Autopsy observations of sporadic Creutzfeldt-Jakob disease

Introduction. Creutzfeldt-Jakob disease is a fatal neurodegenerative disorder caused by deposited prion protein in neurons, which is resistant to human cell proteases. This disease manifests as polymorphic neurological symptoms, progressive dementia, and impaired breathing and swallowing. The fatal outcome is observed within 6–12 months. Postmortem morphological examination reveals spongiform degeneration of brain tissue, neuronophagia, and amyloid-like protein conglomerates. This paper describescharacteristic changes identified on histological examination of brain tissue of a patient with Creutzfeldt-Jakob disease. Materials and methods. We analyzed medical records and the following brain fragments: left and right caudate nuclei, left and right putamen, left and right frontal lobes, left parietal lobe, and left temporal lobe. The paraffin-embedded brain samples were stained with hematoxylin and eosin, toluidine blue, or immunohistochemical reactions with antibodies to myelin basic protein, glial fibrillary acidic protein, and CD68. Results. Characteristic symptoms were identified from the onset of the disease, including sensorimotor aphasia, ataxia, tremor, diplopia, and progressive cognitive decline. MRI revealed increased signal intensity from the heads of the caudate nuclei, foci of gliosis, and atrophy of the frontoparietal lobes. EEG showed sharp-wave discharges. Microscopic examination revealed spongiform degeneration of the white matter, areas of neuronal loss, microglial neuronophagia, reactive astrocytosis, signs of demyelination, and tigrolysis of Nissl matter. Lymphocytic infiltration was not detected. Conclusion. Based on the clinical picture, changes in EEG and MRI, and histological signs, the patient was diagnosed with sporadic Creutzfeldt-Jakob disease. Keywords: Creutzfeldt-Jakob disease, prion diseases, clinical case, morphological features