» Articles » PMID: 20177064

Tracing Conformational Transition of Abnormal Prion Proteins During Interspecies Transmission by Using Novel Antibodies

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2010 Feb 24
PMID 20177064
Citations 13
Authors
Affiliations
Soon will be listed here.
Abstract

Conformational differences in abnormal prion proteins (PrP(Sc)) have been postulated to produce different prion phenotypes. During the interspecies transmission of prions, the conformation of PrP(Sc) may change with passage; however, little is known about the mechanism of PrP(Sc) transition. In this study, novel PrP(Sc)-specific monoclonal antibodies (mAbs) were developed that could detect the PrP(Sc) of mouse but not that of sheep. By using these mAbs, we attempted to examine PrP(Sc) accumulated in mice inoculated with sheep scrapie serially up to five passages. The presence of PrP(Sc) in the mice was confirmed at all passages; however, mAb-bound PrP(Sc) conformer was detected only from the third passage onward. The generated mAb enabled tracing of a particular conformer during adaptation in sheep-to-mice transmission of prion, suggesting that the conformational transition of PrP(Sc) was caused by propagation of this conformer. Such mAbs capable of discriminating conformational differences may allow us to address questions concerning PrP(Sc) conformation and strain diversity.

Citing Articles

Enhancement of binding avidity by bivalent binding enables PrPSc-specific detection by anti-PrP monoclonal antibody 132.

Suzuki A, Yamasaki T, Hasebe R, Horiuchi M PLoS One. 2019; 14(6):e0217944.

PMID: 31170247 PMC: 6553756. DOI: 10.1371/journal.pone.0217944.


Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity.

Wang F, Wang X, Orru C, Groveman B, Surewicz K, Abskharon R PLoS Pathog. 2017; 13(7):e1006491.

PMID: 28704563 PMC: 5524416. DOI: 10.1371/journal.ppat.1006491.


Selective propagation of mouse-passaged scrapie prions with long incubation period from a mixed prion population using GT1-7 cells.

Miyazawa K, Masujin K, Okada H, Ushiki-Kaku Y, Matsuura Y, Yokoyama T PLoS One. 2017; 12(6):e0179317.

PMID: 28636656 PMC: 5479544. DOI: 10.1371/journal.pone.0179317.


Comparison of abnormal isoform of prion protein in prion-infected cell lines and primary-cultured neurons by PrPSc-specific immunostaining.

Tanaka M, Fujiwara A, Suzuki A, Yamasaki T, Hasebe R, Masujin K J Gen Virol. 2016; 97(8):2030-2042.

PMID: 27267758 PMC: 5770843. DOI: 10.1099/jgv.0.000514.


PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains.

Saijo E, Hughson A, Raymond G, Suzuki A, Horiuchi M, Caughey B J Virol. 2016; 90(10):4905-4913.

PMID: 26937029 PMC: 4859706. DOI: 10.1128/JVI.00088-16.


References
1.
Beringue V, Vilotte J, Laude H . Prion agent diversity and species barrier. Vet Res. 2008; 39(4):47. DOI: 10.1051/vetres:2008024. View

2.
Kuczius T, Groschup M . Differences in proteinase K resistance and neuronal deposition of abnormal prion proteins characterize bovine spongiform encephalopathy (BSE) and scrapie strains. Mol Med. 1999; 5(6):406-18. PMC: 2230428. View

3.
Shinagawa M, Takahashi K, Sasaki S, Doi S, Goto H, Sato G . Characterization of scrapie agent isolated from sheep in Japan. Microbiol Immunol. 1985; 29(6):543-51. DOI: 10.1111/j.1348-0421.1985.tb00856.x. View

4.
Prusiner S . Novel properties and biology of scrapie prions. Curr Top Microbiol Immunol. 1991; 172:233-57. DOI: 10.1007/978-3-642-76540-7_14. View

5.
Prusiner S . Prions. Proc Natl Acad Sci U S A. 1998; 95(23):13363-83. PMC: 33918. DOI: 10.1073/pnas.95.23.13363. View