Prion diseases are rare degenerative disorders of the nervous system caused by abnormal accumulation and/or metabolism of prion proteins. They are invariably fatal. Creutzfeldt-Jakob disease (CJD) is the most common human prion disease and the sporadic form accounts for 85% of cases, whilst about 15% are genetic and 1% is iatrogenic. Variant CJD (vCJD) was mostly seen in the UK and France and mainly affected young people. Sporadic CJD (sCJD) occurs throughout the world with mean age of onset in the seventh decade. It typically presents with rapidly declining cognition that may get confused with other forms of dementia. Thus identification of sCJD in older people depends on a judicious awareness of the clinical features. Here we present a clinical, pathological, therapeutic and diagnostic review of sCJD.

Polymorphisms at codons 136, 154 and 171 of the gene encoding the prion protein (PrP) are associated with susceptibility to classical scrapie in sheep. Genetic selection for scrapie resistance based on PrP genotypes is central to the scrapie eradication programme in Great Britain but there are concerns about how this may affect other economically important traits. The objective of this study was to evaluate associations of PrP genotypes with live weight and slaughter traits in a hill sheep breed in Great Britain. Data used were from an experimental flock of Swaledale sheep in which the alleles ARR, ARQ, AHQ and VRQ were present. About 1450 genotyped lambs with birth, marking and weaning weights, and 620 with slaughter records were used for the study. Mixed models with various fixed effects and random direct genetic and maternal effects were tested to determine the appropriate model to use for each trait. None of the differences in lamb performance between PrP genotypes consistently reached significance. Therefore, this study does not support existence of significant relationships between PrP genotype and lamb performance traits in this breed.

At the turn of the last century, infectious diseases represented an important cause of health morbidity and behavioral changes. Neurosyphilis, for example, was relatively common at the time and often led to the development of cognitive impairment and dementia. With the advent of effective antibiotic treatment, the association between infectious diseases and dementia became increasingly less frequent, although a resurgence of interest in this area has taken place during the past 15 years with the emergence of acquired immunodeficiency syndrome (AIDS) and variant Creutzfeldt–Jakob disease (vCJD). This paper reviews the most frequent infectious causes of dementia, including prion diseases, as well as infections caused by herpes virus, human immunodeficiency virus (HIV), toxoplasmosis, cryptococcus, cytomegalovirus, syphilis, borrelia and cysticercosis.

Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer's, Parkinson's, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig's disease), Huntington's, and type II (mature onset) diabetes. In many cases, it has been demonstrated that conformational change and aggregation can occur outside living cells and complex biochemical networks. Hence, approaches from materials and physical science have enhanced our understanding of the role of protein aggregation in these diseases at the molecular and nanoscale levels. In this article, we will review what is known about these protein structures from the perspective of materials science, focusing on the details of emergent oligomeric and nanotube-like structures, their interactions with model lipid bilayers, how the structures relate to observed biological phenomena, and how protein aggregation and amyloid formation can be employed for the good in biology and materials science.