Variant CJD: the present position and future possibilities

Knight, Richard

doi:10.1016/j.ijporl.2003.08.030

Cited by 6 publications

(2 citation statements)

References 18 publications

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“…The emergence of variant Creutzfeldt-Jakob disease (vCJD) has led to major research programmes to understand the epidemiology and transmission routes as well methods for the control of prions which are known to be resistant to standard decontamination and sterilisation procedures. The initial forecast in the number of persons succumbing to this disease fortunately did not materialise, and the transmission to humans via cattle was controlled early on (Ghani et al ., 2003 ;Hilton, 2000 ;Knight, 2003 ). However, despite a decrease in the number of vCJD cases over the last fi ve years there is still approximately 1 in 4000 of the UK population who may be asymptomatic (Ironside, 2012 ).…”

Section: Decontamination Of Prionsmentioning

confidence: 99%

Future trends in decontamination in hospitals and healthcare

Walker

2014

Decontamination in Hospitals and Healthcare

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Section: Decontamination Of Prionsmentioning

confidence: 99%

Future trends in decontamination in hospitals and healthcare

Walker

2014

Decontamination in Hospitals and Healthcare

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“…The diseases caused by these infectious prions include scrapie in sheep and goats, chronic wasting disease (CWD) in deer, elk and moose, bovine spongiform encephalopathy (BSE) in cattle and assorted forms of Creutzfeldt-Jakob disease (CJD) including familial, sporadic, and the recently discovered variant forms (vCJD) in humans. 4,38,35,[43][44][45]88 TSEs are characterized pathologically by the vacuolation and loss of neurons in the central nervous system and the accumulation of the disease isoform (PrP Sc ) of host normal cellular prion protein (PrP C ). 65 PrP C has been found in various types of cells and tissues including the central nervous system, myoblasts and myotubes, vascular endothelial cells, reproductive tissues and cells of hemopoietic lineage.…”

Section: Introductionmentioning

confidence: 99%

Susceptibility of cell substrates to PrP^Scinfection and safety control measures related to biological and biotherapeutical products

LeBrun

Huang²,

Li³

2008

Prion

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Concerns over the potential for infectious prion proteins to contaminate human biologics and biotherapeutics have been raised from time to time. Transmission of the pathogenic form of prion protein (PrP(Sc)) through veterinary vaccines has been observed, yet no human case through the use of vaccine products has been reported. However, iatrogenic transmissions of PrP(Sc) in humans through blood components, tissues and growth hormone have been reported. These findings underscore the importance of reliable detection or diagnostic methods to prevent the transmission of prion diseases, given that the number of asymptomatic infected individuals remains unknown, the perceived incubation time for human prion diseases could be decades, and no cure of the diseases has been found yet. A variety of biochemical and molecular methods can selectively concentrate PrP(Sc) to facilitate its detection in tissues and cells. Furthermore, some methods routinely used in the manufacturing process of biological products have been found to be effective in reducing PrP(Sc) from the products. Questions remain unanswered as to the validation criteria of these methods, the minimal infectious dose of the PrP(Sc) required to cause infection and the susceptibility of cells used in gene therapy or the manufacturing process of biological products to PrP(Sc) infections. Here, we discuss some of these challenging issues.

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One gene, two diseases and three conformations: Molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures

Shamsir

Dalby

2005

Proteins

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Fatal familial insomnia (FFI) and Creutzfeldt-Jakob disease (CJD) are associated to the same mutation at codon 178 but differentiate into clinicopathologically distinct diseases determined by this mutation and a naturally occurring methionine-valine polymorphism at codon 129 of the prion protein gene. It has been suggested that the clinical and pathological difference between FFI and CJD is caused by different conformations of the prion protein. Using molecular dynamics (MD), we investigated the effect of the mutation at codon 178 and the polymorphism at codon 129 on prion protein dynamics and conformation at normal and elevated temperatures. Four model structures were examined with a focus on their dynamics and conformational changes. The results showed differences in stability and dynamics between polymorphic variants. Methionine variants demonstrated a higher stability than valine variants. Elongation of existing beta-sheets and formation of new beta-sheets was found to occur more readily in valine polymorphic variants. We also discovered the inhibitory effect of proline residue on existing beta-sheet elongation.

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Variant CJD: the present position and future possibilities

Cited by 6 publications

References 18 publications

Future trends in decontamination in hospitals and healthcare

Future trends in decontamination in hospitals and healthcare

Susceptibility of cell substrates to PrP^Scinfection and safety control measures related to biological and biotherapeutical products

One gene, two diseases and three conformations: Molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures

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Variant CJD: the present position and future possibilities

Cited by 6 publications

References 18 publications

Future trends in decontamination in hospitals and healthcare

Future trends in decontamination in hospitals and healthcare

Susceptibility of cell substrates to PrPScinfection and safety control measures related to biological and biotherapeutical products

One gene, two diseases and three conformations: Molecular dynamics simulations of mutants of human prion protein at room temperature and elevated temperatures

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Product

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About

Susceptibility of cell substrates to PrP^Scinfection and safety control measures related to biological and biotherapeutical products