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Human physiology, hazards and health risks
Published in Stephen Battersby, Clay's Handbook of Environmental Health, 2016
David J. Baker, Naima Bradley, Alec Dobney, Virginia Murray, Jill R. Meara, John O’Hagan, Neil P. McColl, Caryn L. Cox
Diphtheria is caused by toxin-producing (toxigenic) aerobic bacteria Corynebacterium diphtheriae and less commonly by Corynebacterium ulcerans. The disease is rare in most countries with well-established immunisation programmes. It may present as classical respiratory diphtheria, nasal and cutaneous diphtheria. Extensive organ damage can occur resulting in neurological and cardiac complications and death if left untreated. The case fatality rate is 5–10 per cent. Diagnosis is by culture from throat and nose swabs, nasopharyngeal/oral secretion and serology from blood. Treatment is with appropriate antibiotics and diphtheria antitoxin.
Human physiology, hazards and health risks
Published in Stephen Battersby, Clay's Handbook of Environmental Health, 2023
Revati Phalkey, Naima Bradley, Alec Dobney, Virginia Murray, John O’Hagan, Mutahir Ahmad, Darren Addison, Tracy Gooding, Timothy W Gant, Emma L Marczylo, Caryn L Cox
Diphtheria is caused by toxin-producing (toxigenic) aerobic bacteria Corynebacterium diphtheriae and less commonly by Corynebacterium ulcerans. The disease is rare in most countries with well-established immunisation programmes. It may present as classical respiratory diphtheria, nasal and cutaneous diphtheria. Extensive organ damage can occur resulting in neurological and cardiac complications and death if left untreated. The case fatality rate is 5–10%. Diagnosis is by culture from throat and nose swabs, nasopharyngeal/oral secretion and serology from blood. Treatment is with appropriate antibiotics and diphtheria antitoxin.
Recombinant Antigens as Components of a Diphtheria-Tetanys-PerSüssis Vaccine
Published in Yoshikatsu Murooka, Tadayuki Imanaka, Recombinant Microbes for Industrial and Agricultural Applications, 2020
Andrew J. Makoff, Ian G. Charles, Neil F. Fairweather
Diphtheria is an infectious disease caused by local invasion of the nasopharyngeal tissues by a strain of Corynebacterium diphtheriae that secretes the lethal diphtheria toxin. The infection results in a hemorrhagic, necrotic lesion overlaid by a tough, fibrinous membrane caused by the growth of the organism. In toxigenic strains of C. diphtheriae, the toxin is expressed from the tox gene located on a bacteriophage [reviewed in Ref. 4].
Molecularly imprinted nanoparticles with recognition properties towards diphtheria toxin for ELISA applications
Published in Journal of Biomaterials Science, Polymer Edition, 2023
Süleyman Serdar Alkanlı, Fulya Dal Yöntem, Merve Yaşar, Celal Güven, M. Vezir Kahraman, Nilhan Kayaman Apohan, Zerrin Aktaş, Mustafa Oral Öncül, Ayhan Ünlü, Handan Akçakaya
Although small template molecules can be imprinted, there are some technical difficulties in the imprinting of macromolecules. Macromolecules are incompatible with organic solvents therefore the polymerization process must be carried out in an aqueous solution [5–8]. Epitope imprinting approach, which is a molecular imprinting method, can produce MIPs with high affinity for the target macromolecule by using fragments of macromolecules [9–12]. Diphtheria toxin (DT), a macromolecule with A-B fragments, is secreted by Corynebacterium diphtheria bacterium and enters the cell by endocytosis and then causes diphtheria, a respiratory tract and skin disease. DT consists of receptor-binding (R-), transmembrane (T-), and catalytic (C-) domains. The C-domain, which is an independent folding domain, forms fragment A (FA), and the T- and R-domains form fragment B (FB) [13,14]. The R-domain binds to the cell surface receptors such as epidermal growth factor receptor (EGFR), allowing DT to enter the cell by endocytosis. T-domain inserts into the membrane after decrease of pH in the endosome interior. T-domain has a monomeric globular form comprised of ten α-helices at neutral pH (pH: 7.0). In the presence of anionic bilayers and acidity, the protein undergoes conformational changes. T-domain assists membrane insertion and translocation of C-domain across the endosome membrane into the cytosol [15]. The C-domain is then proteolyzed from the R- and T-domains. The C-domain reaching the cytosol inhibits the eukaryotic elongation factor 2 (eEF2) translation factor, ending protein synthesis and causing cell death [13–16]. FA inhibits globular G-actin polymerization and initiates depolymerization of filamentous F-actin [17–19].