Prion Protein in Milk

نویسندگان

  • Nicola Franscini
  • Ahmed El Gedaily
  • Ulrich Matthey
  • Susanne Franitza
  • Man-Sun Sy
  • Alexander Bürkle
  • Martin Groschup
  • Ueli Braun
  • Ralph Zahn
چکیده

BACKGROUND Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmission is possible. The low concentration of the proteinaceous agent in body fluids and its long incubation time complicate epidemiologic analysis and estimation of spreading and thus the risk of human infection. This situation is particularly unsatisfactory for food and pharmaceutical industries, given the lack of sensitive tools for monitoring the infectious agent. METHODOLOGY/PRINCIPAL FINDINGS We have developed an adsorption matrix, Alicon PrioTrap, which binds with high affinity and specificity to prion proteins. Thus we were able to identify prion protein (PrP(C))--the precursor of prions (PrP(Sc))--in milk from humans, cows, sheep, and goats. The absolute amount of PrP(C) differs between the species (from microg/l range in sheep to ng/l range in human milk). PrP(C) is also found in homogenised and pasteurised off-the-shelf milk, and even ultrahigh temperature treatment only partially diminishes endogenous PrP(C) concentration. CONCLUSIONS/SIGNIFICANCE In view of a recent study showing evidence of prion replication occurring in the mammary gland of scrapie infected sheep suffering from mastitis, the appearance of PrP(C) in milk implies the possibility that milk of TSE-infected animals serves as source for PrP(Sc).

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

A Study on The Effect of Temperature on Human Prion Protein Structure through Molecular Dynamic Simulation

Background & Aims: The normal form of the prion protein is called PrPC and its infectious form is called PrPSc. This protein functions like a crystallized core for the transformation of PrPc into an abnormal PrPSc. The aim of the present study was to investigate the effect of temperature on human prion protein structure through molecular dynamic simulation. Methods: In this research, the GROMAC...

متن کامل

Introducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation

The molecular dynamics (MD) simulation method is used to assess structural details for humanprion protein (hereafter PrPN) and its Asp178 Asn mutant (hereafter PrPm) which causes fatalfamilial insomnia disease. The results reveal that the flexibility and instability increase in PrPmcould be related to specific amino acids exposed to the solvent. Solvation free energy of PrPm is 20kjmot1nni2 mor...

متن کامل

Polymorphism of Prion Protein Gene (PRNP) in Iranian Holstein and Two Local Cattle Populations (Golpayegani and Sistani) of Iran

Bovine spongiform encephalopathy (BSE) is a fatal infectious neurodegenerative disease in cattle, characterized by the accumulation of an abnormal, proteaseresistant prion protein (PrPSc) in the brain. BSE is similar to scrapie in sheep and goats and Creuzfeldt-Jakob disease in humans. Susceptibility in cattle hasbeen shown to be under the influence of two polymorphic locations, which are...

متن کامل

Progress on Milk Safety in Relation to Prion Protein

Transmissible spongiform encephalopathies (TSEs) belong to prion diseases that are invariably common fatal neurological disorders and affect humans and animals. Prion protein (PrP) was regarded as the only infectious agent inprion diseases and much attention was focused on the safety of PrP in foodstuffs. In this review, theprogress on the safety of milk relation to PrP and transmission route o...

متن کامل

Mechanistic prospective for human PrPC conversion to PrPSc: Molecular dynamic insights

PrPC conversion to PrPSc isoform is the main known cause for prion diseases including Crutzfeldt-Jakob, Gerstmann-Sträussler-Sheinker syndrome and fatal familial insomnia in human. The precise mechanism underling this conversion is yet to be well understood. In the present work,  using the coordinate file of PrPC (available on the Protein Data Bank) as a starting structure, separate molecular d...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • PLoS ONE

دوره 1  شماره 

صفحات  -

تاریخ انتشار 2006