Daus ML. Techniques to elucidate the conformation of prions. World J Biol Chem 2015; 6(3): 218-222 [PMID: 26322176 DOI: 10.4331/wjbc.v6.i3.218]
Corresponding Author of This Article
Dr. Martin L Daus, ZBS6 - Proteomics and Spectroscopy, Robert Koch-Institute, Seestrasse 10, 13353 Berlin, Germany. dausm@rki.de
Research Domain of This Article
Biochemistry & Molecular Biology
Article-Type of This Article
Minireviews
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
World J Biol Chem. Aug 26, 2015; 6(3): 218-222 Published online Aug 26, 2015. doi: 10.4331/wjbc.v6.i3.218
Techniques to elucidate the conformation of prions
Martin L Daus
Martin L Daus, ZBS6 - Proteomics and Spectroscopy, Robert Koch-Institute, 13353 Berlin, Germany
Author contributions: Daus ML wrote the paper.
Supported by Alberta Prion Research Institute, Canada (Project title: “Comprehensive Risk Assessment of CWD Transmission to Humans Using Non-human Primates”); and European Metrology Research Programme (EMRP); Researcher Grant: HLT10-BiOrigin (Metrology for the Biomolecular Origin of Disease).
Conflict-of-interest statement: The author declares no conflicts of interest.
Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Correspondence to: Dr. Martin L Daus, ZBS6 - Proteomics and Spectroscopy, Robert Koch-Institute, Seestrasse 10, 13353 Berlin, Germany. dausm@rki.de
Telephone: +49-30-187542844 Fax: +49-30-187542664
Received: March 11, 2015 Peer-review started: March 16, 2015 First decision: April 27, 2015 Revised: May 10, 2015 Accepted: June 15, 2015 Article in press: June 16, 2015 Published online: August 26, 2015 Processing time: 167 Days and 13.7 Hours
Abstract
Proteinaceous infectious particles (prions) are unique pathogens as they are devoid of any coding nucleic acid. Whilst it is assumed that prion disease is transmitted by a misfolded isoform of the cellular prion protein, the structural insight of prions is still vague and research for high resolution structural information of prions is still ongoing. In this review, techniques that may contribute to the clarification of the conformation of prions are presented and discussed.
Core tip: Prions (proteinaceous infectious particles) are misfolded isoforms of cellular proteins that cause neurodegenerative diseases in mammals and humans. Several structural models are available for prions but a 3D-structure does still not exist. More structural information is demanded for the understanding of the conversion process and finally for the design of efficient therapeutic approaches. In this review, techniques that may contribute to the clarification of the conformation of prions are presented.
