Antiaggregating antibody raised against human PrP 106-126 recognizes pathological and normal isoforms of the whole prion protein

Eilat Hanan, Suzette A. Priola, Beka Solomon

Research output: Contribution to journalArticlepeer-review

Abstract

Antibodies to the prion protein (PrP) have been critical to the neuropathological and biochemical characterization of PrP-related degenerative diseases in humans and animals. Although PrP is highly conserved evolutionarily, there is some sequence divergence among species; as a consequence, anti-PrP antibodies have a wide spectrum of reactivity when challenged with PrP from diverse species. We have produced an antibody [monoclonal antibody (mAb) 2-40] raised against a synthetic peptide corresponding to residues (106-126 of human PrP and have characterized it by epitope mapping, Western immunoblot analysis, and immunohistochemistry. The antibody recognizes not only human PrP isoforms but also pathological PrP from all species tested (i.e., sheep, hamsters, and mice). Together with the fact that it recognizes the whole PrP in both cellular and scrapie isoforms, mAb 2-40 may be helpful in studying conformational changes of the PrP, as well as establishing a possible connection between human and animal diseases.

Original languageEnglish
Pages (from-to)693-703
Number of pages11
JournalCellular and Molecular Neurobiology
Volume21
Issue number6
DOIs
StatePublished - 2001

Keywords

  • Immunomodulation
  • Monoclonal antibody
  • PrP 106-126
  • Prion protein

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