Open AccessInfectious amyloid precursor gene sequences in primates used for experimental transmission of human spongiform encephalopathy.
Author(s) -
Larisa Červen̆áková,
Paul Brown,
Lev G. Goldfarb,
James W. Nagle,
Kristen Pettrone,
Richard Rubenstein,
Mark Dubnick,
Clarence J. Gibbs,
D. Carleton Gajdusek
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.25.12159
Subject(s) - biology , genetics , bovine spongiform encephalopathy , gene , transmissible spongiform encephalopathy , gorilla , homology (biology) , genotype , amino acid , virology , prion protein , scrapie , medicine , disease , paleontology , pathology
Based on the analysis of genomic DNA from single healthy animals of each of five primate species, nucleotide and predicted amino acid sequences of the infectious amyloid precursor gene of higher apes (Gorilla and Pan) and Old World (Macaca) and New World (Ateles, Saimiri) monkeys showed 95-99% homology to the human sequences, corresponding to their phylogenetic distance from humans. Two of 18 amino acids that differed from humans resulted from nucleotide changes at sites of mutations in humans with familial forms of spongiform encephalopathy (a deleted codon within the codon 51-91 region of 24 bp repeats and a substitution at codon 198). In each of the five animals, codon 129 specified methionine, the more common of the two polymorphic genotypes in humans. Because genotypic homology did not correlate with experimental transmission rates of human spongiform encephalopathy, primary structural similarity of the infectious amyloid precursor protein in humans and experimental primates may not be an important factor in disease transmissibility.