Staff Publications

Staff Publications

  • external user (warningwarning)
  • Log in as
  • language uk
  • About

    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

    We have a manual that explains all the features 

Record number 370574
Title Molecular discrimination of atypical bovine spongiform encephalopathy strains from a geographical region spanning a wide area in Europe
Author(s) Jacobs, J.G.; Langeveld, J.P.M.; Biacabe, A.G.; Acutis, P.L.; Polak, M.P.; Gavier-Widen, D.; Buschmann, A.; Caramelli, M.; Casalone, C.; Mazza, M.; Groschup, M.; Erkens, J.H.F.; Davidse, A.; Zijderveld, F.G. van; Baron, T.
Source Journal of Clinical Microbiology 45 (2007)6. - ISSN 0095-1137 - p. 1821 - 1829.
DOI https://doi.org/10.1128/JCM.00160-07
Department(s) CVI - Divisie Bacteriologie en TSE's
CVI - Division Virology
CIDC - Divisie Bacteriologie en TSE's
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) transmissible mink encephalopathy - creutzfeldt-jakob-disease - abnormal prion protein - transgenic mice - monoclonal-antibodies - messenger-rna - scrapie agent - n-glycosidase - brain-stem - prp gene
Abstract 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 (PrPSc). 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 PrPSc (Prp(res)), suggesting the existence of at least two additional BSE PrPres variants. These are defined here as the H type and the L type, according to the higher and lower positions of the nonglycosylated PrPres band in Western blots, respectively, compared to the position of the band in classical BSE (C-type) isolates. These molecular Prpres 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 PrPres moieties which can both be glycosylated and which is thus indicative of the existence of two PrPres, 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.
Comments
There are no comments yet. You can post the first one!
Post a comment
 
Please log in to use this service. Login as Wageningen University & Research user or guest user in upper right hand corner of this page.