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Journal of Clinical Microbiology, March 2005, p. 1118-1126, Vol. 43, No. 3
0095-1137/05/$08.00+0 doi:10.1128/JCM.43.3.1118-1126.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Institute of Pathology,1 Department of Neuroscience,3 Cancer Research Center, Case Western Reserve University School of Medicine, Cleveland, Ohio,4 Division of Neuropathology, University of Edinburgh, Edinburgh, United Kingdom2
Received 31 March 2004/ Returned for modification 18 June 2004/ Accepted 19 October 2004
We used different anti-prion protein (anti-PrP) monoclonal antibodies to capture either full-length or truncated PrP species and then used biotinylated lectin to compare the nature of the glycans on bound PrP species present in control, sporadic Creutzfeldt-Jakob disease (sCJD), or variant CJD (vCJD) brains. When full-length PrP species in these three groups were compared, no significant difference in the binding of concanavalin A or Aleuria aurantia lectin was detected. However, the binding of Ricinus communis agglutinin I (RCA) to sCJD and vCJD samples was significantly increased. In contrast, when only truncated PrP species were compared, only vCJD samples had more RCA binding activity. Therefore, while most of the RCA binding activity in sCJD is restricted to the full-length PrP species, the RCA binding activity in vCJD is associated with truncated and full-length PrP species. Furthermore, the RCA binding activity in sCJD and vCJD samples is mostly associated with proteinase K-resistant PrP species, a known signature of infectious prion. Therefore, PrP species in sCJD and vCJD have dissimilar lectin immunoreactivity, which reflects differences in their N-linked glycans. These differences may account for the distinct phenotypes of sCJD and vCJD.
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