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Journal articles on the topic 'Toxoid'

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Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Ruan, Xiaosai, Donald C. Robertson, James P. Nataro, John D. Clements, and Weiping Zhang. "Characterization of Heat-Stable (STa) Toxoids of Enterotoxigenic Escherichia coli Fused to Double Mutant Heat-Labile Toxin Peptide in Inducing Neutralizing Anti-STa Antibodies." Infection and Immunity 82, no. 5 (February 18, 2014): 1823–32. http://dx.doi.org/10.1128/iai.01394-13.

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ABSTRACTA long-standing challenge in developing vaccines against enterotoxigenicEscherichia coli(ETEC), the most common bacteria causing diarrhea in children of developing countries and travelers to these countries, is to protect against heat-stable toxin type Ib (STa or hSTa). STa and heat-labile toxin (LT) are virulence determinants in ETEC diarrhea. LT antigens are often used in vaccine development, but STa has not been included because of its poor immunogenicity and potent toxicity. Toxic STa is not safe for vaccines, but only STa possessing toxicity is believed to be able to induce neutralizing antibodies. However, recent studies demonstrated that nontoxic STa derivatives (toxoids), after being fused to an LT protein, induced neutralizing antibodies and suggested that different STa toxoids fused to an LT protein might exhibit different STa antigenic propensity. In this study, we selected 14 STa toxoids from a mini-STa toxoid library based on toxicity reduction and reactivity to anti-native STa antibodies, and genetically fused each toxoid to a monomeric double mutant LT (dmLT) peptide for 14 STa-toxoid-dmLT toxoid fusions. These toxoid fusions were used to immunize mice and were characterized for induction of anti-STa antibody response. The results showed that different STa toxoids (in fusions) varied greatly in anti-STa antigenicity. Among them, STaN12S, STaN12T, and STaA14Hwere the top toxoids in inducing anti-STa antibodies.In vitroneutralization assays indicated that antibodies induced by the 3×STaN12S-dmLT fusion antigen exhibited the greatest neutralizing activity against STa toxin. These results suggested 3×STaN12S-dmLT is a preferred fusion antigen to induce an anti-STa antibody response and provided long-awaited information for effective ETEC vaccine development.

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2

Zhang, Weiping, Chengxian Zhang, David H. Francis, Ying Fang, David Knudsen, James P. Nataro, and Donald C. Robertson. "Genetic Fusions of Heat-Labile (LT) and Heat-Stable (ST) Toxoids of Porcine Enterotoxigenic Escherichia coli Elicit Neutralizing Anti-LT and Anti-STa antibodies." Infection and Immunity 78, no. 1 (October 26, 2009): 316–25. http://dx.doi.org/10.1128/iai.00497-09.

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ABSTRACT Enterotoxigenic Escherichia coli (ETEC) strains are a major cause of diarrheal disease in humans and farm animals. E. coli fimbriae, or colonization factor antigens (CFAs), and enterotoxins, including heat-labile enterotoxins (LT) and heat-stable enterotoxins (ST), are the key virulence factors in ETEC diarrhea. Unlike fimbriae or LT, STa has not often been included as an antigen in development of vaccines against ETEC diarrhea because of its poor immunogenicity. STa becomes immunogenic only after being coupled with a strongly immunogenic carrier protein. However, native or shorter STa antigens either had to retain toxic activity in order to become antigenic or elicited anti-STa antibodies that were not sufficiently protective. In this study, we genetically mutated the porcine LT (pLT) gene for a pLT192(R→G) toxoid and the porcine STa (pSTa) gene for three full-length pSTa toxoids [STa11(N→K), STa12(P→F), and STa13(A→Q)] and used the full-length pLT192 as an adjuvant to carry the pSTa toxoid for pLT192:pSTa-toxoid fusion antigens. Rabbits immunized with pLT192:pSTa12 or pLT192:pSTa13 fusion protein developed high titers of anti-LT and anti-STa antibodies. Furthermore, rabbit antiserum and antifecal antibodies were able to neutralize purified cholera toxin (CT) and STa toxin. In addition, preliminary data suggested that suckling piglets born by a sow immunized with the pLT192:pSTa13 fusion antigen were protected when challenged with an STa-positive ETEC strain. This study demonstrated that pSTa toxoids are antigenic when fused with a pLT toxoid and that the elicited anti-LT and anti-STa antibodies were protective. This fusion strategy could provide instructive information to develop effective toxoid vaccines against ETEC-associated diarrhea in animals and humans.

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3

Rahman M, S., K. Baek B, T. Hong S, and H. Lee J. "Antibody responses in buffalos immunized with Clostridium perfringens beta and epsilon toxoids." Veterinární Medicína 46, No. 9–10 (January 1, 2001): 241–43. http://dx.doi.org/10.17221/7886-vetmed.

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The antibody responses to toxoids were measured to investigate whether Clostridium perfringens beta and epsilon toxoids induced protective humoral immune responses in buffalos. Total of 24 buffalos were divided into 4 groups (n = 6), beta toxoid, epsilon toxoid, combination and control groups. These buffalo groups were administered each of the designated toxoids. Immunizations in the beta and epsilon toxoid groups induced strong antibody responses. The neutralizing antibody titres from the beta and epsilon toxoid groups were equally log101.2 on day 21 after inoculation whereas there was no antibody titre detected from the control group. A statistically significant (P < 0.01) increase in antibody titre was observed from day 0 to day 14 and 21 after inoculation. The antibody production did not vary significantly due to day of inoculation and toxoid interactions.

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4

Keller, James E. "Characterization of New Formalin-Detoxified Botulinum Neurotoxin Toxoids." Clinical and Vaccine Immunology 15, no. 9 (July 30, 2008): 1374–79. http://dx.doi.org/10.1128/cvi.00117-08.

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ABSTRACT Antigenicities of several formalin-detoxified botulinum neurotoxin preparations were measured by inhibition and sandwich enzyme-linked immunosorbent assay (ELISA), and immunogenicity was studied in mice. The toxoids were derived primarily from the serotype A 150-kDa neurotoxin protein, while one toxoid was derived from the naturally occurring 900-kDa toxin-hemagglutinin complex. Antigenicity was severely compromised in two commercially available toxoids. A variety of new toxoids were synthesized in-house by optimizing formaldehyde reaction conditions. Three of the resulting toxoids were found to be antigenically identical to the native toxin, as measured by inhibition ELISA, in spite of showing a reduction of toxicity by more than 100,000-fold. Sandwich ELISAs indicated that the in-house toxoids were two- to threefold less antigenic than the neurotoxin compared to commercial toxoids, which were about 100-fold less antigenic. Mice were immunized twice, on day 0 and day 14. By day 28, relatively high toxin-specific immunoglobulin G (IgG) titers were detected in animals that had received any of the in-house toxoids, with greater than 99% being IgG1 and the remainder being IgG2. These immunized mice remained asymptomatic after being challenged with 50 to 1,000,000 50% lethal dose (LD50) units of the 900-kDa neurotoxin. In contrast, animals immunized with several different batches of commercially available toxoids did not develop measurable toxin-specific antibody titers. However, these mice survived neurotoxin challenges with 2 LD50 units but died when challenged with 6 LD50 units. Neutralizing titers measured from pools of sera generated with the in-house toxoid preparations ranged from 2.5 to 5 U/ml. In terms of predicting immunogenicity, inhibition ELISAs comparing each formalin toxoid to the parent toxin provided good insight for screening the new toxoids as well as for estimating their relative in vivo potencies. Inhibition ELISA data indicate that those toxoids that most closely resemble the native toxin are highly immunogenic and protective. The superior quality of these new toxoids makes them useful tools for continued use in ELISA development and for antitoxin production.

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5

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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6

Griffiths, G. D., C. D. Lindsay, A. C. Allenby, S. C. Bailey, J. W. Scawin, P. Rice, and D. G. Upshall. "Protection against inhalation toxicity of ricin and abrin by immunisation." Human & Experimental Toxicology 14, no. 2 (February 1995): 155–64. http://dx.doi.org/10.1177/096032719501400201.

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1 Abrin and ricin are highly toxic plant proteins which are very similar in structure and function and inhibit protein synthesis in eukaryotes. 2 Rats have been immunised against either toxin using formaldehyde-toxoids by three subcutaneous injections at intervals of 3 weeks. For abrin, serum titres in 14 out of 15 rats were raised to between 1 : 12800 and 1 : 51200 after two injections, 6 weeks from the start of the experiment. Titres of between 1 : 256 and 1 : 1024 were also measured in lung washes after challenge with active abrin toxin. 3 The three major antibody classes, IgG, IgM and IgA were present in the immune sera but IgG and IgA only were detected in lung washes. The proportion of IgA to IgG was higher in the lung fluid than in sera. Rats immunised by abrin toxoid were protected against 5 LCt50's of abrin by inhalation but others exposed to ricin were not. 4 For ricin, serum titres ranged from 1 : 800 to 1 : 25600 after two injections and after a third injection the titre range was the same but population samples were weighted towards the higher titres. All rats immunised with ricin toxoid survived the challenge of 5 LCt50's of ricin toxin by inhalation over the observation period of 28 days post-challenge. 5 Representative immunised rats (abrin toxoid) were taken at various times post-exposure, humanely killed and tissues were examined for pathological changes. It was concluded that an apparently severe lung lesion occurred at a later time than in non-immunised, toxin challenged rats. This damage was not lethal over the experimental observation periods. 6 Immunisation by the sub-cutaneous route therefore protects against lethality from challenge by inhalation of ricin or abrin toxins but does not prevent significant lung damage.

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7

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 1216 (August 2008): 32–33. http://dx.doi.org/10.2165/00128415-200812160-00087.

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8

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 460 (July 1993): 10. http://dx.doi.org/10.2165/00128415-199304600-00049.

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9

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 364 (August 1991): 12. http://dx.doi.org/10.2165/00128415-199103640-00057.

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10

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 518 (September 1994): 11. http://dx.doi.org/10.2165/00128415-199405180-00046.

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11

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 865 (August 2001): 11–12. http://dx.doi.org/10.2165/00128415-200108650-00035.

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12

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 926 (November 2002): 12. http://dx.doi.org/10.2165/00128415-200209260-00034.

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13

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 649 (May 1997): 12. http://dx.doi.org/10.2165/00128415-199706490-00034.

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14

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 661 (July 1997): 11. http://dx.doi.org/10.2165/00128415-199706610-00032.

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15

Hjerpe, Charles A. "Tetanus Toxoid." Veterinary Clinics of North America: Food Animal Practice 6, no. 1 (March 1990): 231. http://dx.doi.org/10.1016/s0749-0720(15)30920-8.

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16

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 1337 (February 2011): 30. http://dx.doi.org/10.2165/00128415-201113370-00098.

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17

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 387 (February 1992): 8. http://dx.doi.org/10.2165/00128415-199203870-00034.

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18

&NA;. "Tetanus toxoid." Reactions Weekly &NA;, no. 401 (May 1992): 12. http://dx.doi.org/10.2165/00128415-199204010-00056.

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19

Nijland, Reindert, René Heerlien, Leendert W. Hamoen, and Oscar P. Kuipers. "Changing a Single Amino Acid in Clostridium perfringens β-Toxin Affects the Efficiency of Heterologous Secretion by Bacillus subtilis." Applied and Environmental Microbiology 73, no. 5 (January 5, 2007): 1586–93. http://dx.doi.org/10.1128/aem.02356-06.

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ABSTRACT Achieving efficient heterologous protein production and secretion by Bacillus subtilis is an attractive prospect, although often disappointingly low yields are reached. The expression of detoxified Clostridium perfringens β-toxin (β-toxoid) is exemplary for this. Although β-toxin can be efficiently expressed and secreted by Bacillus subtilis, the genetically detoxified, and industrially interesting, β-toxoid variant is difficult to obtain in high amounts. To optimize the expression of this putative vaccine component, we studied the differences in the global gene regulation responses of B. subtilis to overproduction of either β-toxin or β-toxoid by transcriptomics. A clear difference was the upregulation of the CssRS regulon, known to be induced upon secretion stress, when β-toxoid is produced. YkoJ, a protein of unknown function, was also upregulated, and we show that its expression is dependent on cssS. We then focused on the heterologous protein itself and found that the major secretion bottleneck can be traced back to a single amino acid substitution between the β-toxin and the β-toxoid, which results in the rapid degradation of β-toxoid following secretion across the cytoplasmic membrane. In contrast to β-toxin, β-toxoid protein is more prone to degradation directly after secretion, most likely due to poor folding characteristics introduced with point mutations. Our results show that although the host can be adapted in many ways, the intrinsic properties of a heterologous protein can play a decisive role when optimizing heterologous protein production.

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20

Kailasan, Shweta, Thomas Kort, Ipsita Mukherjee, Grant C. Liao, Tulasikumari Kanipakala, Nils Williston, Nader Ganjbaksh, et al. "Rational Design of Toxoid Vaccine Candidates for Staphylococcus aureus Leukocidin AB (LukAB)." Toxins 11, no. 6 (June 14, 2019): 339. http://dx.doi.org/10.3390/toxins11060339.

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Staphylococcus aureus (SA) infections cause high mortality and morbidity in humans. Being central to its pathogenesis, S. aureus thwarts the host defense by secreting a myriad of virulence factors, including bicomponent, pore-forming leukotoxins. While all vaccine development efforts that aimed at achieving opsonophagocytic killing have failed, targeting virulence by toxoid vaccines represents a novel approach to preventing mortality and morbidity that are caused by SA. The recently discovered leukotoxin LukAB kills human phagocytes and monocytes and it is present in all known S. aureus clinical isolates. While using a structure-guided approach, we generated a library of mutations that targeted functional domains within the LukAB heterodimer to identify attenuated toxoids as potential vaccine candidates. The mutants were evaluated based on expression, solubility, yield, biophysical properties, cytotoxicity, and immunogenicity, and several fully attenuated LukAB toxoids that were capable of eliciting high neutralizing antibody titers were identified. Rabbit polyclonal antibodies against the lead toxoid candidate provided potent neutralization of LukAB. While the neutralization of LukAB alone was not sufficient to fully suppress leukotoxicity in supernatants of S. aureus USA300 isolates, a combination of antibodies against LukAB, α-toxin, and Panton-Valentine leukocidin completely neutralized the cytotoxicity of these strains. These data strongly support the inclusion of LukAB toxoids in a multivalent toxoid vaccine for the prevention of S. aureus disease.

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21

Qazi, Omar, Dorothea Sesardic, Robert Tierney, Zahra Söderbäck, Dennis Crane, Barbara Bolgiano, and Neil Fairweather. "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 (August 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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22

Norlin, Gunnar. "PURIFICATION OF DIPHTHERIA TOXIN AND DIPHTHERIA TOXOID." Acta Pathologica Microbiologica Scandinavica 24, no. 5-6 (August 18, 2009): 505–24. http://dx.doi.org/10.1111/j.1699-0463.1947.tb00619.x.

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23

Norlin., Gunnar. "PURIFICATION OF DIPHTHERIA TOXIN AND DIPHTHERIA TOXOID." Acta Pathologica Microbiologica Scandinavica 29, no. 1 (August 17, 2009): 45–56. http://dx.doi.org/10.1111/j.1699-0463.1951.tb00102.x.

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24

Inic-Kanada, Aleksandra, Marijana Stojanovic, Irena Zivkovic, Vladimir Petrusic, and 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, no. 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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25

&NA;. "Tetanus toxoid immunoglobulins." Reactions Weekly &NA;, no. 461 (July 1993): 11. http://dx.doi.org/10.2165/00128415-199304610-00066.

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26

Lleonart-Bellfill, Ramon, Anna Cisteró-Bahima, Maria Teresa Cerdà-Trias, and Alfonso Olivé-Pérez. "Tetanus Toxoid Anaphylaxis." DICP 25, no. 7-8 (July 1991): 870. http://dx.doi.org/10.1177/106002809102500730.

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27

Weisse, M. E. "Tetanus toxoid allergy." JAMA: The Journal of the American Medical Association 264, no. 18 (November 14, 1990): 2448b—2448. http://dx.doi.org/10.1001/jama.264.18.2448b.

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28

BAXBY, DERRICK. "6. The discovery of diphtheria toxoid and the primary and secondary immune response Glenny AT, Südmersen HJ. J Hyg 1921; 20: 176–220." Epidemiology and Infection 133, S1 (October 2005): S21—S22. http://dx.doi.org/10.1017/s0950268805004267.

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The routine title of the long ‘note’ by Glenny and Südmersen reproduced here [1] hides two of the most significant findings in theoretical and applied immunology: a brief description of diphtheria toxoid and a comprehensive account of the primary and secondary immune response. The introduction of antitoxin treatment of diphtheria was heralded, in 1896, without exaggeration as ‘the most important advance of the [19th] Century in the medical treatment of acute infective disease’ [2]. However, there were problems with the standardization and potency of antitoxin. The former was solved by Ehrlich who, in his analysis of toxin–antitoxin interaction, postulated the existence of ‘toxoid’, a non-toxic component of toxin which combined with antitoxin [3]. The latter was solved by the general observation that repeated injections of gradually increased doses of toxin induced increasingly potent antitoxins, an important basis upon which the present paper was founded.

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29

Liu, Mei, Xiaosai Ruan, Chengxian Zhang, Steve R. Lawson, David E. Knudsen, James P. Nataro, Donald C. Robertson, and Weiping Zhang. "Heat-Labile- and Heat-Stable-Toxoid Fusions (LTR192G-STaP13F) of Human Enterotoxigenic Escherichia coli Elicit Neutralizing Antitoxin Antibodies." Infection and Immunity 79, no. 10 (July 25, 2011): 4002–9. http://dx.doi.org/10.1128/iai.00165-11.

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ABSTRACTEnterotoxigenicEscherichia coli(ETEC) strains are a major cause of diarrheal disease in humans and animals. Adhesins and enterotoxins, including heat-labile (LT) and heat-stable (STa) toxins, are the key virulence factors. Antigenic adhesin and LT antigens have been used in developing vaccines against ETEC diarrhea. However, STa has not been included because of its poor immunogenicity and potent toxicity. Our recent study showed that porcine-type STa toxoids became immunogenic and elicited neutralizing anti-STa antibodies after being genetically fused to a full-length porcine-type LT toxoid, LTR192G(W. Zhang et al., Infect. Immun. 78:316-325, 2010). In this study, we mutated human-type LT and STa genes, which are highly homologous to porcine-type toxin genes, for a full-length LT toxoid (LTR192G) and a full-length STa toxoid (STaP13F) and genetically fused them to produce LT192-STa13toxoid fusions. Mice immunized with LT192-STa13fusion antigens developed anti-LT and anti-STa IgG (in serum and feces) and IgA antibodies (in feces). Moreover, secretory IgA antibodies from immunized mice were shown to neutralize STa and cholera toxins in T-84 cells. In addition, we fused the STa13toxoid at the N terminus and C terminus, between the A1 and A2 peptides, and between the A and B subunits of LT192to obtain different fusions in order to explore strategies for enhancing STa immunogenicity. This study demonstrated that human-type LT192-STa13fusions induce neutralizing antitoxin antibodies and provided important information for developing toxoid vaccines against human ETEC diarrhea.

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30

Lee, Seonhyung, Beom-Ku Han, Yang-Hoon Kim, and Ji-Young Ahn. "SpyCatcher-SpyTagged ApxIA Toxoid and the Immune-Modulating Yeast Ghost Shells." Journal of Biomedical Nanotechnology 16, no. 11 (November 1, 2020): 1644–57. http://dx.doi.org/10.1166/jbn.2020.2992.

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Actinobacillus pleuropneumoniaesecretes the hemolytic cytotoxins ApxI, ApxII, ApxIII, and ApxIV, which cause pleurop- neumonia in swine. Of these, ApxI is the most toxic. ApxIA, a repeats-in-toxin toxin-like protein, has strong hemolytic and cytotoxic activities. This study aimed to develop an immune modulator ApxIA toxoid, with a Spytag/Spycatcher pair (SC::ST pair), in yeast ghost shells (YGSs). These YGSs were utilized as ApxIA toxoid delivery platforms for -glucan components that can be recognized by the innate immune system. The SC::ST pair was used to conjugate the ApxIA toxoid to YGSs. The YGS-SC::ST-ToxApxIA was successfully phagocytosed by RAW 264.7 macrophages cells, without any toxicity. Further investigation revealed that YGS-SC::ST-ToxApxIA led to defective immune responses, in addition to increased levels of cytokines IL-1β, TNF-α, and IL-10. A membrane proteomic analysis, to determine preferential major histocompatibility complex binding of ApxIA-derived peptides, was performed and four ApxIA peptides were successfully identified by liquid chromatography with tandem mass spectrometry analysis. The identified peptides may serve as poten- tial vaccine candidates in immunobiology studies of A. pleuropneumoniae. Our results indicate that YGS-SC::ST-ToxApxIA can prevent A. pleuropneumoniae pleuropneumonia (APP) by inducing both humoral and cellular immune responses.

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31

Sato, Hiroko, and Yuji Sato. "Experience with Diphtheria Toxoid–Tetanus Toxoid–Acellular Pertussis Vaccine in Japan." Clinical Infectious Diseases 28, s2 (June 1999): S124—S130. http://dx.doi.org/10.1086/515063.

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32

Falade, S., and O. A. Durojaiye. "THE PROTECTIVE VALUE OF AN AUTOGENOUS BACTERIN AND TOXOID AGAINST EXPERIMENTAL CORYNEBACTERIUM PYOGENES INFECTION IN MICE." Nigerian Journal of Animal Production 11, no. 2 (January 15, 2021): 148–50. http://dx.doi.org/10.51791/njap.v11i2.2544.

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Bacteria and toxin from a borth culture of a porcine strain of Corynebacterium pyogenes were lethal to white Swiss mice within 24th of inoculation. The pyogenic factor was shown to be a component of the bacterial cells and not of the toxin. Mouse protection tests using a formolised bacterin and formolized toxoid conferred protection to experimental challenge. It is suggested that this toxoid may be of value in protecting animals against the natural infection.

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33

Oanh, Thi Kim Nguyen, Viet Khong Nguyen, Henri De Greve, and Bruno Maria Goddeeris. "Protection of Piglets against Edema Disease by Maternal Immunization with Stx2e Toxoid." Infection and Immunity 80, no. 1 (November 14, 2011): 469–73. http://dx.doi.org/10.1128/iai.05539-11.

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ABSTRACTEdema disease (ED) in piglets is caused by Shiga toxin Stx2e-producingEscherichia coli. We show that a genetically disarmed Stx2e toxoid is a safe antigen that generates antiserum protecting piglets against the Stx2e toxin. Immunization of suckling piglets with the Stx2e toxoid was safe, had no adverse effects on growth of the piglets, and resulted in effective prevention of edema disease clinical symptoms after challenge with the Stx2e toxin. Our data showed that maternal immunity against the Stx2e toxoid can be transmitted from the vaccinated sows to the piglets via the colostrum. Very high levels of Stx2e-specific serum antibodies persisted in these piglets until 1 month postweaning, bridging the critical period in which the weaned piglets are most susceptible to edema infection. Challenge with Stx2e toxin resulted in clinical signs of edema disease and death of all control piglets from nonimmunized sows, whereas none of the piglets from immunized sows developed clinical signs of ED.

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Kotloff, Karen L., Steven S. Wasserman, Genevieve A. Losonsky, William Thomas, Richard Nichols, Robert Edelman, Margaret Bridwell, and Thomas P. Monath. "Safety and Immunogenicity of Increasing Doses of aClostridium difficile Toxoid Vaccine Administered to Healthy Adults." Infection and Immunity 69, no. 2 (February 1, 2001): 988–95. http://dx.doi.org/10.1128/iai.69.2.988-995.2001.

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ABSTRACT Clostridium difficile is a major cause of nosocomial diarrhea in industrialized countries. Although most illnesses respond to available therapy, infection can increase morbidity, prolong hospitalization, and produce life-threatening colitis. Vaccines are being explored as an alternative means for protecting high-risk individuals. We assessed the safety, immunogenicity, and dose response of a parenteral vaccine containing C. difficile toxoids A and B. Thirty healthy adults were assigned to receive four spaced inoculations on days 1, 8, 30, and 60 with one of three doses of vaccine (6.25, 25, or 100 μg). At each dose level, subjects were randomized, in a double-blind fashion, to receive either the soluble toxoids (n = 5) or toxoids adsorbed to alum (n = 5). Subjects were monitored for clinical and immunologic responses to vaccination. Vaccination was generally well tolerated, with occasional, usually mild, systemic reactions (abdominal pain, arthralgia, and diarrhea). The most common local reaction, mild arm pain, was reported by all recipients of the toxoid-alum formulation. Nearly all subjects (≥90%) developed vigorous serum antibody responses to both toxins, as measured by immunoglobulin G (IgG) enzyme-linked immunosorbent assay and neutralization of cytotoxicity, whereas fecal IgA increases occurred in approximately 50%. Statistically significant effects of dose and formulation on immunogenicity were not seen, although antibody levels tended to be higher with the alum-adjuvanted formulations and with increasing doses of soluble toxoid. Serum antibody responses among the toxoid-alum group appeared to plateau at 25 μg. We concluded that theC. difficile toxoid vaccine is safe and immunogenic in healthy volunteers. Further development as a prophylactic vaccine or for producing C. difficile hyperimmune globulin is justified.

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Zürcher, M. P., M. Vogel, A. W. Zürcher, M. P. Rudolf, H. Kaufmann, A. B. Lang, S. M. Miescher, and B. M. Stadler. "Protective tetanus toxoid epitopes." Immunology Letters 56 (May 1997): 287. http://dx.doi.org/10.1016/s0165-2478(97)86154-8.

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Bowman, Clive, Stephen Hearing, and Jeremy Bewley. "Tetanus toxoid for adults." Lancet 348, no. 9042 (December 1996): 1664. http://dx.doi.org/10.1016/s0140-6736(05)65736-4.

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Sehgal, R. "Tetanus toxoid for adults." Lancet 349, no. 9051 (February 1997): 573. http://dx.doi.org/10.1016/s0140-6736(97)80123-7.

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Kersten, G., W. Jiskoot, T. Hazendonk, A. Spiekstra, J. Westdijk, and C. Beuvery. "Characterization of Diphtheria Toxoid." Pharmacy and Pharmacology Communications 5, no. 1 (January 1, 1999): 27–31. http://dx.doi.org/10.1211/146080899128734127.

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39

Zürcher, M. "Protective tetanus toxoid epitopes." Immunology Letters 56, no. 1-3 (May 1997): 287. http://dx.doi.org/10.1016/s0165-2478(97)87992-8.

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von König, CH Wirsing, and HJ Schmitt. "Toxoid vaccine for pertussis." Lancet 349, no. 9045 (January 1997): 136. http://dx.doi.org/10.1016/s0140-6736(05)60925-7.

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He, Qiushui, Matti K. Viljanen, Heikki Arvilommi, and Jussi Mertsola. "Toxoid vaccine for pertussis." Lancet 349, no. 9045 (January 1997): 136–37. http://dx.doi.org/10.1016/s0140-6736(05)60926-9.

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Preston, Noel W., and Ruth C. Matthews. "Toxoid vaccine for pertussis." Lancet 349, no. 9045 (January 1997): 137. http://dx.doi.org/10.1016/s0140-6736(05)60927-0.

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43

Schneerson, Rachel, John B. Robbins, John Taranger, Birger Trollfors, and Teresa Lagergård. "Toxoid vaccine for pertussis." Lancet 349, no. 9045 (January 1997): 137–38. http://dx.doi.org/10.1016/s0140-6736(05)60928-2.

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Ludwig, K., M. A. Karmali, C. R. Smith, and M. Petric. "Cross-protection against challenge by intravenousEscherichia coliverocytotoxin 1 (VT1) in rabbits immunized with VT2 toxoid." Canadian Journal of Microbiology 48, no. 1 (January 1, 2002): 99–103. http://dx.doi.org/10.1139/w01-138.

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Rabbits challenged intravenously with Escherichia coli verocytotoxin (VT1, Shiga toxin 1, Stx1) die after developing diarrhea and paralysis, and this outcome can be prevented by pre-immunization with VT1 toxoid. In nonimmune rabbits, intravenously administered125I-VT1 binds to the central nervous system and gastrointestinal tract, whereas in immunized animals, these organs are spared and the toxin localizes in the liver and spleen. In rabbits immunized with either VT1 or VT2 toxoids, both the homologous or heterologous toxins are prevented from binding to target organs. This has lead to the advancement of a hypothesis that cross-protection in vivo can be induced to both toxins by immunization with a toxoid even though these toxins do not exhibit cross-neutralization in vitro. It was shown that rabbits immunized with VT2 were fully protected from the intravenous administration of 10 LD50and 50 LD50of VT1, and this correlated directly with the protection from binding of this toxin to target organs. These findings have important implications on the design of the vaccination strategies to prevent human VT-mediated diseases and also validate the concept of testing for immunity to VT by monitoring the inhibition of binding of the125I-VT to target organs in preference to performing LD50assays.Key words: Escherichia coli, verocytotoxins, immunity, cross-protection.

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TROTT, D. L., M. YANG, J. GONZALEZ, A. E. LARSON, W. H. TEPP, E. A. JOHNSON, and M. E. COOK. "Egg Yolk Antibodies for Detection and Neutralization of Clostridium botulinum Type A Neurotoxin." Journal of Food Protection 72, no. 5 (May 1, 2009): 1005–11. http://dx.doi.org/10.4315/0362-028x-72.5.1005.

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The objective of this research project was to determine the usefulness of an egg antibody platform for producing materials for the detection and neutralization of botulinum type A neurotoxin. Yield estimates for detection and neutralizing antibodies produced using methods described were calculated. Antibody specific to botulinum toxoid A (aToxoid) and toxin A (aBoNT/A) was produced by immunizing hens with botulinum toxoid A (toxoid) followed by increasing amounts of botulinum neurotoxin A (BoNT/A) in Freund incomplete adjuvant. Egg yolks were extracted with polyethylene glycol (PEG) for antibody detection and neutralization experiments. A model aToxoid/toxoid immunoassay using only egg yolk antibody was developed and had a detection limit of 1 pg/ml of toxoid. In an indirect enzyme-linked immunosorbent assay of BoNT/A-specific antibody, the aBoNT/A contained more BoNT/A-specific antibody than did the aToxoid, and aBoNT/A was as effective as commercial rabbit antibody. The aToxoid provided no protection against BoNT/A in a standard mouse neutralization assay; however, 1 mg of PEG-extracted aBoNT/A neutralized 4,000 lethal doses of BoNT/A injected intraperitoneally. Based on these results, we calculated that in 1 month one hen could produce more than 100 liters of antibody detection reagents or enough antibody to neutralize approximately 11.6 million mouse lethal doses of botulinum toxin. Utilization of an egg antibody platform is potentially rapid (28 to 70 days) and scalable to kilogram quantities using current egg production facilities with as few as 1,000 hens.

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Pier, Christina L., William H. Tepp, Marite Bradshaw, Eric A. Johnson, Joseph T. Barbieri, and Michael R. Baldwin. "Recombinant Holotoxoid Vaccine against Botulism." Infection and Immunity 76, no. 1 (October 29, 2007): 437–42. http://dx.doi.org/10.1128/iai.00843-07.

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ABSTRACT The botulinum neurotoxins (BoNT) are the most toxic proteins for humans and designated “Category A Select Agents.” The current vaccine against botulism is in limited supply, and there is a need to develop new vaccine strategies. A recombinant BoNT/A toxoid was produced in Clostridium botulinum that contained a double amino acid substitution, R363A Y365F (termed BoNT/ARYM). BoNT/ARYM was noncatalytic for SNAP25 and nontoxic for mice. Immunization with BoNT/ARYM protected mice from challenge at levels that were similar to chemically inactivated BoNT/A toxoid. BoNT/ARYM elicited an immune response against the light-chain and heavy-chain components of the toxin. Neutralizing anti-BoNT/ARYM sera blocked BoNT toxicity in primary cortical neurons and blocked ganglioside binding by the heavy chain. BoNT/ARYM represents a viable vaccine candidate for a holotoxoid against botulism.

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Oyedeji, Olusola Adetunji, Francis Fadero, Victor Joel-Medewase, Peter Elemile, and Gabriel Ademola Oyedeji. "Trends in neonatal and post-neonatal tetanus admissions at a Nigerian teaching hospital." Journal of Infection in Developing Countries 6, no. 12 (December 15, 2012): 847–53. http://dx.doi.org/10.3855/jidc.2105.

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Introduction: Tetanus accounts for high morbidity and case fatality rates in developing countries. This study therefore aimed to identify reasons for the persistence of this disease. Methodology: Paediatric admissions at Ladoke Akintola University Teaching Hospital between 1 January 2006 and 31 December 2008 diagnosed with tetanus were studied. Data was analyzed with SPSS 18 and statistical significance was set at p < 0.05. Results: Of the total 1,681 paediatric admissions, 30 (1.8%) had tetanus. Of the 878 neonatal admissions, 8 (0.9%) had tetanus, while 22 (2.7%) of the total 803 post-neonatal admissions had tetanus. Neonatal tetanus admissions were significantly higher in 2006 compared to 2007 and 2008 (7 [2.3%] versus 1 [0.2%] [χ2= 7.50, P=0.01]). Of the eight mothers whose neonates had tetanus, seven did not receive tetanus toxoids in pregnancy and five (62.5%) were secondary school dropouts. Post-neonatal tetanus cases admitted in the years 2006, 2007, and 2008 were 4, 12, and 6 children respectively. Most of these 22 children did not receive tetanus toxoid immunization in their first year of life. None of the 22 children received booster doses of tetanus toxoids after their first years of life. Conclusion: Mothers at risk of their babies having tetanus, such as secondary school dropouts, must be identified antenatally and vaccinated with tetanus toxiod. Their babies should also receive good care post-delivery. Completion of routine tetanus toxoid schedule in the first year and booster doses in the post-neonatal age should be ensured.

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Zaragoza, Orellana, Moonen, Moutafis, and Marcellin. "Vaccine Production to Protect Animals Against Pathogenic Clostridia." Toxins 11, no. 9 (September 11, 2019): 525. http://dx.doi.org/10.3390/toxins11090525.

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Clostridium is a broad genus of anaerobic, spore-forming, rod-shaped, Gram-positive bacteria that can be found in different environments all around the world. The genus includes human and animal pathogens that produce potent exotoxins that cause rapid and potentially fatal diseases responsible for countless human casualties and billion-dollar annual loss to the agricultural sector. Diseases include botulism, tetanus, enterotoxemia, gas gangrene, necrotic enteritis, pseudomembranous colitis, blackleg, and black disease, which are caused by pathogenic Clostridium. Due to their ability to sporulate, they cannot be eradicated from the environment. As such, immunization with toxoid or bacterin-toxoid vaccines is the only protective method against infection. Toxins recovered from Clostridium cultures are inactivated to form toxoids, which are then formulated into multivalent vaccines. This review discusses the toxins, diseases, and toxoid production processes of the most common pathogenic Clostridium species, including Clostridium botulinum, Clostridium tetani, Clostridium perfringens, Clostridium chauvoei, Clostridium septicum, Clostridium novyi and Clostridium hemolyticum.

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Macko, Michael B., and Candace E. Powell. "Comparison of the morbidity of tetanus toxoid boosters with tetanus-diphtheria toxoid boosters." Annals of Emergency Medicine 14, no. 1 (January 1985): 33–34. http://dx.doi.org/10.1016/s0196-0644(85)80732-0.

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Mink, ChrisAnna M. "Introduction of Tetanus Toxoid and Reduced Diphtheria Toxoid Vaccines in the United States." Pediatric Infectious Disease Journal 25, no. 4 (April 2006): 363–64. http://dx.doi.org/10.1097/01.inf.0000210479.00996.eb.

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