Final answer:
The characteristic pathological finding for sCJD includes spongy-like lesions in the brain caused by the accumulation of misfolded prion proteins.
Step-by-step explanation:
The characteristic pathological finding for sporadic Creutzfeldt-Jakob disease (sCJD) involves the presence of spongy-like lesions in the brain, which result from abnormal aggregations of misfolded prion proteins—specifically, the infectious form known as PrPSC. The histological examination of brain biopsies typically shows these spongy lesions, neurofibrillary tangles, and amyloid plaques. Additionally, there are auxiliary tests such as the detection of the 14-3-3 protein in cerebrospinal fluid (CSF) that support the diagnosis of CJD.