| Autor: |
Gilch S; Genecenter Munich, Max von Pettenkofer-Institute for Virology, Ludwig-Maximilians-University of Munich, Germany., Spielhaupter C, Schätzl HM |
| Jazyk: |
angličtina |
| Zdroj: |
Biological chemistry [Biol Chem] 2000 May-Jun; Vol. 381 (5-6), pp. 521-3. |
| DOI: |
10.1515/BC.2000.067 |
| Abstrakt: |
We describe the shortest prion protein allele known to date. Surprisingly, it is found as a polymorphism exactly in a species (prosimian lemurs) which seems highly susceptible to oral infection with BSE-derived prions. The truncation of the prion protein we found raises several questions. First, is the truncated octarepeat structure we describe, consisting of two octarepeats, still functional in copper binding? A second question is whether this truncation is related to the remarkable oral infectibility of lemurs with BSE-derived prions. And finally, one could argue that this genotype alone might favour development of a prion disease, even in the absence of exogenous infection. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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