Prion Propagation
The Prion Hypothesis
Prions are unique infectious agents that consist only of a protein, and are not encoded by a nucleic acid. The wild type protein PrPc (Prion-related Protein) consisting of 209 amino acids in primarily alpha-helix secondary structures is expressed throughout the body, although the function is unknown. However, due to a mutation in the amino acid sequence or error in posttranslational protein folding, the PrPc protein is misfolded into an isoform PrPsc, which consists of mainly beta-sheet secondary structures.
The prion hypothesis, which states that prion proteins propagate themselves without nucleic acid involvement, is controversial because it contradicts the fundamental tenet of molecular biology: proteins are translated from RNA which is transcribed from DNA. However, while the precise mechanism of propagation is unclear, there is much evidence to support the theory that PrPsc is the primary, if not sole agent responsible for propagation of more PrPsc. Three methods of prion propagation have been identified as distinct, including sporadic, acquired, and inherited PrPsc accumulation.
Section 1
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Section 2
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Section 3
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Conclusion
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References
Edited by student of Joan Slonczewski for BIOL 238 Microbiology, 2009, Kenyon College.
