Molecular Discrimination of Atypical Bovine Spongiform Encephalopathy Strains from a Geographical Region Spanning a Wide Area in Europe
| Autor: | J. H. F. Erkens, Jan P. M. Langeveld, Mirosław P. Polak, Anne-Gaëlle Biacabe, Anne Buschmann, Maria Caramelli, Cristina Casalone, Thierry Baron, Pier Luigi Acutis, Maria Mazza, J. G. Jacobs, Fred G. van Zijderveld, Dolores Gavier-Widén, Aart Davidse, Martin H. Groschup |
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| Rok vydání: | 2007 |
| Předmět: |
Glycosylation
PrPSc Proteins n-glycosidase animal diseases chemistry.chemical_compound abnormal prion protein CIDC - Divisie Bacteriologie en TSE's Peptide sequence transmissible mink encephalopathy Transmissible spongiform encephalopathy biology food and beverages Antibodies Monoclonal Hydrogen-Ion Concentration Encephalopathy Bovine Spongiform Europe messenger-rna Endopeptidase K Antibody CVI - Division Virology brain-stem Microbiology (medical) Prions Bovine spongiform encephalopathy monoclonal-antibodies Blotting Western Molecular Sequence Data transgenic mice CVI - Divisie Virologie scrapie agent Virology medicine Animals Amino Acid Sequence creutzfeldt-jakob-disease prp gene Transmissible mink encephalopathy Genetic Variation Proteinase K medicine.disease nervous system diseases chemistry biology.protein CVI - Divisie Bacteriologie en TSE's Cattle Brain Stem |
| Zdroj: | Journal of Clinical Microbiology, 45(6), 1821-1829 Journal of Clinical Microbiology 45 (2007) 6 |
| ISSN: | 1098-660X 0095-1137 |
| DOI: | 10.1128/jcm.00160-07 |
| Popis: | Transmissible spongiform encephalopathy strains can be differentiated by their behavior in bioassays and by molecular analyses of the disease-associated prion protein (PrP) in a posttranslationally transformed conformation (PrP Sc ). Until recently, isolates from cases of bovine spongiform encephalopathy (BSE) appeared to be very homogeneous. However, a limited number of atypical BSE isolates have recently been identified upon analyses of the disease-associated proteinase K (PK) resistance-associated moiety of PrP Sc (PrP res ), suggesting the existence of at least two additional BSE PrP res variants. These are defined here as the H type and the L type, according to the higher and lower positions of the nonglycosylated PrP res band in Western blots, respectively, compared to the position of the band in classical BSE (C-type) isolates. These molecular PrP res variants, which originated from six different European countries, were investigated together. In addition to the migration properties and glycosylation profiles (glycoprofiles), the H- and L-type isolates exhibited enhanced PK sensitivities at pH 8 compared to those of the C-type isolates. Moreover, H-type BSE isolates exhibited differences in the binding of antibodies specific for N- and more C-terminal PrP regions and principally contained two aglycosylated PrP res moieties which can both be glycosylated and which is thus indicative of the existence of two PrP res populations or intermediate cleavage sites. These properties appear to be consistent within each BSE type and independent of the geographical origin, suggesting the existence of different BSE strains in cattle. The choice of three antibodies and the application of two pHs during the digestion of brain homogenates provide practical and diverse tools for the discriminative detection of these three molecular BSE types and might assist with the recognition of other variants. |
| Databáze: | OpenAIRE |
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