Navigation Links
Brown team finds crucial protein role in deadly prion spread

A single protein plays a major role in deadly prion diseases by smashing up clusters of these infectious proteins, creating the "seeds" that allow fatal brain illnesses to quickly spread, new Brown University research shows.

The findings are exciting, researchers say, because they might reveal a way to control the spread of prions through drug intervention. If a drug could be made that inhibits this fragmentation process, it could substantially slow the spread of prions, which cause mad cow disease and scrapie in animals and, in rare cases, Creutzfeldt-Jacob disease and kuru in humans.

Because similar protein replication occurs in Alzheimer's and Parkinson's diseases, such a drug could also slow progression of these diseases as well.

"The protein fragmentation we studied has a big impact on how fast prion diseases spread and may also play a role in the accumulation of toxic proteins in neurodegenerative diseases like Parkinson's," said Tricia Serio, an assistant professor in Brown's Department of Molecular Biology, Cell Biology and Biochemistry and lead researcher on the project.

The findings from Serio and her team, which appear online in PLoS Biology, build on their groundbreaking work published in Nature in 2005. That research showed that prions ?strange, self-replicating proteins that cause fatal brain diseases ?convert healthy protein into abnormal protein through an ultrafast process.

This good-gone-bad conversion is one way that prions multiply and spread disease. But scientists believe that there is another crucial step in this propagation process ?fragmentation of existing prion complexes. Once converted, the thinking goes, clusters of "bad" or infectious protein are smashed into smaller bits, a process that creates "seeds" so that prions multiply more quickly in the body. Hsp104, a molecule known to be required for prion replication, could function as this protein "crusher," Serio thought.

To test th ese ideas, Serio and members of her lab studied Sup35, a yeast protein similar to the human prion protein PrP. They put Sup35 together with Hsp104, then activated and deactivated Hsp104. They found that the protein does, indeed, chop up Sup35 complexes ?the first direct evidence that this process occurs in a living cell and that Hsp104 is the culprit.

"To understand how fragmentation speeds the spread of prions, think of a dandelion," Serio said. "A dandelion head is a cluster of flowers that each carries a seed. When the flower dries up and the wind blows, the seeds disperse. Prion protein works the same way. Hsp104 acts like the wind, blowing apart the flower and spreading the seeds."

Serio said that prions still multiply without fragmentation. However, she said, they do so at a much slower rate. So a drug that blocked the activity of Hsp104 could seriously slow progression of prion-related diseases.


'"/>

Source:Brown University


Related biology news :

1. Brown-Harvard team solves mobile DNAs surgical sleight-of-hand
2. Prions rapidly remodel good protein into bad, Brown study shows
3. Brown seaweed contains promising fat fighter, weight reducer
4. Brown scientists map structure of DNA-doctoring protein complex
5. Brown cancer biologists identify major player in cell growth
6. Bones in motion: Brown scientists to create new 3-D X-ray system
7. Current human embryonic stem cell lines contaminated UCSD/Salk team finds
8. Study finds more than one-third of human genome regulated by RNA
9. ASU researchers finds novel chemistry at work to provide parrots vibrant red colors
10. Same mutation aided evolution in many fish species, Stanford study finds
11. NC State scientist finds soft tissue in T. rex bones
Post Your Comments:
*Name:
*Comment:
*Email:


(Date:4/11/2017)... BROOKLYN, N.Y. , April 11, 2017 /PRNewswire-USNewswire/ ... identical fingerprints, but researchers at the New York ... University College of Engineering have found that partial ... fingerprint-based security systems used in mobile phones and ... previously thought. The vulnerability lies in ...
(Date:4/5/2017)... , April 5, 2017  The Allen Institute for ... Cell Explorer: a one-of-a-kind portal and dynamic digital window ... imaging data, the first application of deep learning to ... stem cell lines and a growing suite of powerful ... for these and future publicly available resources created and ...
(Date:4/4/2017)... YORK , April 4, 2017   EyeLock ... today announced that the United States Patent and Trademark ... patent broadly covers the linking of an iris image ... same transaction) and represents the company,s 45 th ... latest patent is very timely given the multi-modal biometric ...
Breaking Biology News(10 mins):
(Date:10/12/2017)... ... October 12, 2017 , ... They call it the “hairy ... a depiction of a system of linkages and connections so complex and dense ... of computer science at Worcester Polytechnic Institute (WPI) and director of the university’s ...
(Date:10/12/2017)... ca (PRWEB) , ... October 12, 2017 , ... ... the Surgical Wound Market with the addition of its newest module, US Hemostats ... $1.2B market for thrombin hemostats, absorbable hemostats, fibrin sealants, synthetic sealants and biologic ...
(Date:10/11/2017)... ... 11, 2017 , ... The CRISPR-Cas9 system has ... and avoiding the use of exogenous expression plasmids. The simplicity of programming this ... gain-of-function studies. , This complement to loss-of-function studies, such as with RNAi ...
(Date:10/11/2017)...  VMS BioMarketing, a leading provider of patient support solutions, ... Educator (CNE) network, which will launch this week. The VMS ... care professionals to enhance the patient care experience by delivering ... health care professionals to help women who have been diagnosed ... ...
Breaking Biology Technology: