Ricin toxin immunization

Lemley, P.V., Wright, D.C. (1991). Active immunization after passive monoclonal antibody and ricin toxin challenge (abstract 029), 10th World Congress on Animal, Plant, and Microbial Toxins. Singapore, China. 

Griffiths, G.D., Bailey, S.C., Hambrook, J.L., Keyte, M., Jayasekera, P., Miles, J. and Williamson, E. (1997) Liposomally-encapsulated ricin toxoid vaccine delivered intratracheally elicits a good immune response and protects against a lethal pulmonary dose of ricin toxin. Vaccine, 15, 1933-1939. 

Lemley, P.V. and Creasia, D.A. (1995) USA 5,453,271, Vaccine against Ricin Toxin. September 26, 1995. Lemley, P.V. and Wright, D.C. (1992) Mice are actively immunized after passive monoclonal antibody... 

Teter, K. and Holmes, R.K. (2002) Inhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin. Pseudomonas aeruginosa exotoxin A, and ricin. Infect Immun, 70, 6172-6179. 

Drugs Available (No specific anti-toxin) Active immunization and passive antibody prophylaxis are under study, as both are effective in protecting animals from death following exposure by intravenous or respiratory routes. Ricin is not dermally active therefore, respiratory protection is the most critical means of prevention. 

Although it is less common than is the castor seed allergic syndrome, workers chronically exposed to subacute ricin or other RIPs may develop Type I allergies directly against the toxins allergies to purified RIPs can be demonstrated by immune sensitization and IgE induction (Hunt et al., 1918 Forster-Waldl et al., 2003 Szalai et al., 2005). 

Other investigators (Marsden et al, 2004) introduced an inhibitor peptide into the ricin A chain which completely eliminated the in vivo cy-totoxicty of the protein, was non-toxic when injected into rats and elicited an immune response that protected the animals from an intratracheal ricin dose of five times the LD50. Most recently, a fragment of the ricin A chain has been identified which has no enzymic activity, does not induce vascular leak syndrome, is very stable and completely protects mice from subsequent exposure to a lethal ricin challenge when the toxin is administered either by intraperitoneal injection or whole-body aerosol exposure (Olsen et al, 2004 Lebeda and Olson, 1999 McHugh et al, 2004). 

SPR is a representative physical phenomenon that is widely utilized for label-free characterization of molecules on thin metal films. The basic principle and operation of SPR has been described in more detail in several review articles [77, 78]. The reports on SPR-based immune sensors have steeply increased for detection of analytes with low molecular weights in recent years. SPR detection in microfluidic systems can provide various advantages. Immunoreactions are completed within a short time due to small sample volumes down to the nanolitre scale. Kim et al. developed a simple and versatile miniaturized SPR immunosensor enabling parallel analyses of multiple analytes [79]. Their SPR sensor was claimed to exhibit good stability and reusability for 40 cycles and more than 35 days. Feltis et al. demonstrated a low-cost handheld SPR-based immunosensor for the toxin Ricin [80]. Springer et al. reported a dispersion-free microfluidic system with a four-channel SPR sensor platform, which considerably improved the response time and sensitivity [81]. The sensor was able to detect short sequences of nucleic acids down to a femtomole level for 4 min. Waswa et al. demonstrated the immunological detection of E. coli 0157 H7 in milk, apple juice, and meat juice extracted from... 

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