Prions are extremely resilient, infectious proteins. Studying their shape-shifting abilities could reveal lessons for how proteins fold at a molecular level, helping scientists design better ones.
Thank you for this excellent article. I've been out of the 'business' for a long time, but I used to be very interested in the subject. I was a fresh post-doc at an institute in Germany almost three and a half decades ago working on mad cow disease and scrapie. My supervisor at the time was a classically minded virologist and he spent a lot of energy (and students) trying to extract some virus-like nucleic acid structures from the infectious agent that later became the 'prion'. His 'dogma' was: these transmissible encephalopathies are forms of 'virus-induced amyloidosis'.
I experienced the controversy with/about Prusiner up close at the time. 'Prion' was almost a 'dirty word' for my boss - it was better not to use it in his presence. I then reoriented myself thematically, but it was an exciting time.
It's a long way from Anfinsen and Ramachandran in the 60s to what structural biology is doing today.
Yes, I remember those days! My wife and I completely stopped eating beef not long after the news came out but it created problems with friends.
I was best man at a friend's wedding. He came from a down-to-earth farming family. For the reception the mother brought out a huge beef mince and said "Here's the mad cow". I figured that if one meal was going to kill you then there wouldn't be enough of us left to keep society going so just ate it.
(Now of course we're trying to figure out how to not eat microplastics - it was so easy back then!)
Excellent article on a fascinating subject. It's fortunate that the stability of an infectious prion is inversely proportional to the speed of its self-replication and spread. If we can predict higher stability states for a deadly prion perhaps we can use synthetics prions to lock infectious oligomers into non-replicating states? Hopefully someday we can reduce the horrific mortality of prion diseases!
Very good article.I was a path resident in 1982 doing autopsies when we were very afraid of prion disease.I did one on an old man with neurodegenerative changes and no diagnosis ,possibly creutzefeld jacob disease but it turned out to be remote effects of neuro endocrine carcinoma.Perhaps this malignancy creates a similar protein to a prion?
Thank you for this excellent article. I've been out of the 'business' for a long time, but I used to be very interested in the subject. I was a fresh post-doc at an institute in Germany almost three and a half decades ago working on mad cow disease and scrapie. My supervisor at the time was a classically minded virologist and he spent a lot of energy (and students) trying to extract some virus-like nucleic acid structures from the infectious agent that later became the 'prion'. His 'dogma' was: these transmissible encephalopathies are forms of 'virus-induced amyloidosis'.
I experienced the controversy with/about Prusiner up close at the time. 'Prion' was almost a 'dirty word' for my boss - it was better not to use it in his presence. I then reoriented myself thematically, but it was an exciting time.
It's a long way from Anfinsen and Ramachandran in the 60s to what structural biology is doing today.
Yes, I remember those days! My wife and I completely stopped eating beef not long after the news came out but it created problems with friends.
I was best man at a friend's wedding. He came from a down-to-earth farming family. For the reception the mother brought out a huge beef mince and said "Here's the mad cow". I figured that if one meal was going to kill you then there wouldn't be enough of us left to keep society going so just ate it.
(Now of course we're trying to figure out how to not eat microplastics - it was so easy back then!)
Thank you for this wonderful story. It was a joy to read. I’m glad to hear you enjoyed our piece.
Excellent article on a fascinating subject. It's fortunate that the stability of an infectious prion is inversely proportional to the speed of its self-replication and spread. If we can predict higher stability states for a deadly prion perhaps we can use synthetics prions to lock infectious oligomers into non-replicating states? Hopefully someday we can reduce the horrific mortality of prion diseases!
Very good article.I was a path resident in 1982 doing autopsies when we were very afraid of prion disease.I did one on an old man with neurodegenerative changes and no diagnosis ,possibly creutzefeld jacob disease but it turned out to be remote effects of neuro endocrine carcinoma.Perhaps this malignancy creates a similar protein to a prion?
Fascinating!
This was a great read!!! thanks!!
Thank you for this excellent article. I've followed the Scrapie/Kuru story since university days.
Pathogens have always punched above their weight in research (you mentoned Streptococcus pneumoniae), presumably cos they attract grant money.
But I wonder if the formation of structural proteins (like KMEF group) might offer the same polymorphism but without the risk?
Super interesting. I'm going to put this in a folder as fodder for a future story. :)