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Prion stability and infectivity in the environment.

Richard C Wiggins¹

¹National Health and Environmental Effects Research Laboratory, US EPA/Office of Research and Development, MD B305-02, Research Triangle Park, NC 27711, USA. wiggins.richard@epa.gov

Neurochemical Research

|May 17, 2008

Summary

Prion proteins, though not fully understood, exhibit remarkable environmental durability and infectivity. Their ability to bind minerals suggests a predisposition to misfolding, potentially creating long-lasting environmental reservoirs of disease.

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Area of Science:

Prion biology and environmental science.

Background:

Normal prion protein biology and infectivity of misfolded isoforms are not fully characterized.
Prion proteins challenge traditional views of protein behavior in biological systems.
Infectivity mechanism involves protein-only, homologous replication of misfolded isoforms.

Purpose of the Study:

To review the status of infectious prions in natural and man-made environments.
To explore the environmental durability and persistence of prion infectivity.
To investigate the role of mineral and metal surface binding in prion infectivity and durability.

Main Methods:

Review of existing scientific literature on prion protein behavior in various environments.
Analysis of studies investigating prion protein interactions with mineral and metal surfaces.
Evaluation of hypotheses regarding prion polypeptide binding to soil minerals and infectivity.

Main Results:

Prion proteins demonstrate extreme durability in diverse environmental conditions, potentially forming reservoirs of infectivity.
Prion proteins exhibit a strong propensity to bind to mineral and metal surfaces.
Evidence suggests bound prions, particularly on soil minerals, may be more infectious than purified forms.

Conclusions:

The binding propensity of prion polypeptides to minerals may predispose them to environmentally stable, misfolded conformations.
Environmental reservoirs of prions pose a persistent infectious risk.
Understanding environmental transmission is crucial for managing prion diseases with zoonotic potential.