Identification of a novel risk factor for chronic wasting disease (CWD) in elk: S100G single nucleotide polymorphism (SNP) of the prion protein gene (PRNP).

Prion diseases are fatal and malignant infectious encephalopathies induced by the pathogenic form of prion protein (PrP) originating from benign prion protein (PrP). A previous study reported that the M132L single nucleotide polymorphism (SNP) of the prion protein gene (PRNP) is associated with susceptibility to chronic wasting disease (CWD) in elk. However, a recent meta-analysis integrated previous studies that did not find an association between the M132L SNP and susceptibility to CWD.

Autoclave treatment fails to completely inactivate DLB alpha-synuclein seeding activity.

Synucleinopathies are characterized by the deposition of alpha-synuclein (α-syn) aggregates in brain tissue. Pathological α-syn aggregates propagate in a prion-like manner and display prion-like biochemical properties. Using RT-QuIC, we measured α-syn seeding activity from brains of Dementia with Lewy body (DLB) patients post autoclave.

Association Study of the M132L Single Nucleotide Polymorphism With Susceptibility to Chronic Wasting Disease in Korean Elk: A Meta-Analysis.

Chronic wasting disease (CWD) is a deleterious brain proteinopathy caused by a pathogenic form of prion protein (PrP), which is converted from a benign form of prion protein (PrP) encoded by the prion protein gene (). In elk, the M132L single nucleotide polymorphism (SNP) of the gene likely plays a pivotal role in susceptibility to CWD. However, the association of the M132L SNP with susceptibility to CWD has not been evaluated in Korean elk to date.

In-depth examination of PrP in Holstein cattle carrying the E211K somatic mutation of the bovine prion protein gene (PRNP).

Prion diseases are transmissible spongiform encephalopathies caused by deleterious prion protein (PrP ) derived from normal prion protein (PrP ), which is encoded by the prion protein gene (PRNP). We performed an in-depth examination to detect PrP by using enzyme immunoassay (EIA), real-time quaking-induced conversion reactions (RT-QuIC) and protein misfolding cyclic amplification (PMCA) in nine brain tissues derived from three Holstein cattle carrying the E211K somatic mutation of the bovine PRNP gene. The EIA, RT-QuIC and PMCA analyses were not able to detect the PrP band in any tested samples.

The complete mitochondrial genome of (Erxleben, 1777), as a model species of Chronic Wasting Disease (CWD).

(Erxleben, 1777) has been used as a model species of Chronic Wasting Disease (CWD). We completed the mitochondrial genome of , susceptible to the CWD. Its length is 16,428 bp, identical to the previous mitochondrial genome of , and 37 genes (13 protein-coding genes, two rRNAs, and 22 tRNAs) were identified.

The first complete mitogenome of (Merriam, 1905).

(Merriam, 1905) is one of the subspecies of elk distributed only in California, USA. We completed the first mitogenome of . Its length is 16,428 bp, which is in middle among 24 available mitogenomes.

Sodium hydroxide treatment effectively inhibits PrP replication in farm soil.

Chronic wasting disease (CWD) agents are shed into biological samples, facilitating their horizontal transmission between cervid species. Once prions enter the environment, binding of PrP by soil particles may maintain them near the soil surface, posing a challenge for decontamination. A 2 N sodium hydroxide (NaOH) or 2% sodium hypochlorite (NaClO) solution is traditionally recommended for prion decontamination of equipment and surfaces.

Establishment of a Madin-Darby bovine kidney cell line expressing anchorless bovine prion protein.

Enzyme-linked immunosorbent assay (ELISA) performed using extensively purified bacterially expressed bovine prion protein (PrP) shows decreased cross-reactivity. We generated a transduced Madin-Darby bovine kidney (MDBK) cell line continuously expressing glycosylphosphatidylinositol (GPI)-anchorless bovine PrP (designated as MDBK ∆GPI protein) by using a lentiviral expression system. The present study also described the method for purifying bovine PrP through sequential culturing without the need for complex purification protocol.

Biological and biochemical characterization of M2B cells: Classical BSE prion is conserved in transgenic mice overexpressing bovine prion protein gene.

M2B cells with persistent classical bovine spongiform encephalopathy (C-BSE) have been established previously. In this study, we performed strain characterization of the M2B cell line in bovine PrP overexpressing mice (Tg 1896). Mice intracranially inoculated with M2B cells and C-BSE survived for 451 ± 7 and 465 ± 31 d post inoculation, respectively.