Alimentary prion infections

Abstract

N eurodegenerative diseases are caused by proteinaceous aggregates, usually consisting of misfolded proteins which are often typified by a high proportion of β-sheets that accumulate in the central nervous system. These diseases, including Morbus Alzheimer, Parkinson disease and Transmissible Spongiform Encephalopathies (TSEs)-also termed prion disorders-afflict a substantial proportion of the human population and, as such, the etiology and pathogenesis of these diseases has been the focus of mounting research. Although many of these diseases arise from genetic mutations or are sporadic in nature, the possible horizontal transmissibility of neurodegenerative diseases poses a great threat to population health. In this article we discuss recent studies that suggest that the "non-transmissible" status bestowed upon Alzheimer and Parkinson diseases may need to be revised as these diseases have been successfully induced through tissue transplants. Furthermore, we highlight the importance of investigating the "natural" mechanism of prion transmission including peroral and perenteral transmission, proposed routes of gastrointestinal uptake and neuroinvasion of ingested infectious prion proteins. We examine the multitude of factors which may influence oral transmissibility and discuss the zoonotic threats that Chronic Wasting disease (CWD), Bovine Spongiform Encephalopathy (BSE) and Scrapie may pose resulting in vCJD or related disorders. In addition, we suggest that the 37 kDa/67 kDa laminin receptor on the cell surface of enterocytes, a major cell population in

Clay Components in Soil Dictate Environmental Stability and Bioavailability of Cervid Prions in Mice

“…Here we report that mice absorbed prions bound to soil significantly faster from the stomach and retained soil-bound prions significantly longer in the cecum, lymph nodes and spleen than unbound prions. Soil likely facilitated prion transport from the stomach to the small intestine, where we showed CD24 positive epithelial cells, including enterocytes and M cells previously shown to take up prions (Foster and Macpherson, 2010; Da Costa Dias et al, 2011; Donaldson et al, 2012; Kincaid et al, 2012), retain prions longer than unbound prions. Later, soil-bound prions were captured mainly by CD11b + /F4/80 + macrophages in Peyer's patches and spleen.…”

The Influence of Nutrition in Alzheimer's Disease: Neuroinflammation and the Microbiome vs. Transmissible Prion

“…Several experimental transmission routes have been investigated for prion disorders such as intra-ocular, intraventricular, intraperitoneal, intraspinal and subcutaneous injections, however, most prion diseases are contracted by ingestion of PrPSc (Da et al, 2011).…”

“…From here, prions can pass into the follicular dendritic cells, allowing their transport to the mesenteric lymphatic ganglions. In this way, the prion proteins can reach the enteric nervous system (ENS) and ultimately enter the CNS (Da et al, 2011).…”

“…Two theories can shed light on the mechanisms by which nutrition is involved, namely: the human microbiome as an important contributing factor to nutritional status, health, and disease (Bhattacharjee and Lukiw, 2013); and the appearance of prion disorders as a result of dietary exposure (Da et al, 2011).…”

Disorders of Protein Conformation as a Typical Component of Various Human Disease Pathogenesis

“…Оттуда молекулы приона переносятся в интестинальные лимфоузлы и распространяются по организму. Наряду с этим в лабораторных условиях доказана возможность транслокации прионов через кишечную стенку и в отсут-ствии М-клеток, с участием особого рецептора энтероци-тов -ламинина LRP/LR [28,29].…”