Direct detection of disease associated prions in brain and lymphoid tissue using antibodies recognizing the extreme N terminus of PrPC.
Prion
; 1(2): 121-7, 2007.
Article
em En
| MEDLINE
| ID: mdl-19164886
ABSTRACT
A simple diagnostic test is described for the detection of TSE in bovine, ovine and human brain and lymphoid tissue that obviates the use of proteinase K as a discriminating reagent. The immunoassay utilises high affinity anti-peptide antibodies that appear blind to the normal isoform of prion protein (PrP(C)). These reagents have been produced with novel N-terminal chimeric peptides and we hypothesise that the retention and stability of the extreme N-terminus of PrP in the disease-associated aggregate makes it an operationally specific marker for TSE. Accordingly, the assay involves homogenisation of the tissue directly in 8M guanidine hydrochloride, a simple one-step capture of PrP(Sc) followed by detection with a europium-labelled anti-PrP(C) antibody. This rapid assay clearly differentiates between levels of disease-associated PrP extracted from brain and lymphoid tissues taken from confirmed TSE positive and negative cattle and sheep. The assay can also be used to detect PrP(Sc) in cases of vCJD.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Química Encefálica
/
Doenças Priônicas
/
Proteínas PrPSc
/
Proteínas PrPC
/
Tecido Linfoide
/
Anticorpos Monoclonais
Tipo de estudo:
Clinical_trials
/
Diagnostic_studies
/
Risk_factors_studies
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Prion
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Reino Unido