diphtheria toxin, and pertussis toxin (PT) from Bordetella pertussis. The antibody concentrations of human immunoglobulin G (IgG) to PT, tetanus toxin, and diphtheria toxin were measured in 123 serum pairs (total of 246 sera) from a vaccine study. The multianalyte bead assay was compared to a standardized in-house IgG- anti-PT enzyme-linked immunosorbent assay (ELISA) of the German reference laboratory for bordetellae, as well as to various commercially available ELISAs for anti-PT IgG, anti-tetanus IgG, and anti-diphtheria IgG. The results of the multiplex assay regarding the antibodies against diphtheria toxin compared favorably with a regression coefficient of 0.938 for values obtained with an ELISA from the same manufacturer used as a reference. Similarly, antibodies to tetanus toxin showed a correlation of 0.910 between the reference ELISA and the multianalyte assay. A correlation coefficient of 0.905 was found when an “in-house” IgG anti-PT and the multiplex assay were compared. Compared to single ELISA systems from two other manufacturers, the multiplex assay performed similarly well or better. The multianalyte assay system was a robust system with fast and accurate results, analyzing three parameters simultaneously in one sample. The system was well suited to quantitatively determine relevant vaccine induced antibodies compared to in-house and commercially available single-antigen ELISA systems.

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Pierce, E. J., M. D. Davison, R. G. Parton, W. H. Habig, and D. R. Critchley. "Characterization of tetanus toxin binding to rat brain membranes. Evidence for a high-affinity proteinase-sensitive receptor." Biochemical Journal 236, no. 3 (1986): 845–52. http://dx.doi.org/10.1042/bj2360845.

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Binding of 125I-labelled tetanus toxin to rat brain membranes in 25 mM-Tris/acetate, pH 6.0, was saturable and there was a single class of high-affinity site (KD 0.26-1.14 nM) present in high abundance (Bmax. 0.9-1.89 nmol/mg). The sites were largely resistant to proteolysis and heating but were markedly sensitive to neuraminidase. Trisialogangliosides were effective inhibitors of toxin binding (IC50 10 nM) and trisialogangliosides inserted into membranes lacking a toxin receptor were able to bind toxin with high affinity (KD 2.6 nM). The results are consistent with previous studies and the hypothesis that di- and trisialogangliosides act as the primary receptor for tetanus toxin under these conditions. In contrast, when toxin binding was assayed in Krebs-Ringer buffer, pH 7.4, binding was greatly reduced, was non-saturable and competition binding studies showed evidence for a small number of high-affinity sites (KD 0.42 nM, Bmax. 0.90 pmol/mg) and a larger number of low-affinity sites (KD 146 nM, Bmax. 179 pmol/mg). Treatment of membranes with proteinases, heat, and neuraminidase markedly reduced binding. Trisialogangliosides were poor inhibitors of toxin binding (IC50 11.0 microM), and trisialogangliosides inserted into membranes bound toxin with low affinity. The results suggest that in physiological buffers tetanus toxin binds with high affinity to a protein receptor, and that gangliosides represent only a low-affinity site.

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Lukić, Ivana, Emilija Marinković, Ana Filipović, et al. "Key protection factors against tetanus: Anti-tetanus toxin antibody affinity and its ability to prevent tetanus toxin – ganglioside interaction." Toxicon 103 (September 2015): 135–44. http://dx.doi.org/10.1016/j.toxicon.2015.06.025.

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Valmori, D., A. Pessi, E. Bianchi, and G. Corradin. "Use of human universally antigenic tetanus toxin T cell epitopes as carriers for human vaccination." Journal of Immunology 149, no. 2 (1992): 717–21. http://dx.doi.org/10.4049/jimmunol.149.2.717.

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Abstract Synthetic constructs were assembled as multiple Ag peptide systems containing repetitive sequences of Plasmodium falciparum and Plasmodium berghei, the causative agents of human and murine malaria respectively, and two universal human tetanus toxin T cell epitopes 830-843 and 947-967. These constructs were tested for antibody production in mice and for their capacity to stimulate human PBL and tetanus toxin-specific T cell clones. A high antibody titer can be obtained in mice when multiple Ag peptide systems are injected in various adjuvants or in PBS alone. Furthermore, all constructs can activate PBL from every donor tested. However, a variable response was obtained when different clones specific for the two tetanus toxin universal epitopes were used. These constructs may represent possible candidates for a malaria vaccine.

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Jacquier, M. R., F. M. Gabert, C. L. Villiers, and M. G. Colomb. "Disulfide linkage between C3b and tetanus toxin on tetanus toxin-specific EBV-transformed B cells." Journal of Immunology 150, no. 10 (1993): 4253–60. http://dx.doi.org/10.4049/jimmunol.150.10.4253.

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Abstract EBV-transformed B cells specific for tetanus toxin were found to bind C3b in excess over the expected figures based on the number of complement receptors CR1. This was confirmed by analysis of cell extracts by SDS-PAGE giving evidence for C3b-membrane protein complexes that were disrupted upon reduction. Alkylation of C3b-free cysteine abolished formation of these complexes and only a noncovalent binding of C3b to CR1 was observed, which could be inhibited by mAb to CR1. When C3b was incubated with the same cells coated with tetanus toxin bound to their specific membrane Ig, preferential formation of disulfide-bonded complexes between tetanus toxin and C3b was observed. These observations correspond to a novel capacity of C3b to interact covalently through its cysteine 1010 with free SH groups of protein acceptors. One hypothesis is that the disulfide bond formation is catalyzed by a thioredoxin-like protein secreted and expressed on the membrane of EBV-transformed B cells. In the context of Ag processing and presentation by B cells, disulfide binding of chaperone C3b to Ag is likely to persist during transcytosis and to play a significant role in the modulation of the processing.

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Bayart, Caroline, Angélique Mularoni, Nada Hemmani, et al. "Tetanus Toxin Fragment C: Structure, Drug Discovery Research and Production." Pharmaceuticals 15, no. 6 (2022): 756. http://dx.doi.org/10.3390/ph15060756.

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Tetanus toxoid (TTd) plays an important role in the pharmaceutical world, especially in vaccines. The toxoid is obtained after formaldehyde treatment of the tetanus toxin. In parallel, current emphasis in the drug discovery field is put on producing well-defined and safer drugs, explaining the interest in finding new alternative proteins. The tetanus toxin fragment C (TTFC) has been extensively studied both as a neuroprotective agent for central nervous system disorders owing to its neuronal properties and as a carrier protein in vaccines. Indeed, it is derived from a part of the tetanus toxin and, as such, retains its immunogenic properties without being toxic. Moreover, this fragment has been well characterized, and its entire structure is known. Here, we propose a systematic review of TTFC by providing information about its structural features, its properties and its methods of production. We also describe the large uses of TTFC in the field of drug discovery. TTFC can therefore be considered as an attractive alternative to TTd and remarkably offers a wide range of uses, including as a carrier, delivery vector, conjugate, booster, inducer, and neuroprotector.

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Selim, A. M., E. M. Ibrahim, Meshad El, and F. K. Hamouda. "Development of IgY antibodies for control of tetanus." Biotehnologija u stocarstvu 31, no. 1 (2015): 109–22. http://dx.doi.org/10.2298/bah1501109s.

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Tetanus is a cut and often highly fatal infectious disease that affects both human and animals; the disease caused by exotoxin which produced by C. tetani. In the current study, we try to get hyperimmune IgY in chicken egg against tetanus toxin and use it as prophylaxis and therapeutic treatment for tetanus. The obtained IgY titer after inoculation of tetanus toxin in chicken eggs was 1320 limit of flocculation (Lf-eq) after 72 hr. IgY in adose of 4500 Lf-eq can be protect donkey after artificial infection by 1 minimum lethal dose (MLD) of C. tetani. While a dose of 30000 Lf-eq IgY intramuscularly two times daily for 2 injections, with 9500 Limit of flocculation Lf-eq IgY intrathecally in subarachnoid space was 100% curative for a donkey which was challenged with 1 MLD of C. tetani. Furthermore, IgY was evaluated experimentally in comparison with IgG in mice. IgY has equally efficacy to IgG in prophylaxis and treatment of tetanus.

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Ward, Stephen J., Gill Douce, Dayse Figueiredo, Gordon Dougan, and Brendan W. Wren. "Immunogenicity of a Salmonella typhimurium aroA aroD Vaccine Expressing a Nontoxic Domain of Clostridium difficile Toxin A." Infection and Immunity 67, no. 5 (1999): 2145–52. http://dx.doi.org/10.1128/iai.67.5.2145-2152.1999.

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ABSTRACT The C-terminal repeat domain of Clostridium difficiletoxin A harbors toxin-neutralizing epitopes and is considered to be a candidate component of a vaccine against C. difficile-associated disease (CDAD). Fourteen of the 38 C-terminal toxin A repeats (14CDTA) were cloned into pTECH-1 in frame with the immunogenic fragment C of tetanus toxin (TETC) to generate plasmid p56TETC. Expression of the TETC-14CDTA fusion protein was driven from the anaerobically inducible nirB promoter within attenuated Salmonella typhimurium BRD509 (aroA aroD). The TETC-14CDTA fusion protein was purified and shown to bind to known toxin A receptors found on the surface of rabbit erythrocytes. Intranasal (i.n.) and intragastric (i.g.) immunization with 107 and 1010 CFU, respectively, of BRD509(p56TETC) generated significant (P < 0.05) anti-toxin A serum responses after a single dose. Antibody titers were elevated following a boosting dose with either live vaccine or a subcutaneous injection of 0.5 μg of purified 14CDTA protein. Importantly, serum from mice immunized with BRD509(p56TETC) neutralized toxin A cytotoxicity. Both i.n. and i.g. immunizations also generated toxin A-specific immunoglobulin A on the pulmonary and intestinal mucosa, respectively. Intranasal vaccination induced consistently higher serum and mucosal anti-toxin A antibody responses. Significant anti-tetanus toxoid serum and mucosal antibodies were also generated by both immunization routes. The availability of live attenuated Salmonella typhi for human use may allow the development of a multivalent mucosal vaccine against CDAD, tetanus, and typhoid.

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Reidler, Jeffry A., and John P. Robinson. "Two-Dimensional Crystallization of Tetanus Toxin." Proceedings, annual meeting, Electron Microscopy Society of America 43 (August 1985): 528–29. http://dx.doi.org/10.1017/s0424820100119466.

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We have prepared two-dimensional (2D) crystals of tetanus toxin using procedures developed by Uzgiris and Kornberg for the directed production of 2D crystals of monoclonal antibodies at an antigen-phospholipid monolayer interface. The tetanus toxin crystals were formed using a small mole fraction of the natural receptor, GT1, incorporated into phosphatidyl choline monolayers. The crystals formed at low concentration overnight. Two dimensional crystals of this type are particularly useful for structure determination using electron microscopy and computer image refinement. Three dimensional (3D) structural information can be derived from these crystals by computer reconstruction of photographs of toxin crystals taken at different tilt angles. Such 3D reconstructions may help elucidate the mechanism of entry of the enzymatic subunit of toxins into cells, particularly since these crystals form directly on a membrane interface at similar concentrations of ganglioside GT1 to the natural cellular receptors.

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Réthy, Lajos, and Lajos Attila Réthy. "Human lethal dose of tetanus toxin." Lancet 350, no. 9090 (1997): 1518. http://dx.doi.org/10.1016/s0140-6736(05)63939-6.

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Fischer, Peter M., and Merlin E. H. Howden. "Synthetic peptide antigens of tetanus toxin." Molecular Immunology 31, no. 15 (1994): 1141–48. http://dx.doi.org/10.1016/0161-5890(94)90028-0.

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Mesnage, Stéphane, Martine Weber-Levy, Michel Haustant, Michèle Mock, and Agnès Fouet. "Cell Surface-Exposed Tetanus Toxin Fragment C Produced by Recombinant Bacillus anthracis Protects against Tetanus Toxin." Infection and Immunity 67, no. 9 (1999): 4847–50. http://dx.doi.org/10.1128/iai.67.9.4847-4850.1999.

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Bacillus anthracis, the causal agent of anthrax, synthesizes two surface layer (S-layer) proteins, EA1 and Sap, which account for 5 to 10% of total protein and are expressed in vivo. A recombinant B. anthracis strain was constructed by integrating into the chromosome a translational fusion harboring the DNA fragments encoding the cell wall-targeting domain of the S-layer protein EA1 and tetanus toxin fragment C (ToxC). This construct was expressed under the control of the promoter of the S-layer component gene. The hybrid protein was stably expressed on the cell surface of the bacterium. Mice were immunized with bacilli of the corresponding strain, and the hybrid protein elicited a humoral response to ToxC. This immune response was sufficient to protect mice against tetanus toxin challenge. Thus, the strategy developed in this study may make it possible to generate multivalent live veterinary vaccines, using the S-layer protein genes as a cell surface display system.

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Ciriza, Jesús, Marcos García-Ojeda, Inmaculada Martín-Burriel, et al. "Antiapoptotic activity maintenance of Brain Derived Neurotrophic Factor and the C fragment of the tetanus toxin genetic fusion protein." Open Life Sciences 3, no. 2 (2008): 105–12. http://dx.doi.org/10.2478/s11535-008-0011-z.

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AbstractNeurotrophic factors have been widely suggested as a treatment for multiple diseases including motorneuron pathologies, like Amyotrophic Lateral Sclerosis. However, clinical trials in which growth factors have been systematically administered to Amyotrophic Lateral Sclerosis patients have not been effective, owing in part to the short half-life of these factors and their low concentrations at target sites. A possible strategy is the use of the atoxic C fragment of the tetanus toxin as a neurotrophic factor carrier to the motorneurons. The activity of trophic factors should be tested because their genetic fusion to proteins could alter their folding and conformation, thus undermining their neuroprotective properties. For this purpose, in this paper we explored the Brain Derived Neurotrophic Factor (BDNF) activity maintenance after genetic fusion with the C fragment of the tetanus toxin. We demonstrated that BDNF fused with the C fragment of the tetanus toxin induces the neuronal survival Akt kinase pathway in mouse cortical culture neurons and maintains its antiapoptotic neuronal activity in Neuro2A cells.

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Rossetto, O., G. Schiavo, P. Polverino de Laureto, S. Fabbiani, and C. Montecucco. "Surface topography of histidine residues of tetanus toxin probed by immobilized-metal-ion affinity chromatography." Biochemical Journal 285, no. 1 (1992): 9–12. http://dx.doi.org/10.1042/bj2850009.

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Tetanus toxin contains 14 histidine residues: six of them are localized in the light chain (L), one is present in the N-terminal half of the heavy chain (HN) and the remaining seven histidines are localized in the C-terminal half of the heavy chain (Hc). Using immobilized-metal-ion affinity chromatography with Chelating Superose-Zn(II), we show that histidines of Hc are exposed to the protein surface and are responsible for the binding of tetanus toxin and of Hc to the immobilized metal. The histidines of the L chain are not available for co-ordination of matrix-bound Zn2+; however, two of them and three of the histidines of fragment Hc are accessible to diethyl pyrocarbonate. Chromatography on Superose-Zn(II) is also shown to be a simple and efficient method for the rapid isolation of tetanus toxin and of its Hc fragment, which can be extended to the botulinum neurotoxins.

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Yu, Rui, Chong Ji, Junjie Xu, et al. "The Immunogenicity of the C Fragment of Tetanus Neurotoxin in Production of Tetanus Antitoxin." BioMed Research International 2018 (December 31, 2018): 1–9. http://dx.doi.org/10.1155/2018/6057348.

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The demand of tetanus antitoxin (TAT) as tetanus treatment in developing and underdeveloped countries is still great since it is relatively easy to achieve and affordable. However, there are still issues in the preparation of highly effective TAT with tetanus toxoid (TT) as the immunogen. The tetanus toxin native C-fragment (TeNT-Hc) retains many properties and it is a very promising candidate for the development of tetanus human vaccine. In this study, we tested the immunogenicity of TeNT-Hc in the preparation of tetanus antibodies, by TeNT-Hc alone or in different combinations with TT. The antibody titers and components in horse serum or plasma in different groups were analyzed and compared with those immunized by the conventional TT and it showed comparability with the results of traditional methods. The plasma efficacy and in vivo tetanus toxin neutralization were also tested. After two stages of immunizations, the average potency in plasma of all groups reached more than 1,000 IU / mL except that in group 4. In group 5, the first two basic immunizations with TT and the subsequent immunizations with TeNT-Hc, it showed slightly higher antibody titers and potency. This study demonstrated that TeNT-Hc is a safe, effective, and yet easy-to-produce low-cost immunogen and suitable for TT replacement in tetanus antitoxin production.

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Popoff, Michel R. "Tetanus in animals." Journal of Veterinary Diagnostic Investigation 32, no. 2 (2020): 184–91. http://dx.doi.org/10.1177/1040638720906814.

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Tetanus is a neurologic disease of humans and animals characterized by spastic paralysis. Tetanus is caused by tetanus toxin (TeNT) produced by Clostridium tetani, an environmental soilborne, gram-positive, sporulating bacterium. The disease most often results from wound contamination by soil containing C. tetani spores. Horses, sheep, and humans are highly sensitive to TeNT, whereas cattle, dogs, and cats are more resistant. The diagnosis of tetanus is mainly based on the characteristic clinical signs. Identification of C. tetani at the wound site is often difficult.

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Möller, Jens, Max Edmund Kraner, and Andreas Burkovski. "More than a Toxin: Protein Inventory of Clostridium tetani Toxoid Vaccines." Proteomes 7, no. 2 (2019): 15. http://dx.doi.org/10.3390/proteomes7020015.

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Clostridium tetani is the etiological agent of tetanus, a life-threatening bacterial infection. The most efficient protection strategy against tetanus is a vaccination with the C. tetani neurotoxin, which is inactivated by formaldehyde-crosslinking. Since we assumed that besides the tetanus toxin, other proteins of C. tetani may also be present in toxoid preparations, we analyzed commercially available vaccines from different countries in respect to their protein content using mass spectrometry. In total 991 proteins could be identified in all five analyzed vaccines, 206 proteins were common in all analyzed vaccines and 54 proteins from the 206 proteins were potential antigens. The additionally present proteins may contribute at least partially to protection against C. tetani infection by supporting the function of the vaccine against the devastating effects of the tetanus toxin indirectly. Two different label-free protein quantification methods were applied for an estimation of protein contents. Similar results were obtained with a Total Protein Approach (TPA)-based method and Protein Discoverer 2.2 software package based on the minora algorithm. Depending on the tetanus toxoid vaccine and the quantification method used, tetanus neurotoxin contributes between 14 and 76 % to the total C. tetani protein content and varying numbers of other C. tetani proteins were detected.

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Gobbur, R. H., P. Jagruthi, Anilkumar Sajjan, and S. S. Kalyanshettar. "An unusual cause for neck rigidity?" IP International Journal of Medical Paediatrics and Oncology 7, no. 3 (2021): 161–63. http://dx.doi.org/10.18231/j.ijmpo.2021.031.

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Otogenic tetanus is a subtype of cephalic tetanus, limited to the head & neck, but can progress to a more generalized form. Caused by the spore-forming bacillus, Clostridium tetani, It produces a potent toxin, tetanospasmin, preventing inhibitory neurotransmitters' release, hence causing rigidity.

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Duc, Le H., Huynh A. Hong, Neil Fairweather, Ezio Ricca, and Simon M. Cutting. "Bacterial Spores as Vaccine Vehicles." Infection and Immunity 71, no. 5 (2003): 2810–18. http://dx.doi.org/10.1128/iai.71.5.2810-2818.2003.

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ABSTRACT For the first time, bacterial spores have been evaluated as vaccine vehicles. Bacillus subtilis spores displaying the tetanus toxin fragment C (TTFC) antigen were used for oral and intranasal immunization and were shown to generate mucosal and systemic responses in a murine model. TTFC-specific immunoglobulin G titers in serum (determined by enzyme-linked immunosorbent assay) reached significant levels 33 days after oral dosing, while responses against the spore coat proteins were relatively low. Tetanus antitoxin levels were sufficient to protect against an otherwise lethal challenge of tetanus toxin (20 50% lethal doses). The robustness and long-term storage properties of bacterial spores, coupled with simplified genetic manipulation and cost-effective manufacturing, make them particularly attractive vehicles for oral and intranasal vaccination.

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Andrade, Luiz Augusto F., and Sonia Maria D. Brucki. "Botulinum toxin A for trismus in cephalic tetanus." Arquivos de Neuro-Psiquiatria 52, no. 3 (1994): 410–13. http://dx.doi.org/10.1590/s0004-282x1994000300021.

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Cephalic tetanus is a localized form of tetanus. As in generalized forms , trismus is a prominent feature of the disease, leading to considerable difficulty in feeding, swallowing of the saliva and mouth hygiene. These difficulties often precede respiratory problems and aspiration bronchopneumonia is a frequent life-threatening complication. Muscle relaxants other than curare drugs may show a limited benefit for relieving trismus. Tetanospasmin, the tetanic neurotoxin, and botulinum toxin share many similarities, having a closely related chemical structure, an origin from related microorganisms (Clostridium tetani and Clostridium botulinum, respectively), and presumably, the same mechanisms of action in the neuron. The difference between the two lies in their peculiar neurospecificity, acting in different neurons. Injection of minute doses of botulinum toxin in the muscles involved in focal dystonias or other localized spastic disorders have proved to be very effective in these conditions. We describe the use of botulinum toxin A in the successful treatment of trismus in a patient suffering from cephalic tetanus. We believe that this form of treatment may be of value in lowering the risk of pulmonary complications in tetanic patients.

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Fabris, Federico, Petra Šoštarić, Ivica Matak, et al. "Detection of VAMP Proteolysis by Tetanus and Botulinum Neurotoxin Type B In Vivo with a Cleavage-Specific Antibody." International Journal of Molecular Sciences 23, no. 8 (2022): 4355. http://dx.doi.org/10.3390/ijms23084355.

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Tetanus and Botulinum type B neurotoxins are bacterial metalloproteases that specifically cleave the vesicle-associated membrane protein VAMP at an identical peptide bond, resulting in inhibition of neuroexocytosis. The minute amounts of these neurotoxins commonly used in experimental animals are not detectable, nor is detection of their VAMP substrate sensitive enough. The immune detection of the cleaved substrate is much more sensitive, as we have previously shown for botulinum neurotoxin type A. Here, we describe the production in rabbit of a polyclonal antibody raised versus a peptide encompassing the 13 residues C-terminal with respect to the neurotoxin cleavage site. The antibody was affinity purified and found to recognize, with high specificity and selectivity, the novel N-terminus of VAMP that becomes exposed after cleavage by tetanus toxin and botulinum toxin type B. This antibody recognizes the neoepitope not only in native and denatured VAMP but also in cultured neurons and in neurons in vivo in neurotoxin-treated mice or rats, suggesting the great potential of this novel tool to elucidate tetanus and botulinum B toxin activity in vivo.

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Chen, Inês, Theresa M. Finn, Liu Yanqing, Qi Guoming, Rino Rappuoli, and Mariagrazia Pizza. "A Recombinant Live Attenuated Strain of Vibrio cholerae Induces Immunity against Tetanus Toxin andBordetella pertussis Tracheal Colonization Factor." Infection and Immunity 66, no. 4 (1998): 1648–53. http://dx.doi.org/10.1128/iai.66.4.1648-1653.1998.

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ABSTRACT An attenuated strain of Vibrio cholerae was used as a carrier for the expression of heterologous antigens such as fragment C from tetanus toxin (TetC) and tracheal colonization factor fromBordetella pertussis (Tcf). In vitro, high levels of protein were obtained when the Escherichia coli nirBpromoter was used and the bacteria were grown with low aeration. Intranasal immunization of mice with IEM101 expressing TetC elicited serum vibriocidal activity and induced antibodies against tetanus toxin which were protective against lethal challenge with 10 times the 50% lethal dose of tetanus toxin. Bacterial viability was essential for the induction of anti-TetC antibodies. Intranasal administration of IEM101 expressing Tcf induced a significant reduction in bacterial colonization of the tracheas of mice challenged with wild-type B. pertussis. These data are in agreement with the putative role of Tcf in Bordetellatracheal colonization. In conclusion, we have demonstrated thatV. cholerae may be used as a live vector to deliver heterologous antigens in vivo and that protection to both systemic and local challenge may be achieved.

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Demotz, S., P. M. Matricardi, C. Irle, P. Panina, A. Lanzavecchia, and G. Corradin. "Processing of tetanus toxin by human antigen-presenting cells. Evidence for donor and epitope-specific processing pathways." Journal of Immunology 143, no. 12 (1989): 3881–86. http://dx.doi.org/10.4049/jimmunol.143.12.3881.

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Abstract Human T cell clones specific for epitopes 830-843 and 947-967 of tetanus toxin can be differentially activated in vitro when APC (PBL or LCL) from different donors are pulsed with tetanus toxin. Although PBL tested do not seem to exhibit substantial differences in the number of precursor T cells specific for these epitopes, APC from the same donors activate clone KT-2 specific for peptide 830-843 but not clone KT-30 specific for peptide 947-967. These APC express the proper restriction element because they can present the corresponding synthetic peptides. The failure to present a particular epitope might, however, be explained by the absence or presence of a protease(s) required for Ag presentation that may vary for different epitopes. Indeed, the protease inhibitor leupeptin was found to inhibit activation of KT-2 but not KT-30 T cell clone by the KK.35 B cell line normally capable of presenting either epitope. In summary, these data suggest that tetanus toxin processing and epitope formation by APC is distinct in different donors and for different epitopes.

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Zanetti, Giulia, Andrea Mattarei, Florigio Lista, Ornella Rossetto, Cesare Montecucco, and Marco Pirazzini. "Novel Small Molecule Inhibitors That Prevent the Neuroparalysis of Tetanus Neurotoxin." Pharmaceuticals 14, no. 11 (2021): 1134. http://dx.doi.org/10.3390/ph14111134.

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Tetanus neurotoxin (TeNT) is a protein exotoxin produced by Clostridium tetani that causes the deadly spastic neuroparalysis of tetanus. It consists of a metalloprotease light chain and of a heavy chain linked via a disulphide bond. TeNT binds to the neuromuscular junction (NMJ) and it is retro-axonally transported into vesicular compartments to the spinal cord, where it is released and taken up by inhibitory interneuron. Therein, the catalytic subunit is translocated into the cytoplasm where it cleaves its target protein VAMP-1/2 with consequent blockage of the release of inhibitory neurotransmitters. Vaccination with formaldehyde inactivated TeNT prevents the disease, but tetanus is still present in countries where vaccination coverage is partial. Here, we show that small molecule inhibitors interfering with TeNT trafficking or with the reduction of the interchain disulphide bond block the activity of the toxin in neuronal cultures and attenuate tetanus symptoms in vivo. These findings are relevant for the development of therapeutics against tetanus based on the inhibition of toxin molecules that are being retro-transported to or are already within the spinal cord and are, thus, not accessible to anti-TeNT immunoglobulins.

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Norton, P. M., J. M. Wells, H. W. G. Brown, A. M. Macpherson, and R. W. F. Le Page. "Protection against tetanus toxin in mice nasally immunized with recombinant Lactococcus lactis expressing tetanus toxin fragment C." Vaccine 15, no. 6-7 (1997): 616–19. http://dx.doi.org/10.1016/s0264-410x(96)00241-1.

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Cavaillon, Jean-Marc. "From Bacterial Poisons to Toxins: The Early Works of Pasteurians." Toxins 14, no. 11 (2022): 759. http://dx.doi.org/10.3390/toxins14110759.

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We review some of the precursor works of the Pasteurians in the field of bacterial toxins. The word “toxin” was coined in 1888 by Ludwig Brieger to qualify different types of poison released by bacteria. Pasteur had identified the bacteria as the cause of putrefaction but never used the word toxin. In 1888, Émile Roux and Alexandre Yersin were the first to demonstrate that the bacteria causing diphtheria was releasing a deadly toxin. In 1923, Gaston Ramon treated that toxin with formalin and heat, resulting in the concept of “anatoxin” as a mean of vaccination. A similar approach was performed to obtain the tetanus anatoxin by Pierre Descombey, Christian Zoeller and G. Ramon. On his side, Elie Metchnikoff also studied the tetanus toxin and investigated the cholera toxin. His colleague from Odessa, Nikolaï GamaleÏa who was expected to join Institut Pasteur, wrote the first book on bacterial poisons while other Pasteurians such as Etienne Burnet, Maurice Nicolle, Emile Césari, and Constant Jouan wrote books on toxins. Concerning the endotoxins, Alexandre Besredka obtained the first immune antiserum against lipopolysaccharide, and André Boivin characterized the biochemical nature of the endotoxins in a work initiated with Lydia Mesrobeanu in Bucharest.

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Brossier, Fabien, Martine Weber-Levy, Michèle Mock, and Jean-Claude Sirard. "Protective Antigen-Mediated Antibody Response against a Heterologous Protein Produced In Vivo by Bacillus anthracis." Infection and Immunity 68, no. 10 (2000): 5731–34. http://dx.doi.org/10.1128/iai.68.10.5731-5734.2000.

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ABSTRACT Bacillus anthracis secretes a lethal toxin composed of two proteins, the lethal factor (LF) and the protective antigen (PA), which interact within the host or in vitro at the surfaces of eukaryotic cells. Immunization with attenuated B. anthracisstrains induces an antibody response against PA and LF. The LF-specific response is potentiated by the binding of LF to PA. In this study, we investigated the capacity of PA to increase the antibody response against a foreign antigen. We constructed a chimeric gene encoding the PA-binding part of LF (LF254) fused to the C fragment of tetanus toxin (ToxC). The construct was introduced by allelic exchange into the locus encoding LF. Two recombinant B. anthracis strains secreting the hybrid protein LF254-ToxC were generated, one in a PA-producing background and the other in a PA-deficient background. Mice were immunized with spores of the strains, and the humoral response and protection against tetanus toxin were assessed. The B. anthracis strain producing both PA and LF254-ToxC induced significantly higher antibody titers and provided better protection against a lethal challenge with tetanus toxin than did its PA-deficient counterpart. Thus, PA is able to potentiate protective immunity against a heterologous antigen, demonstrating the potential of B. anthracis recombinant strains for use as live vaccine vehicles.

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Ahaduzzaman, Md. "Updates on tetanus toxin: A fundamental approach." Journal of Advanced Veterinary and Animal Research 2, no. 1 (2015): 23. http://dx.doi.org/10.5455/javar.2015.b54.

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Williamson, Lura C., Karen E. Bateman, Julianne C. M. Clifford, and Elaine A. Neale. "Neuronal Sensitivity to Tetanus Toxin Requires Gangliosides." Journal of Biological Chemistry 274, no. 35 (1999): 25173–80. http://dx.doi.org/10.1074/jbc.274.35.25173.

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Chen, Chen, Michael R. Baldwin, and Joseph T. Barbieri. "Molecular Basis for Tetanus Toxin Coreceptor Interactions†." Biochemistry 47, no. 27 (2008): 7179–86. http://dx.doi.org/10.1021/bi800640y.

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Gaber, Tarek A.-Z. K., and Sailaja Mannemela. "Botulinum Toxin for Muscle Spasm after Tetanus." Journal of the Royal Society of Medicine 98, no. 2 (2005): 63. http://dx.doi.org/10.1177/014107680509800207.

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Najib, Abderrahim, Patricia Pelliccioni, Carles Gil, and José Aguilera. "Serotonin transporter phosphorylation modulated by tetanus toxin." FEBS Letters 486, no. 2 (2000): 136–42. http://dx.doi.org/10.1016/s0014-5793(00)02294-8.

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