What Is Creutzfeldt-Jakob Disease and Why Are Cases in Oregon Alarming?

Updated April 6, 2026

In 2025, health officials in Hood River County, Oregon, detected three cases of Creutzfeldt-Jakob Disease (CJD). Two of the three people have already died. It’s a small number, but it’s the kind of cluster that raises big questions because the disease is untreatable and 100% fatal.

What Causes CJD?

CJD is part of a family of illnesses caused by prions. Prions are misfolded proteins that damage brain tissue. Unlike bacteria or viruses, prions aren’t living organisms. They’re corrupted proteins that trigger a chain reaction in the brain, causing spongiform encephalopathy, a condition where brain tissue becomes riddled with holes. Think of it as a rogue protein convincing other proteins to turn against you.

Symptoms of CJD

Creutzfeldt-Jakob Disease progresses quickly and leads to severe neurological decline. While symptoms can vary slightly depending on the type, the overall pattern involves a rapid transition from subtle cognitive issues to profound brain dysfunction and, ultimately, death—often within a year.

Early-stage symptoms

• Subtle cognitive changes such as memory loss, impaired judgment, confusion, and difficulty concentrating.
• Mood and personality shifts including anxiety, depression, irritability, and apathy.
• Initial physical signs like balance problems, unsteadiness, or mild coordination issues.

Mid-stage symptoms

• Rapidly progressing dementia along with speech and swallowing difficulties.
• Involuntary muscle movements (myoclonus), vision problems, and worsening coordination leading to frequent falls.
• Stiffness, tremors, and trouble walking independently.

Late-stage symptoms

• Severe cognitive and physical decline resulting in mutism, incontinence, and immobility.
• Complete loss of voluntary muscle control, leading to coma.
• Death, typically due to infection or respiratory failure related to immobility.

Types of Creutzfeldt-Jakob Disease

Creutzfeldt-Jakob Disease (CJD) is not a singular illness but a group of rare, fatal brain disorders that differ in how they develop. While all types involve the buildup of misfolded prion proteins that destroy brain tissue, the source of these prions can vary—ranging from spontaneous occurrence to inherited mutations or even transmission through contaminated medical instruments or food.

1. Sporadic CJD (sCJD)

The most common form, sporadic CJD (sCJD), accounts for approximately 85–90% of cases. It arises without warning or clear cause, typically affecting individuals over the age of 60. Researchers believe that spontaneous mutations in the PRNP gene, which codes for the prion protein, may play a role, but no definitive risk factors have been identified.

2. Familial or genetic CJD (fCJD)

Familial or genetic CJD results from inherited mutations in the PRNP gene. It tends to cluster in families and represents 10–15% of known cases worldwide. The age of onset and rate of progression can vary depending on the specific mutation, but the condition is always fatal.

3. Iatrogenic CJD (iCJD)

Iatrogenic CJD is extremely rare and results from accidental transmission during medical procedures. Documented cases have occurred through exposure to contaminated surgical instruments, dural grafts, corneal transplants, or human-derived growth hormones. Thanks to strict sterilization protocols and modern donor screening practices, such instances have become exceptionally uncommon.

4. Variant CJD (vCJD)

Lastly, variant CJD is linked to eating beef products infected with Bovine Spongiform Encephalopathy (BSE), or “mad cow disease.” First identified in the United Kingdom in the 1990s, vCJD typically affects younger people, often in their 20s or 30s, and has a longer incubation period compared to other forms. Though symptoms may progress more slowly, the disease is still invariably fatal.

How Do People Get Infected with Prions?

That’s one of the scariest parts. Most CJD cases are sporadic, meaning we don’t know exactly how the person got infected. But we do know that prions can be transmitted through contaminated meat, surgical equipment, or, in rare cases, inherited genetic mutations. In animals, similar diseases spread when nervous system tissue is consumed—often through industrial feed practices. That’s what caused the mad cow disease outbreaks that were widely discussed in the 1990s.

Why a Cluster of Prion Disease Cases Matters?

It’s easy to shrug off one or two deaths from a rare disease. But three in one area? That deserves a rigorous investigation. Prion diseases are poorly understood, difficult to detect early, and always lethal. This cluster is a reminder that even in an era of advanced diagnostics and molecular testing, some infectious threats still evade our best tools and public health surveillance systems.

What Can We Learn from This?

A lot. First, we need to keep investing in disease surveillance for rare pathogens—especially in rural or underserved areas. Second, this is a reminder that the boundary between environmental and human health is thin. Just like chronic wasting disease in deer, prion threats may be lurking in ecosystems we don’t fully understand.

And finally, it’s personal. One of my first instructors in field epidemiology and outbreak investigation at CDC, Dr. Stephen Thacker, died from a prion disease he likely acquired decades earlier while living in the United Kingdom. It was a tragic and powerful lesson in humility: the idea that the microbes we study may be the ones that kill us.