Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein
Proteinase-K resistant prion protein (PrPres) has the property to aggregate in TSE-injured animal tissues. We have developed a test method to discriminate scrapie-infected and mock-infected hamsters by detecting the PrPres in plasma. It seemed that aggregation of the PrPres with some heterogeneous m...
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Online Access: | https://doi.org/10.4137/MBI.S3103 |
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doaj-d0bd960ff2b04d5c853aba5d2fcc90a32020-11-25T03:26:30ZengSAGE PublishingMicrobiology Insights1178-63612009-01-01210.4137/MBI.S3103Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion ProteinKazuo Tsukui0Kenji Tadokoro1Department of Infectious Disease Research, Central Blood Institute, the Japanese Red Cross Society, 2-1-67 Tatsumi, Koto-ku, Tokyo 135-8521, Japan.Department of Infectious Disease Research, Central Blood Institute, the Japanese Red Cross Society, 2-1-67 Tatsumi, Koto-ku, Tokyo 135-8521, Japan.Proteinase-K resistant prion protein (PrPres) has the property to aggregate in TSE-injured animal tissues. We have developed a test method to discriminate scrapie-infected and mock-infected hamsters by detecting the PrPres in plasma. It seemed that aggregation of the PrPres with some heterogeneous molecule(s) enabled successful detection by this method. In order to investigate which molecule became the partner in the PrPres aggregates; we examined some molecules that could presumably have this ability. As a result, we found synthetic Poly-A RNA, especially in its denatured form, to be the most effective entity although glycoprotein, sulfated polysaccharide showed less effectiveness. DNA in the denatured form also has a high affinity, although in the presence of protein the effectiveness unsuccessful. On the basis of this result, it is possible that the PrPres aggregate in scrapie-infected hamster plasma is composed of PrPres and RNA.https://doi.org/10.4137/MBI.S3103 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Kazuo Tsukui Kenji Tadokoro |
spellingShingle |
Kazuo Tsukui Kenji Tadokoro Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein Microbiology Insights |
author_facet |
Kazuo Tsukui Kenji Tadokoro |
author_sort |
Kazuo Tsukui |
title |
Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein |
title_short |
Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein |
title_full |
Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein |
title_fullStr |
Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein |
title_full_unstemmed |
Affinity Association between Polynucleotide, Glycoprotein, or Sulfated Polysaccharides and Disease-Associated Prion Protein |
title_sort |
affinity association between polynucleotide, glycoprotein, or sulfated polysaccharides and disease-associated prion protein |
publisher |
SAGE Publishing |
series |
Microbiology Insights |
issn |
1178-6361 |
publishDate |
2009-01-01 |
description |
Proteinase-K resistant prion protein (PrPres) has the property to aggregate in TSE-injured animal tissues. We have developed a test method to discriminate scrapie-infected and mock-infected hamsters by detecting the PrPres in plasma. It seemed that aggregation of the PrPres with some heterogeneous molecule(s) enabled successful detection by this method. In order to investigate which molecule became the partner in the PrPres aggregates; we examined some molecules that could presumably have this ability. As a result, we found synthetic Poly-A RNA, especially in its denatured form, to be the most effective entity although glycoprotein, sulfated polysaccharide showed less effectiveness. DNA in the denatured form also has a high affinity, although in the presence of protein the effectiveness unsuccessful. On the basis of this result, it is possible that the PrPres aggregate in scrapie-infected hamster plasma is composed of PrPres and RNA. |
url |
https://doi.org/10.4137/MBI.S3103 |
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