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| A SINGLE HAMSTER PRP AMINO-ACID BLOCKS CONVERSION TO PROTEASE-RESISTANT PRP IN SCRAPIE-INFECTED MOUSE NEUROBLASTOMA-CELLS |
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| Author(s): PRIOLA SA, CHESEBRO B |
| Source: JOURNAL OF VIROLOGY Volume: 69 Issue: 12 Pages: 7754-7758 Published: DEC 1995 |
| Times Cited: 84 References: 41 |
| Abstract: Neurodegeneration caused by the transmissible spongiform encephalopathies is associated with the conversion of a normal host protein, PrP-sen, into an abnormal aggregated protease-resistant form, PrP-res. In scrapie-infected mouse neuroblastoma cells, mouse PrP-sen is converted into PrP-res but recombinant hamster PrP-sen expressed in these cells is not. In the present studies, recombinant hamster/mouse PrP-sen molecules were expressed in these scrapie-infected cells to define specific PrP amino acid residues critical for the conversion to PrP-res. The results showed that homology to the region of mouse PrP-sen from amino acid residues 112 to 138 was required for conversion of recombinant PrP-sen to PrP-res in scrapie-infected mouse cells. Furthermore, a single hamster-specific PrP amino acid at residue 138 could inhibit the conversion of the recombinant PrP-sen into PrP-res. The data are consistent,vith studies in humans which show that specific amino acid residue changes within PrP can influence disease pathogenesis and transmission of transmissible spongiform encephalopathies across species barriers. |
| Document Type: Article |
| Language: English |
| Reprint Address: PRIOLA, SA (reprint author), NIAID, ROCKY MT LABS, PERSISTENT VIRAL DIS LAB, HAMILTON, MT 59840 USA |
| Publisher: AMER SOC MICROBIOLOGY, 1325 MASSACHUSETTS AVENUE, NW, WASHINGTON, DC 20005-4171 |
| Subject Category: Virology |
| IDS Number: TE366 |
| ISSN: 0022-538X |
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