Human Microbiology Institute have discovered prion-like domains in thousands of viruses, bolstering research that opens new ways of viral pathogenicity, suggests new targets for development of new antiviral drugs and links viruses to diseases such as Alzheimer’s and Parkinson’s.
Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition to the previously demonstrated pathogenic roles of prions during the development of different mammalian diseases, including neurodegenerative diseases, they have recently been shown to represent an important functional component in many prokaryotic and eukaryotic organisms and bacteriophages, confirming the previously unexplored important regulatory and functional roles.
Prions are infectious proteins that due to their β-sheet-rich conformation can self-propagate, leading to the accumulation of misfolded proteins in the brain possesses neurotoxic effects and are known to be implicated in neurodegenerative diseases. The reason for the human prions formation remains illusive.
In the paper, HMI discusses the discovery of over 2,600 proteins possessing prion-like structures across viruses.
The discovery of prions in viral proteins uncovers a previously unknown pathway for the development of diseases associated with protein misfolding, including Alzheimer’s and Parkinson’s diseases, ataxias and amyotrophic lateral sclerosis
Previous works have shown that viruses play a role in the development of some diseases listed above, and the discovery by HMI for the first time proposes that the misfolding of proteins is the previously unknown pathway for these prions to infect humans.
Moreover, the research suggests a new possible targets that can be used for the development of novel antiviral drugs, which could have huge implications in how we treat and fight a whole host of diseases.
In another aspect , this study explains the previously unknown mechanisms of viral pathogenicity
The research, was published in Nature’s Scientific Reports.