Epitope map of two polyclonal antibodies that recognize amyloid lesions in patients with Alzheimer's disease

J. Ghiso, T. Wisniewski, R. Vidal, A. Rostagno, B. Frangione

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Two synthetic peptides with sequences identical with those of fragments of the extracellular domain of the Alzheimer's disease amyloid precursor protein (APP) were used to raise antibodies. SP28 comprises positions 597-624 of the APP695 isoform, whereas SP41 extends towards the N-terminus (amino acids 584-624) and contains the entire SP28 peptide. Using e.l.i.s.a. and inhibition experiments we identified the two β-turn-containing segments 602-607 and 617-624 as the epitopes recognized by anti-SP41 and anti-SP28 respectively. Both antibodies immunolabelled amyloid lesions in brains from Alzheimer's-disease patients and patients with related disorders, whereas they were unreactive in control brains. However, when probed on immunoblots, anti-SP28 failed to detect full-length APP from baculovirus-infected Sf9 cells, and anti-SP41 reacted weakly compared with other anti-APP antisera. The data suggest that these antibodies are directed to conformational epitopes not existent in the native molecules but present after alternative APP processing.

Original languageEnglish (US)
Pages (from-to)517-522
Number of pages6
JournalBiochemical Journal
Volume282
Issue number2
DOIs
StatePublished - Jan 1 1992

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this