Final answer:
CJD diagnosis is confirmed by symptoms such as rapid cognitive decline, laboratory results including high levels of 14-3-3 protein in the CSF, an abnormal EEG, and histological examination of a brain autopsy showing characteristic signs of prion disease.
Step-by-step explanation:
The diagnosis of Creutzfeldt-Jakob disease (CJD) involves multiple clinical features and specific laboratory results. A key indicator is the presence of a particular protein, the 14-3-3 protein, found in high concentrations in a patient's cerebrospinal fluid (CSF). Additionally, an abnormal electroencephalogram (EEG) that resembles neurodegenerative diseases can contribute to the diagnosis. These findings, paired with a patient's rapid cognitive decline, often lead to a conclusion of CJD. Definitive diagnosis is typically given postmortem with a brain autopsy showing characteristic amyloid plaques, vacuoles, and prion proteins.
Advanced tests such as RT-QuIC are also helpful for earlier detection of abnormal prion proteins in tissues. It is critical that clinicians handling suspected prion-infected materials exercise caution to avoid infection. While prion diseases like CJD cannot be cured, medications may help slow progression, with care largely focused on comfort due to the debilitating symptoms.