In prion research, which method is often used to demonstrate the presence of abnormal prion proteins?

• A. Microscopy
• B. Electrophoresis
• C. Western blotting
• D. DNA sequencing

Answer: (C)

The correct answer is Western blotting, a highly effective technique used in prion research to detect and characterize abnormal prion proteins. This method works by separating proteins based on their size using gel electrophoresis and then transferring them onto a membrane where they can be probed with specific antibodies that bind to the proteins of interest.

In the context of prion diseases, the abnormal prion protein (often referred to as PrP^Sc) has distinct properties compared to the normal prion protein (PrP^C), such as its resistance to protease digestion. Western blotting allows researchers to visualize these differences because the antibodies used will specifically bind to the abnormal prion proteins, facilitating their identification and quantification after exposure to a detection reagent.

This method is particularly valuable because it provides both qualitative and quantitative information about the presence of these abnormal proteins, which is crucial in understanding the pathology of prion diseases. Other methods, despite their utility in different contexts, do not provide the specificity or detail required for this type of analysis. For example, microscopy can visualize cell structures but does not offer the specific protein identification needed for prion proteins, while electrophoresis alone does not reveal the nature of the proteins without further techniques like Western blotting