Prions are infectious proteins that induce the misfolding of other proteins, leading to severe diseases; however, they do not influence gene expression.

Prions function by converting normal, properly folded proteins into their misfolded counterparts. This process results in the aggregation of misfolded proteins, which can inflict damage on cells and tissues. The misfolding occurs due to a change in the protein’s conformation, which subsequently disrupts its normal function and its interactions with other molecules.

Importantly, prions do not impact gene expression. Gene expression is the process through which the information encoded in a gene is utilized to synthesize a functional protein. Prions do not modify the genetic code, nor do they interfere with the transcription and translation processes necessary for protein synthesis. Instead, they act on pre-existing proteins, causing them to misfold.

The consequences of prion-induced protein misfolding can be catastrophic. Prion-related diseases include Creutzfeldt-Jakob disease, kuru, and bovine spongiform encephalopathy (commonly known as mad cow disease). These conditions are marked by the accumulation of misfolded proteins in the brain, leading to severe neurological symptoms such as dementia, loss of coordination, and muscle rigidity.

In conclusion, prions are responsible for the misfolding of proteins but do not alter gene expression. Understanding the mechanisms by which prions cause disease is crucial for the development of effective treatments and strategies to prevent the spread of prion diseases.