Related Experiment Video

Updated: Jun 4, 2026

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
11:41

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay

Published on: March 10, 2015

HEPES inhibits the conversion of prion protein in cell culture

Karine Delmouly1, Maxime Belondrade1, Danielle Casanova1

  • 1Institut de Génétique Humaine, CNRS-UPR 1142, 141 rue de la Cardonille, 34396 Montpellier Cedex 5, France.

The Journal of General Virology
|February 4, 2011
PubMed

Insights

The buffering agent HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) significantly inhibits prion protein (PrPSc) accumulation in live cells. This finding impacts prion research and offers potential for controlling prion propagation in cell cultures.

Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) is a common buffering reagent in cell culture.
  • HEPES is known to influence cellular processes, including molecule uptake, oxidative stress, and ion channel activity.

Purpose of the Study:

  • To investigate the effect of HEPES on prion protein accumulation in infected cells.
  • To determine if HEPES influences the biology or environment of prion protein.

Main Methods:

  • Cell culture experiments using prion-infected cells.
  • Monitoring the accumulation of the abnormal prion protein isoform (PrPSc) in the presence of varying HEPES concentrations.

Main Results:

  • HEPES demonstrated a concentration-dependent inhibition of PrPSc accumulation in live cells.
  • This inhibitory effect was specific to live cells, suggesting a biological mechanism rather than a direct chemical interaction.
  • The findings suggest HEPES modifies the cellular environment or prion biology.

Conclusions:

  • HEPES can significantly inhibit prion protein accumulation in cell culture models.
  • Results necessitate re-evaluation of previous cell biology studies using HEPES buffers.
  • The inhibitory effect of HEPES may offer a novel strategy for preventing prion contamination and propagation in cell cultures.

More Related Videos

A Cell Culture Model for Producing High Titer Hepatitis E Virus Stocks10:28

A Cell Culture Model for Producing High Titer Hepatitis E Virus Stocks

Published on: June 26, 2020

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors16:49

Two Methods of Heterokaryon Formation to Discover HCV Restriction Factors

Published on: July 16, 2012

Related Concept Videos

Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...