C. diphtheriae Diphtheria Toxoid Antigen is highly purified Diphtheria Toxin from Corynebacterium diphtheriae, which following the purification process has been detoxified by formaldehyde.
Nature
Native
Tag/Conjugate
Unconjugated
Purity
>1500Lf/mg.PN
Format
Liquid
Buffer
0.01% Ammonium sulfate, pH 7.0
Preservative
None
Storage
Store at 2°C to 8°C
Introduction
Corynebacterium diphtheriae is a gram-positive, nonmotile bacteria found in soil and animal feces. C. diphteriae infect the epithelial cells of the upper respiratory tract from where they produce and secrete a potent toxin. This toxin is absorbed and disseminated through lymph channels and blood to the susceptible tissues of the body.
Antigen Description
Diphtheria is a contagious disease spread by direct physical contact or breathing the aerosolized secretions of infected individuals. Historically quite common, diphtheria has largely been eradicated in industrialized nations through widespread vaccination. In the United States, for example, there were 52 reported cases of diphtheria between 1980 and 2000; between 2000 and 2007, there were only three cases as the diphtheria–pertussis–tetanus (DPT) vaccine is recommended for all school-age children. Boosters of the vaccine are recommended for adults, since the benefits of the vaccine decrease with age without constant re-exposure; they are particularly recommended for those traveling to areas where the disease has not been eradicated.
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Background
Corynebacterium diphtheriae is a Gram-positive bacterium that causes the infectious disease known as diphtheria. One of the key virulence factors produced by C. diphtheriae is the diphtheria toxin. The diphtheria toxin is encoded by a gene called tox, which is carried by a bacteriophage (a virus that infects bacteria) and can be horizontally transferred between different strains of C. diphtheriae. The diphtheria toxin is an A-B toxin, consisting of two main components: the enzymatically active A subunit and the binding B subunit. The B subunit facilitates the binding of the toxin to specific receptors on the surface of target cells, while the A subunit enters the cell and exerts its toxic effects. Once inside the cell, the A subunit of the diphtheria toxin inhibits protein synthesis by modifying a specific component of the host cell's protein synthesis machinery. This disruption of protein synthesis leads to cell death and contributes to the characteristic tissue damage observed in diphtheria infections.
Figure 1. Mechanism of action of diphtheria toxin. (Source: Babar, S. et al., 2017)
The toxoid is created by inactivating the toxin, typically through a process of chemical treatment or genetic modification, while retaining its immunogenic properties. Vaccination with the diphtheria toxoid is the primary method of preventing diphtheria. The toxoid is included in diphtheria-containing vaccines, such as the DTP (Diphtheria, Tetanus, Pertussis) vaccine or DTaP (Diphtheria, Tetanus, acellular Pertussis) vaccine. When administered as part of a vaccine, the diphtheria toxoid stimulates the immune system to produce specific antibodies that can recognize and neutralize the diphtheria toxin. This immune response provides protection against diphtheria infection and its associated complications. In addition to its use in vaccines, the diphtheria toxoid antigen is also employed in diagnostic tests for diphtheria. Serological assays, such as enzyme-linked immunosorbent assays (ELISA), can accurately identify the immune response to the diphtheria toxoid and help confirm or rule out diphtheria infection.
Q: Can you tell us the method you quantify the protein concentration with?
A: Lowry method
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References
Proteomics of diphtheria toxoid vaccines reveals multiple proteins that are immunogenic and may contribute to protection of humans against Corynebacterium diphtheriae
Introduced for mass immunization in the 1920s, vaccines against diphtheria are among the oldest and safest vaccines known. The basic principle of their production is the inactivation of purified diphtheria toxin by formaldehyde cross-linking, which converts the potentially fatal toxin in a completely harmless protein aggregate, which is still immunogenic. Since in addition to diphtheria toxin also other proteins may be secreted by Corynebacterium diphtheriae during cultivation, we assumed that diphtheria toxoid might not be the only component present in the vaccine. To address this question, we established a protocol to reverse formaldehyde cross-linking and carried out mass spectrometric analyses. Different secreted, membrane-associated and cytoplasmic proteins of C. diphtheriae were detected in several vaccine preparations from across the world. Based on these results, bioinformatics and Western blot analyses were applied to characterize if these proteins are immunogenic and may therefore support protection against C. diphtheriae. In frame of this study, we could show that the C. diphtheriae toxoid vaccines induce antibodies against different C. diphtheriae proteins and against diphtheria toxin secreted by Corynebacterium ulcerans, an emerging pathogen which is outnumbering C. diphtheriae as cause of diphtheria-like illness in Western Europe.
Corynebacterium diphtheriae: diphtheria toxin, the tox operon, and its regulation by Fe2+ activation of apo-DtxR
Diphtheria is one of the most well studied of all the bacterial infectious diseases. These milestone studies of toxigenic Corynebacterium diphtheriae along with its primary virulence determinant, diphtheria toxin, have established the paradigm for the study of other related bacterial protein toxins. This review highlights those studies that have contributed to our current understanding of the structure-function relationships of diphtheria toxin, the molecular mechanism of its entry into the eukaryotic cell cytosol, the regulation of diphtheria tox expression by holo-DtxR, and the molecular basis of transition metal ion activation of apo-DtxR itself. These seminal studies have laid the foundation for the protein engineering of diphtheria toxin and the development of highly potent eukaryotic cell-surface receptor-targeted fusion protein toxins for the treatment of human diseases that range from T cell malignancies to steroid-resistant graft-versus-host disease to metastatic melanoma. This deeper scientific understanding of diphtheria toxin and the regulation of its expression have metamorphosed the third-most-potent bacterial toxin known into a life-saving targeted protein therapeutic, thereby at least partially fulfilling Paul Erlich's concept of a magic bullet—"a chemical that binds to and specifically kills microbes or tumor cells."
COA
Publication 
Figure 1. Mechanism of action of diphtheria toxin.
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