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Related Experiment Videos

Prion protein in milk.

Nicola Franscini1, Ahmed El Gedaily, Ulrich Matthey

  • 1Alicon AG, Schlieren, Switzerland.

Plos One
|December 22, 2006
PubMed
Summary
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A new adsorption matrix, Alicon PrioTrap, detects prion protein (PrP(C)) in milk from various species. This finding raises concerns about milk as a potential source of prion diseases, like transmissible spongiform encephalopathies (TSEs).

Area of Science:

  • Prion biology and disease transmission.
  • Food safety and public health.

Background:

  • Prions cause transmissible spongiform encephalopathies (TSEs) primarily in the central nervous system.
  • Evidence suggests prions are in body fluids, raising concerns about blood transmission and human infection risk.
  • Lack of sensitive detection tools hinders epidemiological analysis and risk assessment for industries.

Purpose of the Study:

  • To develop a sensitive method for detecting prion protein in body fluids.
  • To assess the presence and concentration of prion protein in milk from various species.

Main Methods:

  • Development of an adsorption matrix, Alicon PrioTrap, for high-affinity prion protein binding.
  • Identification of prion protein (PrP(C)), the precursor to prions (PrP(Sc)), in milk samples.

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Main Results:

  • Alicon PrioTrap successfully identified PrP(C) in milk from humans, cows, sheep, and goats.
  • PrP(C) concentrations varied by species, ranging from ng/l in human milk to µg/l in sheep milk.
  • PrP(C) was detected in commercial milk products, with ultrahigh temperature treatment only partially reducing its concentration.

Conclusions:

  • The presence of PrP(C) in milk suggests that milk from TSE-infected animals could be a source of PrP(Sc).
  • This finding has significant implications for food safety and the potential transmission of prion diseases through dairy products.