Techniques to elucidate the conformation of prions

doi:10.4331/wjbc.v6.i3.218

Advanced Search

BPG is committed to discovery and dissemination of knowledge

Home / Archive / Volume 6, Issue 3

This Article

Academic Content and Language Evaluation of This Article

CrossCheck and Google Search of This Article

Academic Rules and Norms of This Article

Citation of this article

Corresponding Author of This Article

Research Domain of This Article

Article-Type of This Article

Open-Access Policy of This Article

Times Cited Counts in Google of This Article

Number of Hits and Downloads for This Article

Total Article Views (8008)

All Articles published online

The chart showing PDF series, WORD series, HTML series, Figures (1-1) series.

Item

Count

PDF

458

WORD

346

HTML

3907

Figures (1-1)

473

Sum=5184

Publishing Process of This Article

The chart showing Browse series, Download series.

Item

Count

Browse

996

Download

1826

Sum=2822

Aug 26, 2015 (publication date) through Feb 12, 2026

Times Cited of This Article

Times Cited (1)

Journal Information of This Article

Publication Name

World Journal of Biological Chemistry

ISSN

1949-8454

Publisher of This Article

Baishideng Publishing Group Inc, 7041 Koll Center Parkway, Suite 160, Pleasanton, CA 94566, USA

- Full Article with Cover (PDF)
- Full Article (XML)

Minireviews

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.

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.

Keywords: Prion; Amyloid; Neurodegenerative disease; Protein structure; Fourier-transform infrared spectroscopy

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.