Protein toxins bacterial

A subfamily of Rho proteins, the Rnd family of small GTPases, are always GTP-bound and seem to be regulated by expression and localization rather than by nucleotide exchange and hydrolysis. Many Rho GTPase effectors have been identified, including protein and lipid kinases, phospholipase D and numerous adaptor proteins. One of the best characterized effector of RhoA is Rho kinase, which phosphorylates and inactivates myosin phosphatase thereby RhoA causes activation of actomyosin complexes. Rho proteins are preferred targets of bacterial protein toxins ( bacterial toxins). 

The bacterial culture converts a portion of the supplied nutrient into vegetative cells, spores, crystalline protein toxin, soluble toxins, exoenzymes, and metabolic excretion products by the time of complete sporulation of the population. Although synchronous growth is not necessary, nearly simultaneous sporulation of the entire population is desired in order to obtain a uniform product. Depending on the manner of recovery of active material for the product, it will contain the insolubles including bacterial spores, crystals, cellular debris, and residual medium ingredients plus any soluble materials which may be carried with the fluid constituents. Diluents, vehicles, stickers, and chemical protectants, as the individual formulation procedure may dictate, are then added to the harvested fermentation products. The materials are used experimentally and commercially as dusts, wettable powders, and sprayable liquid formulations. Thus, a... 

Clostridial neurotoxins are bacterial protein toxins that consist of a heavy and a light chain connected by a disulfide bond and non-covalent interactions. They... 

S. Olsnes J. Wesche P. O. Falnes, Uptake of Protein Toxins Acting Inside Cells. In Bacterial Protein Toxins] K. Aktorles, I. Just, Eds. Springer Berlin, 2000 Vol. 145, Chapter 1, pp 1-19. 

S. R. Monday G. A. Bohach, Properties ot Staphylococcus aureus Enterotoxins and Toxic Shock Syndrome Toxin-1. in The Comprehensive Sourcebook of Bacterial Protein Toxins, 2nd ed. J. E. Aiout, J. H. Freer, Eds. Academic Press London, 1999 pp 589-610. 

T. Uchiyama K. imanishi T. Miyoshi-Akiyama, Staphyiococcai Superantigens and the Diseases they Cause. In The Comprehensive Sourcebook of Bacterial Protein Toxins, 3rd ed. J. E. Alouf, M. R. Popoff, Eds. Academic Press Paris, 2006 pp 830-843. 

Montecucco, C., Papini, E. and Schiavo, G., Bacterial protein toxins penetrate via a four step mechanism, FEES Lett., 346, 92-98, 1994. 

Sakaguchi, G., Kozaki, S. and Ohshi, I., Bacterial Protein Toxins, Academic Press, London, pp. 435 43, 1984. 

Deliganding Carbonic Adsorbents for Simultaneous Removal of Protein-Bound Toxins, Bacterial Toxins and Inflammatory Cytokines... 

The term microbial toxin is usually reserved by microbiologists for toxic substances produced by microorganisms that are of high molecular weight and have antigenic properties toxic compounds produced by bacteria that do not fit these criteria are referred to simply as poisons. Many of the former are proteins or mucoproteins and may have a variety of enzymatic properties. They include some of the most toxic substances known, such as tetanus toxin, botulinus toxin, and diphtheria toxin. Bacterial toxins may be extremely toxic to mammals and may affect a variety of organ systems, including the nervous system and the cardiovascular system. A detailed account of their chemical nature and mode of action is beyond the scope of this volume. 

Montecucco C, Schiavo G, Dasgupta BR (1989) Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes. Biochem J 259 47-53 Montecucco C, Papini E, Schiavo G (1994) Bacterial protein toxins penetrate cells via a four-step mechanism. FEBS Lett 346 92-8... 

Niemann H (1991) Molecular biology of clostridial neurotoxins. In Alouf J, Freer J (eds) A source-book of bacterial protein toxins. Academic Press, London, pp 303 18 Nishiki T, Tokuyama Y, Kamata Y, Nemoto Y, Yoshida A et al. (1996) The high-affinity binding of Clostridium botulinum type b neurotoxin to synaptotagmin ii associated with gangliosides gtlb/gdla. FEBS Lett 378 253-7... 

Also M. Freissmuth and A. G. Gilman. Mutations of Gs alpha designed to alter the reactivity of the protein with bacterial toxins. Substitutions at Argl87 result in loss of GTPase activity. J Biol Chem, 264 (36), 21907-21914, 1989. 

Leppla, S.H. (2000). Anthrax toxin. In Bacterial Protein Toxins (K. Aktories, ed.), pp. 445-72. Springer, Berlin. 

Fig. 3.3 shows the principle behind the design of immunotoxins. A number of protein toxins of bacterial and plant origin are useful for the production of immunotoxins. These include the diphtheria toxin and pseudomonas exotoxin from bacteria, and ricin, arbin, pokeweed antiviral proteins, saporin, and gelonin from plants (Pastan et al, 1986 Pastan and FitzGerald, 1991). All of these toxins kill cells by entering the cells, and enzymatically inactivating the translational machinery of the cells. Some, such as diphtheria toxin, arbin, and ricin, are composed of two protein chains, A and B. The B chains bind to the cell-surface... 

Various peptide and protein toxins, such bacterial toxins like cholera and botulinum, e.g., [98], venoms from spiders, frogs, snakes. 

Moss J, Vaughan M (1988b) ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins. In Adv. Enzym. 61 303-379. 

Gill DM, Coburn J (1988) ADP-ribosylation of membrane proteins by bacterial toxins in the presence of NAD glycohydrolase. In Biochim. Biophys. Acta 954 65-72. 

Sauerborn M, Hegenbarth S, Laufenberg-Feldmann R, etal. (1994) Monoclonal antibodies discriminating between Clostridium difficile toxins A and B. In Bacterial protein toxins (Freer J, Aitken R, Alouf JE, et al. eds) pp 510-511, Stuttgart Jena New York Gustav Fischer Verlag. 

Since the L chain of TeTx and BoNTs is responsible for the cytosolic activity of the CNTs, at least this domain of the toxin molecule must reach the cytosol. Pharmacological and morphologic evidence indicates that the CNTs enter the cell by endocytosis (Black and Dolly, 1986 b) and that TeTx and BoNTs have to pass through a low pH step for neuron intoxication to occur (Williamson and Neale, 1992 Simpson et at., 1994). Acidic pH does not activate the toxin directly via a structural change, since the direct introduction of the L chain in the neutral pH environment of the cytosol is sufficient to block exocytosis (Penner et at., 1986 Anhert-Hilger et al., 1989 b Bittner et al., 1989 a, b Mochida et al., 1989 Weller et al., 1991). Hence, low pH is necessary for the process of L chain membrane translocation from the vesicle lumen into the cytosol, by analogy with the other bacterial protein toxins with a three-domain structure (Montecucco et al., 1994). 

Alouf JE, Geoffrey C (1991) The family of the antigenically-related, cholesterolbinding ("sulphydryl-activated") cytolytic toxins. In Alouf JE, Freer JH (ed) Sourcebook of bacterial protein toxins. Academic Press Ltd, p. 147-186. 

Montecucco C, Papini E, Schiavo G (1994) Bacterial protein toxins penetrate cells via a four-step mechanism. In FEBS Lett 346 92—98. 

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