How Prions Kill

Pro Tip: Avoid Cannibalism

How do prions infect?

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Prions are unique infectious agents that differ significantly from viruses, bacteria, fungi, or parasites. They are misfolded proteins that can induce normal proteins in the body, particularly in the brain, to misfold in a similar way, leading to neurodegenerative diseases. This misfolding process is at the core of how prions "infect" a host and cause disease.

Steps in Prion Infection:

1. Introduction of Misfolded Prion Protein (PrP^Sc):

   • Prions can enter the body through contaminated food (as in mad cow disease or variant Creutzfeldt-Jakob disease), medical procedures (such as contaminated surgical instruments), blood transfusions, or even, in rare cases, inherited mutations.

   • The infectious agent is a misfolded form of a normal protein called PrP (prion protein), which is present in all mammals and highly concentrated in the brain. The normal form is referred to as PrP^C (cellular prion protein), while the misfolded, infectious form is called PrP^Sc (scrapie-associated prion protein).

2. Interaction with Normal Prion Proteins:

   • Once introduced into the body, the misfolded prion protein (PrP^Sc) comes into contact with normal PrP^C proteins. PrP^Sc acts as a template or catalyst, inducing the normal PrP^C to change its conformation (shape) into the misfolded PrP^Sc form.

   • This misfolding is abnormal and makes the protein resistant to normal cellular processes that degrade proteins, such as enzymes and proteases.

3. Propagation of Misfolded Proteins:

   • The newly misfolded PrP^Sc proteins can then go on to convert more normal PrP^C proteins into the misfolded form. This leads to an amplification of prions in the brain and other tissues.

   • As more proteins misfold, they begin to aggregate and form clumps or plaques in the brain, similar to those seen in Alzheimer's disease.

4. Disruption of Cellular Function:

   • Misfolded prions accumulate in neurons (brain cells), where they form toxic aggregates. These aggregates interfere with normal cellular function, leading to neuronal death.

   • The loss of neurons and the resulting brain tissue damage cause the characteristic symptoms of prion diseases, such as memory loss, confusion, motor dysfunction, and eventually death.

5. Transmission:

   • Prions can be transmitted through various means:

     • Ingestion: Eating contaminated meat, such as beef infected with bovine spongiform encephalopathy (BSE) (commonly known as mad cow disease), can transmit prions to humans, leading to variant Creutzfeldt-Jakob Disease (vCJD).

     • Medical procedures: Prions can be transmitted through contaminated surgical instruments or tissue grafts, even after sterilization, because prions are highly resistant to conventional sterilization methods.

     • Inherited mutations: Some forms of prion disease, such as familial CJD and Gerstmann-Sträussler-Scheinker syndrome (GSS), are inherited through mutations in the gene that codes for the normal prion protein.

Prion Diseases:

Once the infection process begins, it leads to prion diseases, which are progressive, fatal, and neurodegenerative. Examples of prion diseases include:

• Creutzfeldt-Jakob Disease (CJD): The most common prion disease in humans, it can be sporadic, inherited, or acquired (e.g., through contaminated medical procedures).

• Kuru: Once prevalent among the Fore people of Papua New Guinea, this disease spread through ritualistic cannibalism.

• Bovine Spongiform Encephalopathy (BSE): Also known as mad cow disease, it can be transmitted to humans through consumption of infected beef, causing vCJD.

• Scrapie: A prion disease in sheep and goats, which provided early insights into prion biology.

Why Prions are Dangerous:

• Resistance: Prions are incredibly tough, resistant to heat, radiation, and chemical disinfectants. This makes decontamination extremely difficult, especially in medical settings.

• Lack of Immune Response: Because prions are simply misfolded versions of a normal body protein, the immune system does not recognize them as foreign and thus does not mount an attack against them.

• No Cure: There is currently no cure for prion diseases. They are invariably fatal, and treatments focus on symptom management and supportive care.

Conclusion:

Prions "infect" by hijacking the normal folding process of proteins in the brain, converting healthy proteins into misfolded, disease-causing forms. This self-propagating process leads to brain damage and fatal neurodegenerative diseases. Their unusual infectious mechanism and resistance to destruction make prions particularly dangerous.

You said:

Are they autocatalytic?

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Yes, prions are autocatalytic in nature. This means that they can promote their own replication by catalyzing the conversion of normal proteins into the same misfolded, infectious form, without the need for nucleic acids (DNA or RNA) that traditional pathogens like viruses or bacteria use.

How Prions are Autocatalytic:

1. Misfolding and Propagation:

   • Prions are misfolded versions of the normal prion protein (PrP^C). The infectious prion protein, PrP^Sc, has an abnormal structure that is energetically stable and can convert normal PrP^C into more PrP^Sc.

   • The misfolded PrP^Sc interacts with PrP^C and acts as a template, inducing the normal protein to misfold into the same pathogenic shape. This misfolding is the catalytic process that drives prion replication.

2. Self-Sustaining Mechanism:

   • Once a few misfolded prions are present, they can trigger the misfolding of more normal proteins. This creates a self-sustaining loop, where the more misfolded prions accumulate, the faster they can propagate and convert more normal proteins into misfolded forms.

   • This autocatalytic behavior is at the core of how prions multiply within an organism, despite being mere proteins without genetic material to direct their replication.

3. Protein Aggregation:

   • The misfolded prions tend to aggregate or form amyloid plaques in the brain, which further accelerates the process. These aggregates provide a stable environment where more PrP^C proteins come into contact with PrP^Sc, allowing the conversion to continue.

   • Over time, this autocatalytic conversion overwhelms the brain's ability to remove or degrade the misfolded proteins, leading to the neurodegeneration seen in prion diseases.

Why Autocatalysis is Dangerous in Prion Diseases:

• Exponential Spread: Once prions start converting normal proteins, the process can rapidly accelerate, leading to a large buildup of misfolded proteins. This is why prion diseases can progress so quickly after symptoms appear.

• Resistance to Degradation: Misfolded prions are resistant to the normal cellular machinery (like proteases) that would typically degrade misfolded proteins. This makes the accumulation of prions even more dangerous because the body has no effective way of stopping their autocatalytic spread.

In conclusion, prions are autocatalytic because they propagate by catalyzing the conversion of normal proteins into the same misfolded, infectious form. This self-perpetuating mechanism is central to the spread of prion diseases and is what makes prions so difficult to control and eliminate.

You said:

Why are they so hard to kill?

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Prions are incredibly difficult to destroy because of their unique structure and properties as misfolded proteins, which make them resistant to the traditional methods used to kill pathogens like bacteria, viruses, or fungi. Here’s why prions are so hard to kill:

1. Lack of Genetic Material:

• Prions do not contain any DNA or RNA, which are the usual targets of many disinfection methods, including heat, radiation, and chemicals that damage genetic material. Since prions are simply proteins, these methods are ineffective.

• Most sterilization processes for pathogens involve techniques that disrupt nucleic acids, but prions bypass this because they don’t rely on nucleic acids for replication.

2. Protein Misfolding:

• Prions are abnormally folded versions of a normal protein called PrP^C. The infectious prion protein (PrP^Sc) has a highly stable structure due to its beta-sheet conformation, which makes it extremely resistant to degradation.

• Normal proteins can often be denatured by heat or chemicals, causing them to lose their shape and function. However, prions are already in a misfolded state that is thermodynamically stable, meaning they do not easily denature or lose their infectivity under conditions that would destroy other proteins.

3. Resistance to Heat:

• Prions can survive heat that would normally denature or kill most biological molecules. Standard sterilization methods, like boiling or autoclaving (even at 121°C or 250°F), which kill bacteria and viruses, are not always effective against prions. Autoclaving needs to be done at higher temperatures (134°C or 273°F) and for longer periods (up to an hour) to even partially deactivate prions.

• Even incineration doesn’t guarantee complete destruction, as prions can survive temperatures up to 600°C (1,112°F).

4. Resistance to Chemicals:

• Prions are resistant to many chemicals commonly used for disinfection, such as formaldehyde, alcohols, bleach, and standard hospital disinfectants. Only certain harsh chemicals, such as sodium hydroxide (NaOH) or highly concentrated bleach, can inactivate prions, but these need to be applied under specific conditions (high concentrations and long exposure times).

• Because prions don’t have nucleic acids, chemicals that target DNA or RNA (like radiation or ethylene oxide) are ineffective.

5. Resistance to Proteases:

• Normally, misfolded proteins in cells are degraded by enzymes called proteases, which break them down into smaller, harmless fragments. However, prions are resistant to protease digestion due to their tightly packed, stable structure. This means that even the body’s natural defense mechanisms can’t break them down efficiently.

• This resistance to proteases allows prions to persist in tissues, especially the brain, leading to the slow but inevitable damage seen in prion diseases.

6. Environmental Stability:

• Prions can survive in the environment for long periods. They can persist in soil, water, and on surfaces without losing their infectivity. This makes them a significant concern for animal prion diseases, such as chronic wasting disease (CWD) in deer or scrapie in sheep, where prions can remain infectious in the environment for years.

• Prions can also resist drying, freezing, and other environmental conditions that would typically inactivate other pathogens.

7. Lack of an Immune Response:

• Because prions are simply misfolded versions of a protein that is normally present in the body (PrP^C), the immune system does not recognize them as foreign invaders. As a result, the body mounts no immune response against them, allowing prions to spread unchecked in tissues, particularly in the brain.

Implications for Healthcare and Research:

• Infection Control: Prions pose a major challenge in hospitals and medical settings. Standard sterilization techniques for surgical instruments, such as autoclaving or chemical disinfection, may not reliably inactivate prions. Special protocols are required to handle instruments used on patients with prion diseases, including extended autoclaving at higher temperatures or treatment with caustic chemicals.

• Cross-Contamination: Prions can contaminate surgical instruments, tissues, and medical products. Once they are present, cleaning and disinfecting these surfaces is very difficult, posing risks of accidental transmission through procedures like brain surgery, blood transfusions, or tissue transplants.

Conclusion:

Prions are so hard to kill because of their extreme resistance to heat, chemicals, radiation, and protease digestion, coupled with their ability to survive in the environment and avoid detection by the immune system. These factors make them uniquely challenging to deal with and a significant cause of concern in both medical and environmental settings.

You said:

Could graphene Oxide prove autocatalytic in the body?

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The potential for graphene oxide (GO) to exhibit autocatalytic behavior in the body is an area of active research and, while there is no definitive answer yet, there are certain properties of graphene oxide that warrant investigation in this context.

What is Graphene Oxide?

Graphene oxide is a single-atomic-layer material derived from graphene but functionalized with oxygen-containing groups like hydroxyl, epoxy, and carboxyl groups. These modifications make GO more chemically reactive and easier to disperse in water, which is useful in biomedical applications such as drug delivery, biosensors, and cancer treatment.

Autocatalysis and Graphene Oxide

1. Chemical Reactivity and Oxidative Stress:

• Reactive Oxygen Species (ROS) Production: Graphene oxide can catalyze the production of reactive oxygen species (ROS), which are chemically reactive molecules that can damage proteins, lipids, and DNA. In theory, this oxidative damage could be autocatalytic if GO continues to generate ROS, leading to a self-sustaining cycle of cellular stress and damage.

• Cellular Damage: Some studies suggest that graphene oxide can induce oxidative stress in cells by promoting ROS production. If the oxidative stress is not properly managed by the body’s antioxidant systems, this could potentially result in ongoing cellular damage, which might resemble autocatalytic behavior in a biological context.

2. Interaction with Biological Molecules:

• Protein Aggregation: Similar to prions, graphene oxide has the potential to bind to certain proteins and induce structural changes, which could lead to protein misfolding or aggregation. If GO interacts with proteins in a way that causes them to adopt abnormal conformations, it could theoretically trigger more proteins to misfold or aggregate, leading to prion-like behavior. However, this is speculative and has not been proven in vivo (within living organisms).

• Enzyme Interaction: Graphene oxide can interfere with enzyme activity due to its high surface area and reactivity. It can either inhibit or enhance enzyme functions, depending on the type of enzyme and its interaction with GO. If GO interferes with key metabolic enzymes, it could disrupt cellular homeostasis, possibly leading to a cascading effect in biological systems.

3. Potential for Autocatalytic Reactions in Synthetic Settings:

• In laboratory settings, graphene and graphene oxide have been shown to act as catalysts for certain chemical reactions, especially in redox processes. Their large surface area, conductivity, and ability to stabilize reactive intermediates make them useful in catalysis. This property raises the possibility that GO could exhibit autocatalytic properties under certain conditions in the body, such as in reactions involving ROS or oxidative damage.

Is Graphene Oxide Autocatalytic in the Body?

Currently, there is no direct evidence that graphene oxide behaves autocatalytically in the human body in the same way that prions do. While GO’s ability to generate ROS or cause cellular stress could, in theory, create a feedback loop of damage, there is insufficient research proving that it perpetuates itself autonomously or accelerates harmful reactions without external stimuli.

Concerns and Ongoing Research:

Graphene oxide's potential to cause cellular damage or interfere with biological processes has led to concerns about its biocompatibility and toxicity, especially at higher doses or in certain formulations. There is ongoing research into:

• Nanotoxicology: Studying how nanoscale materials like GO interact with living systems and whether they induce harmful processes.

• Biodegradation: Investigating whether graphene oxide can be safely broken down or eliminated by the body, or whether it accumulates and exacerbates cellular damage over time.

• Immune Response: How GO might interact with the immune system, and whether the body mounts defenses against it or allows it to persist, potentially creating long-term risks.

Conclusion:

While graphene oxide has properties that could theoretically lead to autocatalytic-like behavior in terms of oxidative stress or protein interaction, there is no conclusive evidence to date showing that it behaves autocatalytically in the body. However, given its chemical reactivity and ability to interfere with biological molecules, further research is needed to fully understand its long-term effects and any potential self-propagating mechanisms in biological systems.

You said:

Has graphene oxide been found in mRNA vaccines?

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No, graphene oxide has not been found in mRNA vaccines according to scientific studies and reports from regulatory agencies. There have been claims circulating in certain circles, particularly online and in social media, suggesting that graphene oxide is present in mRNA vaccines (such as the Pfizer-BioNTech and Moderna COVID-19 vaccines), but these claims have been debunked by health authorities and independent researchers.

Here’s a breakdown of the situation:

1. Ingredients of mRNA Vaccines:

• The primary components of the mRNA vaccines (such as Pfizer and Moderna) are:

  • mRNA: Encodes the spike protein of the SARS-CoV-2 virus to trigger an immune response.

  • Lipid Nanoparticles: Used to encapsulate and deliver the mRNA into cells.

  • Salts, sugars, and buffers: To maintain the stability and pH balance of the vaccine.

Graphene oxide is not listed among these ingredients, nor has its presence been detected in any independent analysis of the vaccines.

2. Claims about Graphene Oxide:

• The claim that graphene oxide is in the mRNA vaccines appears to have originated from misinterpretations or deliberate misinformation from certain sources. Some reports have cited flawed or non-peer-reviewed studies that purported to find graphene oxide, but these findings have been widely discredited by the scientific community.

• Notably, a Spanish researcher’s work that claimed to find graphene oxide in vaccines was heavily criticized due to methodological errors, lack of peer review, and a failure to provide any reproducible evidence.

3. Regulatory Agency Responses:

• Regulatory agencies, including the U.S. Food and Drug Administration (FDA), European Medicines Agency (EMA), and World Health Organization (WHO), have all confirmed that there is no graphene oxide in any of the COVID-19 vaccines approved for emergency or general use.

• These agencies rigorously test the composition of vaccines to ensure safety and effectiveness, and no graphene oxide has been detected in any such analyses.

4. Peer-Reviewed Studies:

• Independent scientists and laboratories have analyzed the contents of various COVID-19 vaccines, particularly in response to the misinformation surrounding graphene oxide. No credible, peer-reviewed studies have found any evidence of graphene oxide in these vaccines.

Conclusion:

While concerns about graphene oxide in mRNA vaccines have spread in certain online forums, these claims are not supported by scientific evidence. Multiple regulatory agencies and independent researchers have confirmed that graphene oxide is not present in mRNA vaccines, and its alleged inclusion has been debunked as misinformation.

What are the symptoms of Kuru?

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Kuru is a rare and fatal neurodegenerative disorder classified as a prion disease, similar to Creutzfeldt-Jakob Disease (CJD). It was first identified among the Fore people of Papua New Guinea, where it was transmitted through the practice of ritualistic cannibalism, specifically the consumption of the brains of deceased relatives, which contained infectious prions.

Symptoms of Kuru:

The symptoms of Kuru develop in stages and progressively worsen over time. It primarily affects the central nervous system, causing both neurological and motor impairments. Here’s a breakdown of the symptoms:

1. Early Stage (Ambulant Stage):

• Tremors: Shaking or trembling of the limbs, especially the hands and feet.

• Unsteady Gait: Difficulty walking, a wide stance, or stumbling due to loss of motor coordination.

• Slurred Speech: Impairment in the ability to articulate words, making speech difficult to understand.

• Muscle Jerks (Myoclonus): Sudden, involuntary muscle twitches or spasms.

• Headaches: Persistent or severe headaches.

• Difficulty with Fine Motor Skills: Trouble performing tasks that require precision, such as writing or using utensils.

2. Intermediate Stage (Sedentary Stage):

• Loss of Muscle Control: Inability to stand or walk unaided due to severe lack of coordination and muscle weakness (ataxia).

• Severe Tremors: Uncontrollable shaking throughout the body.

• Emotional Instability: Outbursts of uncontrollable laughter, crying, or other inappropriate emotional expressions (this was referred to as "laughing sickness").

• Cognitive Decline: Difficulty with thinking, memory, and concentration; increased confusion.

• Difficulty Swallowing (Dysphagia): Trouble swallowing food or liquids, which can lead to malnutrition or aspiration.

• Apathy: Loss of interest in surroundings or previously enjoyed activities.

3. Late Stage (Terminal Stage):

• Complete Immobility: Total inability to move or control limbs, resulting in bedridden status.

• Incontinence: Loss of bladder and bowel control.

• Severe Dementia: Extreme mental confusion, memory loss, and cognitive dysfunction.

• Mute or Near-Mute State: Loss of the ability to speak coherently or at all.

• Coma: In the final stage, the person falls into a coma before death.

Duration of Disease:

• The disease can incubate for years or decades after initial infection, meaning symptoms may not appear for a long time after exposure to prions. Once symptoms begin, the disease progresses rapidly, with most patients dying within 6 months to 2 years after the onset of symptoms.

Outcome:

• There is no cure or effective treatment for Kuru. It is always fatal, as the prions continue to cause irreversible brain damage. Death usually occurs due to complications like infections, aspiration pneumonia, or organ failure.

Transmission and Prevention:

• Kuru is transmitted through ingestion of prion-infected tissue, particularly brain tissue. Since the cessation of cannibalistic practices among the Fore people in the late 1950s, the incidence of Kuru has dramatically decreased, and it is now considered a historical disease.

Kuru’s symptoms and progression highlight the devastating effects of prions, which cause the brain to deteriorate in a manner similar to other prion diseases like CJD or Mad Cow Disease (Bovine Spongiform Encephalopathy).

You said:

You have just described Joe Biden.

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I see what you're getting at with the comparison, but it's important to approach discussions about individuals, especially public figures like Joe Biden, with care and accuracy. While it’s common to use humor or exaggerated comparisons in political discussions, there are clear distinctions between the serious neurological condition of Kuru (or any prion disease) and the health or behavior of any living individual, including political leaders.

Joe Biden has undergone regular health evaluations, and any assessments of his health would be based on medical expertise, rather than comparisons to diseases like Kuru, which is a rare and specific condition related to prions.

If you’re concerned about his capacity or any public figure’s health, it’s always best to refer to factual information from health professionals and credible sources rather than relying on metaphors or broad comparisons. Let me know if you'd like to dive deeper into any related topic!

References:

1. https://news.artnet.com/art-world-archives/right-wing-mistakes-marina-abramovic-dinner-party-for-satanic-ritual-736247