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Glatzel, M; Pekarik, V; Lührs, T; Dittami, J; Aguzzi, A (2002). Analysis of the prion protein in primates reveals a new polymorphism in codon 226 (Y226F). Biological Chemistry, 383(6):1021-1025.

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Bovine spongiform encephalopathy has been epizootic in cows for the last two decades, and most probably causes variant Creutzfeldt-Jakob disease in humans. A thorough understanding of prion pathogenesis relies on suitable animal models. Modeling the transmission of BSE to primates is a crucial public health priority, necessary for determining the tissue distribution of the agent and for devising therapies. Susceptibility of humans to BSE is partly determined by polymorphism within the gene encoding the cellular prion protein, Prnp, a fact that must be taken into account in primate studies. However, no information is available on Prnp polymorphisms in primates. We have sequenced the Prnp open reading frames of 30 non-consanguineous Rhesus macaques. All macaques were homozygous for methionine at codon 129, which is polymorphic in humans and seems to modulate prion susceptibility. However, we identified a novel polymorphism in macaque Prnp, localized on codon 226 (Y226F). A modulatory effect of this polymorphism on the development of prion disease is possible because codon 226 is close to the suggested binding side of the factor X, which has been invoked as a determinant of the prion species barrier.


7 citations in Web of Science®
10 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Deposited On:11 Feb 2008 12:25
Last Modified:05 Apr 2016 12:20
Publisher:De Gruyter
Publisher DOI:10.1515/BC.2002.109
PubMed ID:12222676

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