scholarly journals Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation

2013 ◽  
Vol 135 (28) ◽  
pp. 10202-10205 ◽  
Author(s):  
Marcin I. Apostol ◽  
Kay Perry ◽  
Witold K. Surewicz
Keyword(s):  
Crystal Structure ◽  
Prion Protein ◽  
Protein Fragment ◽  
Oligomer Formation ◽  
Human Prion Protein

scholarly journals Crystal structure of human prion protein bound to a therapeutic antibody

2009 ◽  
Vol 106 (8) ◽  
pp. 2554-2558 ◽  
Author(s):  
S. V. Antonyuk ◽  
C. R. Trevitt ◽  
R. W. Strange ◽  
G. S. Jackson ◽  
D. Sangar ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Prion Protein ◽  
Therapeutic Antibody ◽  
Human Prion Protein

scholarly journals Sulphated glycosaminoglycans prevent the neurotoxicity of a human prion protein fragment

1998 ◽  
Vol 335 (2) ◽  
pp. 369-374 ◽  
Author(s):  
Mar PÉREZ ◽  
Francisco WANDOSELL ◽  
Camilo COLAÇO ◽  
Jesús AVILA
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Transmissible Spongiform Encephalopathies ◽  
Therapeutic Effects ◽  
Protein Fragment ◽  
Spongiform Encephalopathies ◽  
Sulphated Polysaccharides ◽  
Human Prion Protein ◽  
Sulphated Glycosaminoglycans

Although a number of features distinguish the disease isoform of the prion protein (PrPSc) from its normal cellular counterpart (PrPC) in the transmissible spongiform encephalopathies (TSEs), the neuropathogenesis of these diseases remains an enigma. The amyloid fibrils formed by fragments of human PrP have, however, been shown to be directly neurotoxic in vitro. We show here that sulphated polysaccharides (heparin, keratan and chondroitin) inhibit the neurotoxicity of these amyloid fibrils and this appears to be mediated via inhibition of the polymerization of the PrP peptide into fibrils. This provides a rationale for the therapeutic effects of sulphated polysaccharides and suggests a rapid in vitro functional screen for TSE therapeutics.

scholarly journals Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

2011 ◽  
Vol 59 (8) ◽  
pp. 965-971 ◽  
Author(s):  
Aya Kojima ◽  
Yasunori Mabuchi ◽  
Motomi Konishi ◽  
Rika Okihara ◽  
Makoto Nagano ◽  
...  
Keyword(s):  
Prion Protein ◽  
Metal Binding ◽  
Protein Fragment ◽  
Binding Ability ◽  
Human Prion Protein ◽  
Metal Binding Ability

Spectroscopic and Electronic Structure Studies of Copper(II) Binding to His111 in the Human Prion Protein Fragment 106−115: Evaluating the Role of Protons and Methionine Residues

2011 ◽  
Vol 50 (5) ◽  
pp. 1956-1972 ◽  
Author(s):  
Lina Rivillas-Acevedo ◽  
Rafael Grande-Aztatzi ◽  
Italia Lomelí ◽  
Javier E. García ◽  
Erika Barrios ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Prion Protein ◽  
Protein Fragment ◽  
Human Prion Protein ◽  
Methionine Residues

Recombinant Human Prion Protein Fragment 90–231, a Useful Model to Study Prion Neurotoxicity

2012 ◽  
Vol 16 (1-2) ◽  
pp. 50-59 ◽  
Author(s):  
Alessandro Corsaro ◽  
Stefano Thellung ◽  
Valentina Villa ◽  
Mario Nizzari ◽  
Antonio Aceto ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Fragment ◽  
Human Prion Protein

scholarly journals PACAP protects neuronal PC12 cells from the cytotoxicity of human prion protein fragment 106-126

FEBS Letters ◽  
2002 ◽  
Vol 522 (1-3) ◽  
pp. 65-70 ◽  
Author(s):  
Satomi Onoue ◽  
Keiichi Ohshima ◽  
Kosuke Endo ◽  
Takehiko Yajima ◽  
Kazuhisa Kashimoto
Keyword(s):  
Pc12 Cells ◽  
Prion Protein ◽  
Protein Fragment ◽  
Human Prion Protein ◽  
Neuronal Pc12 Cells

scholarly journals Structural studies on the folded domain of the human prion protein bound to the Fab fragment of the antibody POM1

2012 ◽  
Vol 68 (11) ◽  
pp. 1501-1512 ◽  
Author(s):  
Pravas Kumar Baral ◽  
Barbara Wieland ◽  
Mridula Swayampakula ◽  
Magdalini Polymenidou ◽  
Muhammad Hafiz Rahman ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Prion Protein ◽  
Prion Diseases ◽  
Passive Immunization ◽  
Antibody Fragment ◽  
Binding Mode ◽  
Cellular Prion Protein ◽  
Fab Fragment ◽  
Human Prion Protein

Prion diseases are neurodegenerative diseases characterized by the conversion of the cellular prion protein PrPcinto a pathogenic isoform PrPsc. Passive immunization with antiprion monoclonal antibodies can arrest the progression of prion diseases. Here, the crystal structure of the Fab fragment of an antiprion monoclonal antibody, POM1, in complex with human prion protein (huPrPc) has been determined to 2.4 Å resolution. The prion epitope of POM1 is in close proximity to the epitope recognized by the purportedly therapeutic antibody fragment ICSM18 Fab in complex with huPrPc. POM1 Fab forms a 1:1 complex with huPrPcand the measuredKdof 4.5 × 10−7 Mreveals moderately strong binding between them. Structural comparisons have been made among three prion–antibody complexes: POM1 Fab–huPrPc, ICSM18 Fab–huPrPcand VRQ14 Fab–ovPrPc. The prion epitopes recognized by ICSM18 Fab and VRQ14 Fab are adjacent to a prion glycosylation site, indicating possible steric hindrance and/or an altered binding mode to the glycosylated prion proteinin vivo. However, both of the glycosylation sites on huPrPcare positioned away from the POM1 Fab binding epitope; thus, the binding mode observed in this crystal structure and the binding affinity measured for this antibody are most likely to be the same as those for the native prion proteinin vivo.

scholarly journals Hypoxia protects neuronal cells from human prion protein fragment-induced apoptosis

2010 ◽  
Vol 112 (3) ◽  
pp. 715-722 ◽  
Author(s):  
Jae-Suk Seo ◽  
Jae-Won Seol ◽  
Myung-Hee Moon ◽  
Jae-Kyo Jeong ◽  
You-Jin Lee ◽  
...  
Keyword(s):  
Prion Protein ◽  
Neuronal Cells ◽  
Protein Fragment ◽  
Human Prion Protein ◽  
Induced Apoptosis
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