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ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Virus and Prion Research » Research » Publications at this Location » Publication #91253
Title: IDENTIFICATION OF THE SUGAR RESIDUES OF THE CARBOHYDRATE MOIETY OF THE PRION PROTEIN FROM HAMSTER, SHEEP, AMERICAN ELK AND MULE DEER (INT.SYMP. "PRION & LENTIVIRAL DISEASES,"AUGUST 20-23,1998, REYKJAVIK, ICELAND

Author
item Schmerr, Mary Jo
item Goodwin, Kathryn
item JENNY, ALLEN - APHIS,NVSL,AMES, IA.
item WILLIAMS, E - UNIV.OF WY.,LARAMIE, WY.

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 8/23/1998
Publication Date: N/A
Citation: N/A

Interpretive Summary:

Technical Abstract: Characterization of the abnormal prion protein, PrP**sc, that is associated with transmissible spongiform encephalopathies (TSEs), is difficult because of the properties of this protein. However, elucidation of the pathogenesis of these diseases is dependent upon this characterization. Rodent adapted strains of scrapie have been used to characterize the properties of PrP**sc because of the high concentrations of PrP**sc in the brains of infected animals. Most of the characterization PrP**sc has been directed to the peptide backbone and not to the carbohydrate portion of this protein. In addition, there are few reports of direct characterization of PrP**sc from naturally infected animals such as sheep. In this study, we identified the sugar residues of the carbohydrate moiety of PrP**sc from sheep, American elk, mule deer and a hamster adapted strain of scrapie. Brain samples were obtained from animals that were showing clinical signs of infection with a TSE (scrapie in sheep; chronic wasting disease in elk and mule deer). The brains were homogenized in a buffer and subjected to treatment with 10% sarcosine and proteinase K treatment. PrP**sc was semi purified by a series of ultracentrifugations. The semi- purified samples were treated with SDS and run on SDS-PAGE and blotted onto nitrocellulose. The samples were incubated with several lectins specific for individual sugars. The blots were developed using a chemiluminescent substrate. The signal was captured using x-ray film. Different sugar residues as well as different patters of glycosylation for the isoforms of PrP**sc were observed among the species tested. This identification of the sugar residues is important in understanding the function of the carbohydrate moiety of PrP**sc in natural infections.