Novel antibody-lectin enzyme-linked immunosorbent assay that distinguishes prion proteins in sporadic and variant cases of Creutzfeldt-Jakob disease

Tao Pan, Ruliang Li, Boon-Seng Wong, Shin-Chung Kang, James Ironside, Man-Sun Sy

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)1118-26
Number of pages9
JournalJournal of Clinical Microbiology
Volume43
Issue number3
DOIs
Publication statusPublished - Mar 2005

Keywords

  • Biotinylation
  • Creutzfeldt-Jakob Syndrome
  • Diagnosis, Differential
  • Endopeptidase K
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Plant Lectins
  • Polysaccharides
  • Prions

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