Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange

One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involve...

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Published in:	Nature structural & molecular biology Vol. 18; no. 4; pp. 504 - 506
Main Authors:	Surewicz, Witold K, Smirnovas, Vytautas, Baron, Gerald S, Offerdahl, Danielle K, Raymond, Gregory J, Caughey, Byron
Format:	Journal Article
Language:	English
Published:	New York Nature Publishing Group US 01-04-2011 Nature Publishing Group
Subjects:	631/1647/2258 631/45/535 692/699/375/365/1937 Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Brain Brain Chemistry brief-communication Deuterium Genetic aspects Hydrogen Ion exchange Life Sciences Mammals Mass Spectrometry Membrane Biology Molecular biology Physiological aspects Prion diseases Prions Prions - chemistry Protein Structure Proteins Risk factors Structure United States
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Abstract	One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrPSc consists of β-strands and relatively short turns and/or loops, with no native α-helices present.
AbstractList	One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP(Sc). Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrP(Sc). Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrP(Sc) consists of β-strands and relatively short turns and/or loops, with no native α-helices present. One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP super(Sc). Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrP super(Sc). Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrP super(Sc) consists of beta -strands and relatively short turns and/or loops, with no native alpha -helices present. Hydrogen-deuterium exchange/mass spec analysis of PrP Sc derived from mouse brains reveals that the infectious form of the prion adopts conformations that differ substantially from those previously postulated by various structural models. One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP Sc . Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrP Sc . Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80–90 to the C-terminus, which in PrP Sc consists of β-strands and relatively short turns and/or loops, with no native α-helices present. One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrPSc consists of β-strands and relatively short turns and/or loops, with no native α-helices present. One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrPSc consists of β-strands and relatively short turns and/or loops, with no native α-helices present. [PUBLICATION ABSTRACT]
Audience	Academic
Author	Baron, Gerald S Smirnovas, Vytautas Caughey, Byron Offerdahl, Danielle K Raymond, Gregory J Surewicz, Witold K
Author_xml	– sequence: 1 givenname: Witold K surname: Surewicz fullname: Surewicz, Witold K organization: Department of Physiology and Biophysics, Case Western Reserve University – sequence: 2 givenname: Vytautas surname: Smirnovas fullname: Smirnovas, Vytautas organization: Department of Physiology and Biophysics, Case Western Reserve University – sequence: 3 givenname: Gerald S surname: Baron fullname: Baron, Gerald S organization: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health – sequence: 4 givenname: Danielle K surname: Offerdahl fullname: Offerdahl, Danielle K organization: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health – sequence: 5 givenname: Gregory J surname: Raymond fullname: Raymond, Gregory J organization: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health – sequence: 6 givenname: Byron surname: Caughey fullname: Caughey, Byron organization: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/21441913$$D View this record in MEDLINE/PubMed
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Snippet	One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of... Hydrogen-deuterium exchange/mass spec analysis of PrP Sc derived from mouse brains reveals that the infectious form of the prion adopts conformations that... One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP(Sc). Here we used mass spectrometry analysis of... One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP super(Sc). Here we used mass spectrometry...
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SubjectTerms	631/1647/2258 631/45/535 692/699/375/365/1937 Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Brain Brain Chemistry brief-communication Deuterium Genetic aspects Hydrogen Ion exchange Life Sciences Mammals Mass Spectrometry Membrane Biology Molecular biology Physiological aspects Prion diseases Prions Prions - chemistry Protein Structure Proteins Risk factors Structure
Title	Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
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