Reversion of Toxicity of Diphtheria Toxoid

Akama, Kiyoto; Kameyama, Shoichi; Otani, Sho; Sadahiro, Seiji; Murata, Ryosuke

doi:10.7883/yoken1952.24.183

Cited by 18 publications

(10 citation statements)

References 5 publications

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“…Although the latest epidemic (1955)(1956)(1957)(1958)(1959)(1960) was confirmed bacteriologically, isolation of the causative organisms from reported cases has been rare recently as pointed out by Mizuhara et al (1966) and Akama (1975). These authors isolated Streptococci and other organisms from the lesion on the throat of the patients clinically diagnosed as diphtheria.…”

Section: -1976mentioning

confidence: 99%

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Immunization Against Diphtheria in Japan

Murata

1981

JJMSB

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Section: -1976mentioning

confidence: 99%

“…Test for the reversal o f toxicity was introduced in 1970 (Akama et al, 1971) Igarashi, 1956 andMiyamura, 1976).…”

Section: -1976mentioning

confidence: 99%

Immunization Against Diphtheria in Japan

Murata

1981

JJMSB

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“…The detoxification of highly purified toxin proteins using formaldehyde alone has two well-recognized limitations. First, the chemical toxoiding results in polymerization and aggregation due to the formation of methylene bridges among toxoid proteins [1,32,91]. Second, the resultant toxoid can reverse into a partially toxic state as time goes by [1,32,91].…”

Section: Conventional Production Platform: Chemical Detoxification Ofmentioning

confidence: 99%

“…First, the chemical toxoiding results in polymerization and aggregation due to the formation of methylene bridges among toxoid proteins [1,32,91]. Second, the resultant toxoid can reverse into a partially toxic state as time goes by [1,32,91]. After a long search by many scientists for ways to prevent this toxoid aggregation, in 1962 Linggood and colleagues found that toxoiding purified diphtheria toxin using the combination of formaldehyde and lysine not only prevents the synthesis of any toxoid aggregates but also produces a soluble diphtheria toxoid that does not revert into toxin over time [1,32,91].…”

Section: Conventional Production Platform: Chemical Detoxification Ofmentioning

confidence: 99%

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The Evolution and Value of Diphtheria Vaccine

Bae¹

2011

KSBB Journal

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1) This review article provides an overview of the evolution of diphtheria vaccine, its value and its future. Diphtheria is an infectious illness caused by diphtheria toxin produced by pathogenic strains of Corynebacterium diphtheriae. It is characterized by a sore throat with membrane formation due to local tissue necrosis, which can lead to fatal airway obstruction; neural and cardiac damage are other common complications. Diphtheria vaccine was first brought to market in the 1920s, following the discovery that diphtheria toxin can be detoxified using formalin. However, conventional formalin-inactivated toxoid vaccines have some fundamental limitations. Innovative technologies and approaches with the potential to overcome these limitations are discussed in this paper. These include genetic inactivation of diphtheria toxoid, innovative vaccine delivery systems, new adjuvants (both TLRindependent and TLR-dependent adjuvants), and heat-and freeze-stable agents, as well as novel platforms for producing improved conventional vaccine, DNA vaccine, transcutaneous (microneedle-mediated) vaccine, oral vaccine and edible vaccine expressed in transgenic plants. These innovations target improvements in vaccine quality (efficacy, safety, stability and consistency), ease of use and/or thermal stability. Their successful development and use should help to increase global diphtheria vaccine coverage.

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Ion-Exchange Chromatography to Analyze Components of a Clostridium difficile Vaccine

Rustandi

Wang

Lancaster³

et al. 2016

Methods in Molecular Biology

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Ion-exchange (IEX) chromatography is one of many separation techniques that can be employed to analyze proteins. The separation mechanism is based on a reversible interaction between charged amino acids of a protein to the charged ligands attached to a column at a given pH. This interaction depends on both the pI and conformation of the protein being analyzed. The proteins are eluted by increasing the salt concentration or pH gradient. Here we describe the use of this technique to characterize the charge variant heterogeneities and to monitor stability of four protein antigen components of a Clostridium difficile vaccine. Furthermore, the IEX technique can be used to monitor reversion to toxicity for formaldehyde-treated Clostridium difficile toxins.

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Reversion of Toxicity of Diphtheria Toxoid

Cited by 18 publications

References 5 publications

Immunization Against Diphtheria in Japan

Immunization Against Diphtheria in Japan

The Evolution and Value of Diphtheria Vaccine

Ion-Exchange Chromatography to Analyze Components of a Clostridium difficile Vaccine

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