Tetanus efficiency

As discussed previously, the immune theory of aging is based, to a considerable degree, on the fact that the immune system becomes less efficient with aging. Importantly, Zn also plays a role in the immune system. For example, Zn supplementation in the elderly (a) increases the number of circulating T-lymphocytes (b) improves delayed cutaneous hypersensitivity to various antigens and (c) increases the immunoglobulin G antibody response to tetanus vaccine (D13). This early study is supported by additional recent reports which also demonstrate that Zn supplementation improves the immune system in the elderly (F9, R6). 

Tetanus toxoid (the vaccine for tetanus) encapsulated in polyester microspheres was produced for single-injection immunization. The entrapment efficiency of the protein vaccine was significantly improved by coencapsulation with excipients such as trehalose and y-hydroxypropyl cyclodextrin. However, these excipients did not impart stabilizing effect on tetanus toxoid. In contrast, bovine serum albumin was foimd to be the most prominent stabilizer for protein in the body after administration by injection. 

Coating of PLGA nanoparticles with the mucoadhesive CS improves the stability of the particles in the presence of lysozyme and enhanced the nasal transport of the encapsulated tetanus toxoid. Nanoparticles made solely of CS are stable upon incubation with lysozyme. Moreover, these particles are very efficient in improving the nasal absorption of insulin as well as the local and systemic immune responses to tetanus toxoid, following intranasal administration. 

Particularly efficient synthetic antitumour vaccines are obtained when the synthetic glycopeptide antigens, as for example 37 (Scheme 6), are coupled to tetanus toxoid. Reaction of the glycopeptide 37 with diethyl squarate afforded the squaric monoamide 59 which was used for the conjugation to TTox to result in the formation of the glycopeptide-TTox vaccine 60 (Scheme 18). ... 

Botulinum and tetanus neurotoxins, which are extensively soluble in water, are known to form efficient membrane channels at a low pH in artificial membranes (Hoch et al. 1985 Boquet and Duflot, 1982). Membrane channel formation by a water soluble protein is an intriguing phenomenon, because for water solubility, hydrophobic domains are needed on the surface of a protein whereas for membrane channel formation, adequate hydrophobic segments will be required for the interaction with non-polar membrane bilayer. A major question to be answered is how are the polypeptides integrated in the lipid bilayer. Are the hydrophobic segments of these neurotoxins hidden in aqueous medium which get exposed... 

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