The infectious potential of protein misfolding: insights from cross-over studies of prion diseases and common neurodegenerative disorders.

In recent years, important progress has been made in the study of the pathogenesis of neurodegenerative diseases, especially the role of protein misfolding and aberrant aggregation in the development of diseases has attracted much attention. As a class of zoonotic infectious neurodegenerative diseases caused by prion protein misfolding and aggregation, prion diseases, with their unique transmission characteristics, have provided important insights for the study of other neurodegenerative diseases. A growing body of research has shown that similar abnormal protein aggregation phenomena occur in common neurodegenerative diseases such as Alzheimer's disease (AD) and Parkinson's disease (PD). These misfolded proteins exhibit striking similarities to prions in terms of seeding capacity, cytotoxicity, and propagation properties. Further investigation into the prion-like behavior of these aberrant proteins in neurodegenerative diseases can offer new directions for diagnosis and treatment. Recent studies have demonstrated that AD can be transmitted through medical routes, which warns us that neurodegenerative diseases are potentially infectious and deserve further attention and research. This article systematically reviews the pathological features and transmission mechanisms of abnormal proteins in prion diseases and other neurodegenerative disorders, aiming to provide a new perspective for the prevention and treatment of these diseases. Moreover, this research holds significant implications for public health and clinical practice. By revealing the potential transmissibility of neurodegenerative diseases, it can help improve medical protocols and reduce the risk of iatrogenic transmission.