Accumulation of prion protein in the vagus nerve in creutzfeldt–jakob disease

• Published in: Annals of neurology 2019-05, Vol.85 (5), p.782-787
• Main Authors: Kresl, Philip, Rahimi, Jasmin, Gelpi, Ellen, Aldecoa, Iban, Ricken, Gerda, Danics, Krisztina, Keller, Eva, Kovacs, Gabor G.
• Format: Article
• Language: English
• Subjects: Antibodies; Bovine spongiform encephalopathy; Brief Communication; Brief Communications; Cohort Studies; Creutzfeldt-Jakob disease; Creutzfeldt-Jakob Syndrome - metabolism; Creutzfeldt-Jakob Syndrome - pathology; Disease; Humans; Morphology; Movement disorders; Neurodegenerative diseases; Neurological diseases; Parkinson's disease; Prion protein; Prion Proteins - analysis; Prion Proteins - metabolism; Proteins; Retrospective Studies; Synuclein; Vagus nerve; Vagus Nerve - chemistry; Vagus Nerve - metabolism; Vagus Nerve - pathology
• ISSN: 0364-5134; 1531-8249
• DOI: 10.1002/ana.25451

Disease‐associated proteins are thought to propagate along neuronal processes in neurodegenerative diseases. To detect disease‐associated prion protein (PrPSc) in the vagus nerve in different forms and molecular subtypes of Creutzfeldt–Jakob disease (CJD), we applied 3 different anti‐PrP antibodies. We screened the vagus nerve in 162 sporadic and 30 genetic CJD cases. Four of 31 VV‐2 type sporadic CJD and 7 of 30 genetic CJD cases showed vagal PrPSc immunodeposits with distinct morphology. Thus, PrPSc in CJD affects the vagus nerve analogously to α‐synuclein in Parkinson disease. The morphologically diverse deposition of PrPSc in genetic and sporadic CJD argues against uniform mechanisms of propagation of PrPSc. Ann Neurol 2019;85:782–787