Pulling rabbits to reveal the secrets of the prion protein

Pedro Fernandez-Funez, Yan Zhang, Jonatan Sanchez-Garcia, Kurt Jensen, Wen Quan Zou, Diego E. Rincon-Limas

Research output: Contribution to journalShort survey

15 Citations (Scopus)

Abstract

The Prion protein (PrP) is a membrane-tethered glycoprotein that plays a central role in a unique class of neurodegenerative diseases that affect humans and other mammals. Prion diseases have genetic and sporadic origins, but their infectious nature sets them apart from other neurodegenerative disorders. According to the "protein-only" hypothesis, misfolded PrP conformers (prions) are responsible for both spongiform degeneration of the brain and disease transmissibility. Thus, understanding PrP conformational dynamics is key to developing effective therapies. Classic studies showing the different susceptibility to prion disease in mammals have recently found support in structural and transgenic studies with PrP from susceptible (mouse, hamster) and resistant (rabbit, horse, dog) animals. These studies identify key residues in PrP that determine both PrP structure and its propensity to acquire a ß-structure conformation proposed to be neurotoxic.

Original languageEnglish (US)
Pages (from-to)262-266
Number of pages5
JournalCommunicative and Integrative Biology
Volume4
Issue number3
DOIs
StatePublished - May 1 2011

Fingerprint

prions
rabbits
Rabbits
Prion Diseases
Neurodegenerative Diseases
Mammals
prion diseases
neurodegenerative diseases
Prions
Membrane Glycoproteins
Brain Diseases
mammals
membrane glycoproteins
Cricetinae
Horses
protein structure
Prion Proteins
Dogs
hamsters
genetically modified organisms

Keywords

  • Drosophila models
  • Neurotoxicity
  • Prion diseases
  • Prion protein
  • Protein structure

Cite this

Fernandez-Funez, P., Zhang, Y., Sanchez-Garcia, J., Jensen, K., Zou, W. Q., & Rincon-Limas, D. E. (2011). Pulling rabbits to reveal the secrets of the prion protein. Communicative and Integrative Biology, 4(3), 262-266. https://doi.org/10.4161/cib.4.3.15054

Pulling rabbits to reveal the secrets of the prion protein. / Fernandez-Funez, Pedro; Zhang, Yan; Sanchez-Garcia, Jonatan; Jensen, Kurt; Zou, Wen Quan; Rincon-Limas, Diego E.

In: Communicative and Integrative Biology, Vol. 4, No. 3, 01.05.2011, p. 262-266.

Research output: Contribution to journalShort survey

Fernandez-Funez, P, Zhang, Y, Sanchez-Garcia, J, Jensen, K, Zou, WQ & Rincon-Limas, DE 2011, 'Pulling rabbits to reveal the secrets of the prion protein', Communicative and Integrative Biology, vol. 4, no. 3, pp. 262-266. https://doi.org/10.4161/cib.4.3.15054
Fernandez-Funez, Pedro ; Zhang, Yan ; Sanchez-Garcia, Jonatan ; Jensen, Kurt ; Zou, Wen Quan ; Rincon-Limas, Diego E. / Pulling rabbits to reveal the secrets of the prion protein. In: Communicative and Integrative Biology. 2011 ; Vol. 4, No. 3. pp. 262-266.
@article{8d4ff33996e64cfe9cd5f6a710bd92a1,
title = "Pulling rabbits to reveal the secrets of the prion protein",
abstract = "The Prion protein (PrP) is a membrane-tethered glycoprotein that plays a central role in a unique class of neurodegenerative diseases that affect humans and other mammals. Prion diseases have genetic and sporadic origins, but their infectious nature sets them apart from other neurodegenerative disorders. According to the {"}protein-only{"} hypothesis, misfolded PrP conformers (prions) are responsible for both spongiform degeneration of the brain and disease transmissibility. Thus, understanding PrP conformational dynamics is key to developing effective therapies. Classic studies showing the different susceptibility to prion disease in mammals have recently found support in structural and transgenic studies with PrP from susceptible (mouse, hamster) and resistant (rabbit, horse, dog) animals. These studies identify key residues in PrP that determine both PrP structure and its propensity to acquire a {\ss}-structure conformation proposed to be neurotoxic.",
keywords = "Drosophila models, Neurotoxicity, Prion diseases, Prion protein, Protein structure",
author = "Pedro Fernandez-Funez and Yan Zhang and Jonatan Sanchez-Garcia and Kurt Jensen and Zou, {Wen Quan} and Rincon-Limas, {Diego E.}",
year = "2011",
month = "5",
day = "1",
doi = "10.4161/cib.4.3.15054",
language = "English (US)",
volume = "4",
pages = "262--266",
journal = "Communicative and Integrative Biology",
issn = "1942-0889",
publisher = "Landes Bioscience",
number = "3",

}

TY - JOUR

T1 - Pulling rabbits to reveal the secrets of the prion protein

AU - Fernandez-Funez, Pedro

AU - Zhang, Yan

AU - Sanchez-Garcia, Jonatan

AU - Jensen, Kurt

AU - Zou, Wen Quan

AU - Rincon-Limas, Diego E.

PY - 2011/5/1

Y1 - 2011/5/1

N2 - The Prion protein (PrP) is a membrane-tethered glycoprotein that plays a central role in a unique class of neurodegenerative diseases that affect humans and other mammals. Prion diseases have genetic and sporadic origins, but their infectious nature sets them apart from other neurodegenerative disorders. According to the "protein-only" hypothesis, misfolded PrP conformers (prions) are responsible for both spongiform degeneration of the brain and disease transmissibility. Thus, understanding PrP conformational dynamics is key to developing effective therapies. Classic studies showing the different susceptibility to prion disease in mammals have recently found support in structural and transgenic studies with PrP from susceptible (mouse, hamster) and resistant (rabbit, horse, dog) animals. These studies identify key residues in PrP that determine both PrP structure and its propensity to acquire a ß-structure conformation proposed to be neurotoxic.

AB - The Prion protein (PrP) is a membrane-tethered glycoprotein that plays a central role in a unique class of neurodegenerative diseases that affect humans and other mammals. Prion diseases have genetic and sporadic origins, but their infectious nature sets them apart from other neurodegenerative disorders. According to the "protein-only" hypothesis, misfolded PrP conformers (prions) are responsible for both spongiform degeneration of the brain and disease transmissibility. Thus, understanding PrP conformational dynamics is key to developing effective therapies. Classic studies showing the different susceptibility to prion disease in mammals have recently found support in structural and transgenic studies with PrP from susceptible (mouse, hamster) and resistant (rabbit, horse, dog) animals. These studies identify key residues in PrP that determine both PrP structure and its propensity to acquire a ß-structure conformation proposed to be neurotoxic.

KW - Drosophila models

KW - Neurotoxicity

KW - Prion diseases

KW - Prion protein

KW - Protein structure

UR - http://www.scopus.com/inward/record.url?scp=79960099910&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79960099910&partnerID=8YFLogxK

U2 - 10.4161/cib.4.3.15054

DO - 10.4161/cib.4.3.15054

M3 - Short survey

VL - 4

SP - 262

EP - 266

JO - Communicative and Integrative Biology

JF - Communicative and Integrative Biology

SN - 1942-0889

IS - 3

ER -