Neuropathologically directed profiling of PRNP somatic and germline variants in sporadic human prion disease.
Gannon A McDonoughYuchen ChengKatherine S MorilloRyan N DoanZinan ZhouConnor J KennyAaron FoutzChae KimMark L CohenBrian S ApplebyChristopher A WalshJiri G SafarAugust Yue HuangMichael B MillerPublished in: Acta neuropathologica (2024)
Creutzfeldt-Jakob Disease (CJD), the most common human prion disease, is associated with pathologic misfolding of the prion protein (PrP), encoded by the PRNP gene. Of human prion disease cases, < 1% were transmitted by misfolded PrP, ~ 15% are inherited, and ~ 85% are sporadic (sCJD). While familial cases are inherited through germline mutations in PRNP, the cause of sCJD is unknown. Somatic mutations have been hypothesized as a cause of sCJD, and recent studies have revealed that somatic mutations accumulate in neurons during aging. To investigate the hypothesis that somatic mutations in PRNP may underlie sCJD, we performed deep DNA sequencing of PRNP in 205 sCJD cases and 170 age-matched non-disease controls. We included 5 cases of Heidenhain variant sporadic CJD (H-sCJD), where visual symptomatology and neuropathology implicate localized initiation of prion formation, and examined multiple regions across the brain including in the affected occipital cortex. We employed Multiple Independent Primer PCR Sequencing (MIPP-Seq) with a median depth of > 5000× across the PRNP coding region and analyzed for variants using MosaicHunter. An allele mixing experiment showed positive detection of variants in bulk DNA at a variant allele fraction (VAF) as low as 0.2%. We observed multiple polymorphic germline variants among individuals in our cohort. However, we did not identify bona fide somatic variants in sCJD, including across multiple affected regions in H-sCJD, nor in control individuals. Beyond our stringent variant-identification pipeline, we also analyzed VAFs from raw sequencing data, and observed no evidence of prion disease enrichment for the known germline pathogenic variants P102L, D178N, and E200K. The lack of PRNP pathogenic somatic mutations in H-sCJD or the broader cohort of sCJD suggests that clonal somatic mutations may not play a major role in sporadic prion disease. With H-sCJD representing a localized presentation of neurodegeneration, this serves as a test of the potential role of clonal somatic mutations in genes known to cause familial neurodegeneration.
Keyphrases
- copy number
- genome wide
- single cell
- endothelial cells
- squamous cell carcinoma
- late onset
- gene expression
- amyotrophic lateral sclerosis
- oxidative stress
- brain injury
- optical coherence tomography
- multiple sclerosis
- electronic health record
- single molecule
- risk assessment
- climate change
- quantum dots
- early onset
- circulating tumor
- small molecule
- rectal cancer
- neoadjuvant chemotherapy
- transcription factor
- genome wide identification
- case report
- resting state
- binding protein
- protein protein
- real time pcr
- sensitive detection
- case control