400 Americans Diagnosed with Fatal Prion Diseases Each Year, 90% Over Age 55

Imagine a disease so mysterious and lethal that it strikes primarily the older population, affecting about 400 Americans each year. Prion diseases, a group of rare brain disorders, not only puzzle the world’s leading scientists but also progress swiftly with no known cure.

The majority of those diagnosed are over the age of 55 ¹, highlighting a disturbing trend in age-related vulnerability. These conditions are caused by proteins in the brain folding incorrectly, which disrupts normal brain function and leads to severe neurological decline.

With such a significant impact on a specific age group, researchers are urgently trying to decipher why these proteins misfold and how to stop this deadly process.

Let’s take a closer look at what makes these diseases so challenging to understand and fight.

The Rogue Proteins Behind Fatal Brain Disorders

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At the heart of prion diseases are proteins, the workhorses of the cell, which sometimes fold incorrectly due to a glitch in the molecular origami that shapes them.

Normally, misfolded proteins are just cellular debris swiftly cleared away. However, prions are the exception.

These misfolded proteins not only evade cleanup but also corrupt their properly folded counterparts, triggering a domino effect that leads to disease. As prions accumulate, they form clumps that interfere with nerve cell function, leading to a cascade of devastating symptoms, from memory loss to fatal organ failure.

Creutzfeldt-Jakob Disease & Its Kin

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The most well-known prion disease in humans is Creutzfeldt-Jakob Disease (CJD), a rare but fatal condition that destroys brain tissue, leading to rapid neurological decline and death.

But humans aren’t the only ones affected.²

Mad cow disease in cattle, scrapie in sheep, and chronic wasting disease in deer are all variations of prion diseases, each caused by the same type of misfolded brain protein, albeit with slight differences. These diseases highlight prions’ insidious nature and ability to jump between species, posing significant challenges to public health and wildlife management.

The Challenge of Detection & Treatment

One of the most daunting aspects of prion diseases is their detection. Prions are nearly identical to normal proteins, the only difference being their folded shape. This makes them incredibly difficult to identify and, subsequently, to treat.

Current technology lacks the means to either destroy these misfolded proteins or revert them to their proper shape, leaving scientists at a standstill in finding a cure. However, the rarity of prion diseases, comparable to the likelihood of being struck by lightning, offers a small consolation in the face of their deadly nature.

A Silver Lining: The Unexpected Benefits of Prions

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Despite their fearsome reputation, prions aren’t all bad. In yeast, prions represent a unique mechanism of inheritance that operates at the protein conformation level rather than through nucleotide sequences. This phenomenon provides yeast cells with a form of memory, allowing them to adapt to environmental stresses.

For instance, the [PSI+] prion, a misfolded form of the Sup35 protein, can enhance the survival of yeast cells under adverse conditions by enabling them to read through stop codons, thus producing full-length proteins that might be beneficial in stress responses.

This duality of prions—being both a potential threat and a survival advantage—underscores the complexity of these proteins and suggests that the very mechanism causing devastating diseases in mammals can confer critical benefits in other organisms.³

The Frontier of Protein Research

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The study of prions and proteins has been revolutionized by advancements in artificial intelligence, particularly by DeepMind’s AlphaFold system . AlphaFold’s ability to predict protein structures based on amino acid sequences has opened new horizons in understanding how proteins work, facilitating research in fields ranging from environmental conservation to medical science.

This breakthrough illustrates the potential of AI in unraveling the mysteries of biology. It offers hope that one day, we might not only fully understand prion diseases but also find a way to cure them.

Prion diseases remain one of the most perplexing and terrifying anomalies in biology, a reminder of the delicate balance within our cells and the chaos that ensues when it’s disrupted. While the search for detection methods and treatments continues, the progress in protein research offers a beacon of hope.

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  1. ncbi.nlm.nih.gov/pmc/articles/PMC4879966/
  2. ninds.nih.gov/health-information/disorders/creutzfeldt-jakob-disease
  3. ncbi.nlm.nih.gov/pmc/articles/PMC3415993/
  4. deepmind.google/technologies/alphafold/
Martha A. Lavallie
Martha A. Lavallie
Author & Editor | + posts

Martha is a journalist with close to a decade of experience in uncovering and reporting on the most compelling stories of our time. Passionate about staying ahead of the curve, she specializes in shedding light on trending topics and captivating global narratives. Her insightful articles have garnered acclaim, making her a trusted voice in today's dynamic media landscape.