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Detecting Differences in Prion Protein Conformation by Quantifying Methionine Oxidation.

Christopher J Silva¹, Melissa Erickson-Beltran¹

¹Produce Safety & Microbiology Research Unit, Western Regional Research Center, United States Department of Agriculture, Agricultural Research Service, Albany, California 94710, United States.

|January 31, 2022

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Prion protein conformation, crucial for disease, can be studied by tracking methionine oxidation. This method helps identify prion strains, enhancing food safety measures.

Area of Science:

Biochemistry
Structural Biology
Food Safety

Background:

Prion diseases are linked to protein misfolding and conformational changes.
The chemical environment of amino acids within a prion influences its reactivity.
Methionine oxidation can serve as an indicator of surface-exposed residues and protein conformation.

Purpose of the Study:

To develop a method for quantifying methionine oxidation in prion peptides.
To utilize methionine oxidation as a tool for defining prion conformation.
To differentiate between prion strains for improved food safety.

Main Methods:

Peptide identification from digested recombinant prion protein and hamster-adapted scrapie (Sc237 strain).
Development of a multiple reaction monitoring (MRM)-based assay to quantify methionine oxidation.

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Analysis of methionine-containing peptides to assess conformational states.

Main Results:

Successfully identified and quantified methionine oxidation in specific prion-derived peptides.
Demonstrated that methionine oxidation patterns are dependent on prion conformation.
Showcased the potential to distinguish between different prion strains based on oxidation profiles.

Conclusions:

Methionine oxidation is a sensitive reporter of prion protein conformation.
The developed method offers a novel approach for prion strain characterization.
This technique holds significant implications for prion disease research and food safety surveillance.