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Title: Prions: the danger of biochemical weapons
Source: [None]
URL Source: ... KrGyVmH05Ya8NPZQiwehw4PdM-jBt4
Published: Apr 28, 2021
Author: Mike Rivero
Post Date: 2021-04-28 08:45:45 by Horse
Keywords: None
Views: 19

The knowledge of biotechnology increases the risk of using biochemical weapons for mass destruction. Prions are unprecedented infectious pathogens that cause a group of fatal neurodegenerative diseases by a novel mechanism. They are transmissible particles that are devoid of nucleic acid. Due to their singular characteristics, Prions emerge as potential danger since they can be used in the development of such weapons. Prions cause fatal infectious diseases, and to date there is no therapeutic or prophylactic approach against these diseases. Furthermore, Prions are resistant to food-preparation treatments such as high heat and can find their way from the digestive system into the nervous system; recombinant Prions are infectious either bound to soil particles or in aerosols. Therefore, lethal Prions can be developed by malicious researchers who could use it to attack political enemies since such weapons cause diseases that could be above suspicion.

1 Introduction

People have had a passion for weapons of mass destruction since the government military agencies search for chemical weapons culminating with the use of poisonous gases in the First War. During the Cold War, there were many rumors of research on biochemical and biological weapons since intelligence agencies of North America and Russian, used different types of weapons, such as radioactive, poison and contagious disease weapons, agaist their political enemies because these weapons cause diseases that could be above suspicion. It is important to emphasize that Prions also have this characteristic. Therefore it is plausible that Prion weapons can be used not only by governments but also by terrorists.

Furthermore, hypothetically, if Prions were used as a biochemical weapon, they could damage not only humans and animals, but the worldwide economies; therefore, even if Prions do not kill instantly a target, they can be a very persuasive object for those who have access to it.Prion diseases include a group of fatal neurodegenerative and infectious disorders in humans such as Creutzfeldt-Jacob disease (CJD), a variant form of CJD (vCJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), and kuru, fatal familial insomnia (FFI); in animals, they include: scrapie of sheep and goats, chronic wasting disease (CWD) of mule deer and elk, and bovine spongiform encephalopathy (BSE) of cattle (Prusiner, 1996). The central feature of these disorders is the conformational change of the host encoded, cellular Prion protein (PrPc), see figures (Figure 1A and Figure 2B, C) to an abnormal, partially proteinase K resistant and infectious isoform (PrPSc) with an aggregation propensity accumulating in the brain of diseased individuals (Figure 1B and Figure 2D) (Gambetti et al., 2003; Tatzelt & Schätzl, 2007). Cases of vCJD in Great Britain and France raised the possibility that BSE has been transmitted to humans (Bateman et al., 1995; Cousens et al., 1997). Macaque monkeys and marmosets both developed neurologic disease several years after inoculation with bovine Prions (Baker et al., 1993; Ono et al., 2011). These experiments clearly show that the inoculation of Prions is potentially fatal, and the fact that Prion strains are transmitted between species raised the possibility that a large section of the population is at high risk as a result of exposure to BSE Prions (Anderson et al., 1996; Sweeting et al., 2010; Bruce et al., 1997; Collinge et al., 1996; Griffin, 1997; Lasmézas et al., 1996; Scott et al., 1993).

Prions have key features which help them to survive in the environment for long periods, such as the resistance to protein degradation, "partially resistant to proteinase K" (Bolton et al., 1982; Prusiner, 1991), high resistant when exposed to irradiation, heat, and harsh chemical treatments (Plum, 1997), plus the fact that they can be attached to soil (Johnson et al., 2006; Saunders et al., 2011a) and spread through air, and therefore they are extremely hazardous (Denkers et al., 2010). Although Prions are just only a polypeptide sequence, they are resistant to heat since people who consumed contaminated meat after preparation got sick; this raised the possibility that a particular conformation of bovine PrPSc was selected for heat resistance during the manufacture of meat and bone meal (MBM). Therefore, it is believed that MBM is the source of Prions responsible for BSE (Prusiner, 1997).

Therefore, hypothetically, Prions can be manufactured based on the molecular characteristics of the Prion protein to make deadly biochemical weapons. The study on how the conversion of PrPC (the normal cellular protein) into PrPSc (the abnormal disease-causing isoform) (Supattapone, 2010) can generate polypeptide sequences designed exclusively to kill.Basically, an ideal Prion polypeptide sequence to be used as a biochemical weapon must be easily recombined and produced in large scale (Supattapone, 2010), be resistant to cold and heat, be fatal in very small quantities, and be transmitted through air, as demonstrated by (Denkers et al., 2010; Haybaeck et al., 2011), and through water, food and soil, as demonstrated by (Saunders et al., 2009; Saunders et al., 2011a), Gough & Maddison (2010) and (Smith et al., 2011). If Prions do not meet all specifications necessary of a biochemical weapon to kill, they at least have key features such as surviving through the digestive system, as demonstrated by Sales (2006), resistance to high temperatures during food preparation processes (Prusiner, 1997), recombinant Prions are infectious, as demonstrated by (Wang et al., 2010; Legname et al., 2004; Makarava et al., 2010), and lastly, a few molecules can produce a chain reaction in the conversion of PrPc into PrPSc causing a fatal neurodegenerative disease (Rigter et al. 2009).

Poster Comment:

Continues at source. Prions have been associated with covid swab tests. Stay away from them.

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