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Fundamentals of prions and their inactivation (review)

Akikazu Sakudo1, Yasuhisa Ano, Takashi Onodera

  • 1Laboratory of Biometabolic Chemistry, School of Health Sciences, Faculty of Medicine, University of the Ryukyus, 207 Uehara, Nishihara, Okinawa, Japan. sakudo@med.u-ryukyu.ac.jp

International Journal of Molecular Medicine
|January 29, 2011
PubMed

Insights

Prions are infectious proteins causing fatal neurodegenerative diseases. Standard sterilization methods fail to inactivate prions, necessitating specialized procedures to prevent disease transmission.

Area of Science:

  • Neuroscience
  • Infectious Diseases
  • Biochemistry

Background:

  • Prions are misfolded proteins (PrPSc) responsible for transmissible spongiform encephalopathies like BSE and CJD.
  • The normal cellular prion protein (PrPC) has physiological roles, including anti-oxidative stress.
  • PrPSc arises from PrPC through conformational changes.

Purpose of the Study:

  • To review the fundamental nature of prions.
  • To discuss the challenges in prion inactivation.
  • To highlight the importance of effective prion decontamination.

Main Methods:

  • Review of existing literature on prion biology.
  • Analysis of conventional sterilization techniques.
  • Evaluation of prion resistance to inactivation methods.

Main Results:

  • Prions are highly resistant to standard disinfection and sterilization.
  • Common methods like alcohol, autoclaving (121°C, 20 min), and gamma irradiation are ineffective against prions.
  • Iatrogenic transmission of prion diseases underscores the need for validated inactivation protocols.

Conclusions:

  • Prion inactivation requires specialized protocols beyond conventional methods.
  • Effective prion decontamination is critical for preventing iatrogenic disease transmission.
  • Further research into robust prion inactivation strategies is essential.

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