An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy

Pedro Piccardo, Jan P M Langeveld, Andrew F. Hill, Stephen Dlouhy, Katherine Young, Giorgio Giaccone, Giacomina Rossi, Marianna Bugiani, Orso Bugiani, Rob H. Meloen, John Collinge, Fabrizio Tagliavini, Bernardino Ghetti

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity (from strong immunopositivity to lack of reactivity) when challenged with PrP from diverse species. We have produced an antibody (anti-PrP95-108) raised against a synthetic peptide corresponding to residues 95 to 108 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (ie, cattle, sheep, hamsters, and mice). This is probably due to the fact that the epitope recognized by this antibody includes residues 100 to 108 of human PrP, a sequence that is also present in PrP of several other species. Thus, this reagent is valuable not only for the study of human prion diseases but also for analysis of the possible relationship between human and animal disorders.

Original languageEnglish
Pages (from-to)1415-1420
Number of pages6
JournalAmerican Journal of Pathology
Volume152
Issue number6
StatePublished - Jun 1998

Fingerprint

Bovine Spongiform Encephalopathy
Animal Diseases
Creutzfeldt-Jakob Syndrome
Prion Diseases
Conserved Sequence
Protein Isoforms
Antibodies
Prion Proteins
Epitope Mapping
Cricetinae
Epitopes
Anti-Idiotypic Antibodies
Sheep
Western Blotting
Immunohistochemistry

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. / Piccardo, Pedro; Langeveld, Jan P M; Hill, Andrew F.; Dlouhy, Stephen; Young, Katherine; Giaccone, Giorgio; Rossi, Giacomina; Bugiani, Marianna; Bugiani, Orso; Meloen, Rob H.; Collinge, John; Tagliavini, Fabrizio; Ghetti, Bernardino.

In: American Journal of Pathology, Vol. 152, No. 6, 06.1998, p. 1415-1420.

Research output: Contribution to journalArticle

Piccardo, P, Langeveld, JPM, Hill, AF, Dlouhy, S, Young, K, Giaccone, G, Rossi, G, Bugiani, M, Bugiani, O, Meloen, RH, Collinge, J, Tagliavini, F & Ghetti, B 1998, 'An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy', American Journal of Pathology, vol. 152, no. 6, pp. 1415-1420.
Piccardo, Pedro ; Langeveld, Jan P M ; Hill, Andrew F. ; Dlouhy, Stephen ; Young, Katherine ; Giaccone, Giorgio ; Rossi, Giacomina ; Bugiani, Marianna ; Bugiani, Orso ; Meloen, Rob H. ; Collinge, John ; Tagliavini, Fabrizio ; Ghetti, Bernardino. / An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. In: American Journal of Pathology. 1998 ; Vol. 152, No. 6. pp. 1415-1420.
@article{256c664c8882485692fccc89c89c06f8,
title = "An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy",
abstract = "Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity (from strong immunopositivity to lack of reactivity) when challenged with PrP from diverse species. We have produced an antibody (anti-PrP95-108) raised against a synthetic peptide corresponding to residues 95 to 108 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (ie, cattle, sheep, hamsters, and mice). This is probably due to the fact that the epitope recognized by this antibody includes residues 100 to 108 of human PrP, a sequence that is also present in PrP of several other species. Thus, this reagent is valuable not only for the study of human prion diseases but also for analysis of the possible relationship between human and animal disorders.",
author = "Pedro Piccardo and Langeveld, {Jan P M} and Hill, {Andrew F.} and Stephen Dlouhy and Katherine Young and Giorgio Giaccone and Giacomina Rossi and Marianna Bugiani and Orso Bugiani and Meloen, {Rob H.} and John Collinge and Fabrizio Tagliavini and Bernardino Ghetti",
year = "1998",
month = "6",
language = "English",
volume = "152",
pages = "1415--1420",
journal = "American Journal of Pathology",
issn = "0002-9440",
publisher = "Elsevier Inc.",
number = "6",

}

TY - JOUR

T1 - An antibody raised against a conserved sequence of the prion protein recognizes pathological isoforms in human and animal prion diseases, including Creutzfeldt-Jakob disease and bovine spongiform encephalopathy

AU - Piccardo, Pedro

AU - Langeveld, Jan P M

AU - Hill, Andrew F.

AU - Dlouhy, Stephen

AU - Young, Katherine

AU - Giaccone, Giorgio

AU - Rossi, Giacomina

AU - Bugiani, Marianna

AU - Bugiani, Orso

AU - Meloen, Rob H.

AU - Collinge, John

AU - Tagliavini, Fabrizio

AU - Ghetti, Bernardino

PY - 1998/6

Y1 - 1998/6

N2 - Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity (from strong immunopositivity to lack of reactivity) when challenged with PrP from diverse species. We have produced an antibody (anti-PrP95-108) raised against a synthetic peptide corresponding to residues 95 to 108 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (ie, cattle, sheep, hamsters, and mice). This is probably due to the fact that the epitope recognized by this antibody includes residues 100 to 108 of human PrP, a sequence that is also present in PrP of several other species. Thus, this reagent is valuable not only for the study of human prion diseases but also for analysis of the possible relationship between human and animal disorders.

AB - Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity (from strong immunopositivity to lack of reactivity) when challenged with PrP from diverse species. We have produced an antibody (anti-PrP95-108) raised against a synthetic peptide corresponding to residues 95 to 108 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (ie, cattle, sheep, hamsters, and mice). This is probably due to the fact that the epitope recognized by this antibody includes residues 100 to 108 of human PrP, a sequence that is also present in PrP of several other species. Thus, this reagent is valuable not only for the study of human prion diseases but also for analysis of the possible relationship between human and animal disorders.

UR - http://www.scopus.com/inward/record.url?scp=17344386598&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17344386598&partnerID=8YFLogxK

M3 - Article

VL - 152

SP - 1415

EP - 1420

JO - American Journal of Pathology

JF - American Journal of Pathology

SN - 0002-9440

IS - 6

ER -