Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions
Identifieur interne : 000E71 ( Main/Exploration ); précédent : 000E70; suivant : 000E72Accessibility of a critical prion protein region involved in strain recognition and its implications for the early detection of prions
Auteurs : J. Yuan [États-Unis] ; Z. Dong [États-Unis] ; J.-P. Guo [Canada] ; J. Mcgeehan [Royaume-Uni] ; X. Xiao [États-Unis] ; J. Wang [États-Unis] ; I. Cali [États-Unis] ; P. L. Mcgeer [Canada] ; N. R. Cashman [Canada] ; R. Bessen [États-Unis] ; W. K. Surewicz [États-Unis] ; G. Kneale [Royaume-Uni] ; R. B. Petersen [États-Unis] ; P. Gambetti [États-Unis] ; W. Q. Zou [États-Unis]Source :
- Cellular and Molecular Life Sciences [ 1420-682X ] ; 2008-02-01.
English descriptors
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Abstract
Abstract.: Human prion diseases are characterized by the accumulation in the brain of proteinase K (PK)-resistant prion protein designated PrP27-30 detectable by the 3F4 antibody against human PrP109-112. We recently identified a new PK-resistant PrP species, designated PrP*20, in uninfected human and animal brains. It was preferentially detected with the 1E4 antibody against human PrP 97-108 but not with the anti-PrP 3F4 antibody, although the 3F4 epitope is adjacent to the 1E4 epitope in the PrP*20 molecule. The present study reveals that removal of the N-terminal amino acids up to residue 91 significantly increases accessibility of the 1E4 antibody to PrP of brains and cultured cells. In contrast to cells expressing wild-type PrP, cells expressing pathogenic mutant PrP accumulate not only PrP*20 but also a small amount of 3F4-detected PK-resistant PrP27-30. Remarkably, during the course of human prion disease, a transition from an increase in 1E4-detected PrP*20 to the occurrence of the 3F4-detected PrP27-30 was observed. Our study suggests that an increase in the level of PrP*20 characterizes the early stages of prion diseases.
Url:
DOI: 10.1007/s00018-007-7478-z
Affiliations:
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Xiao</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and National Prion Disease Pathology Surveillance Center, Case Western Reserve University, 2085 Adelbert Road, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Wang, J" sort="Wang, J" uniqKey="Wang J" first="J." last="Wang">J. Wang</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and National Prion Disease Pathology Surveillance Center, Case Western Reserve University, 2085 Adelbert Road, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Cali, I" sort="Cali, I" uniqKey="Cali I" first="I." last="Cali">I. 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Cashman</name><affiliation wicri:level="1"><country xml:lang="fr">Canada</country><wicri:regionArea>Brain Research Centre, University of British Columbia Hospital, 2211 Wesbrook Mall, V6T 2B5, Vancouver, BC</wicri:regionArea><wicri:noRegion>BC</wicri:noRegion></affiliation></author><author><name sortKey="Bessen, R" sort="Bessen, R" uniqKey="Bessen R" first="R." last="Bessen">R. Bessen</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Veterinary Molecular Biology, Montana State University, P.O. Box 173610, 59717, Bozeman, Montana</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author><author><name sortKey="Surewicz, W K" sort="Surewicz, W K" uniqKey="Surewicz W" first="W. K." last="Surewicz">W. K. Surewicz</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Physiology and Biophysics, Case Western Reserve University, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Kneale, G" sort="Kneale, G" uniqKey="Kneale G" first="G." last="Kneale">G. Kneale</name><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, University of Portsmouth, PO1 2DT, Portsmouth</wicri:regionArea><wicri:noRegion>Portsmouth</wicri:noRegion></affiliation></author><author><name sortKey="Petersen, R B" sort="Petersen, R B" uniqKey="Petersen R" first="R. B." last="Petersen">R. B. Petersen</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and National Prion Disease Pathology Surveillance Center, Case Western Reserve University, 2085 Adelbert Road, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Neuroscience, Case Western Reserve University, 2085 Adelbert Road, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Gambetti, P" sort="Gambetti, P" uniqKey="Gambetti P" first="P." last="Gambetti">P. Gambetti</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and National Prion Disease Pathology Surveillance Center, Case Western Reserve University, 2085 Adelbert Road, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Zou, W Q" sort="Zou, W Q" uniqKey="Zou W" first="W. Q." last="Zou">W. Q. Zou</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pathology and National Prion Disease Pathology Surveillance Center, Case Western Reserve University, 2085 Adelbert Road, 44106, Cleveland, Ohio</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation></author></analytic><monogr></monogr><series><title level="j">Cellular and Molecular Life Sciences</title><title level="j" type="abbrev">Cell. Mol. Life Sci.</title><idno type="ISSN">1420-682X</idno><idno type="eISSN">1420-9071</idno><imprint><publisher>Birkhäuser-Verlag</publisher><pubPlace>Basel</pubPlace><date type="published" when="2008-02-01">2008-02-01</date><biblScope unit="volume">65</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="631">631</biblScope><biblScope unit="page" to="643">643</biblScope></imprint><idno type="ISSN">1420-682X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1420-682X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Creutzfeldt-Jakob disease</term><term>Prion protein</term><term>epitope</term><term>gene 5 protein</term><term>neuroblastoma cell</term><term>prion disease</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract.: Human prion diseases are characterized by the accumulation in the brain of proteinase K (PK)-resistant prion protein designated PrP27-30 detectable by the 3F4 antibody against human PrP109-112. We recently identified a new PK-resistant PrP species, designated PrP*20, in uninfected human and animal brains. It was preferentially detected with the 1E4 antibody against human PrP 97-108 but not with the anti-PrP 3F4 antibody, although the 3F4 epitope is adjacent to the 1E4 epitope in the PrP*20 molecule. The present study reveals that removal of the N-terminal amino acids up to residue 91 significantly increases accessibility of the 1E4 antibody to PrP of brains and cultured cells. In contrast to cells expressing wild-type PrP, cells expressing pathogenic mutant PrP accumulate not only PrP*20 but also a small amount of 3F4-detected PK-resistant PrP27-30. Remarkably, during the course of human prion disease, a transition from an increase in 1E4-detected PrP*20 to the occurrence of the 3F4-detected PrP27-30 was observed. Our study suggests that an increase in the level of PrP*20 characterizes the early stages of prion diseases.</div></front></TEI><affiliations><list><country><li>Canada</li><li>Royaume-Uni</li><li>États-Unis</li></country><region><li>Montana</li><li>Ohio</li></region></list><tree><country name="États-Unis"><region name="Ohio"><name sortKey="Yuan, J" sort="Yuan, J" uniqKey="Yuan J" first="J." last="Yuan">J. Yuan</name></region><name sortKey="Bessen, R" sort="Bessen, R" uniqKey="Bessen R" first="R." last="Bessen">R. Bessen</name><name sortKey="Cali, I" sort="Cali, I" uniqKey="Cali I" first="I." last="Cali">I. Cali</name><name sortKey="Dong, Z" sort="Dong, Z" uniqKey="Dong Z" first="Z." last="Dong">Z. Dong</name><name sortKey="Gambetti, P" sort="Gambetti, P" uniqKey="Gambetti P" first="P." last="Gambetti">P. Gambetti</name><name sortKey="Petersen, R B" sort="Petersen, R B" uniqKey="Petersen R" first="R. B." last="Petersen">R. B. Petersen</name><name sortKey="Petersen, R B" sort="Petersen, R B" uniqKey="Petersen R" first="R. B." last="Petersen">R. B. Petersen</name><name sortKey="Surewicz, W K" sort="Surewicz, W K" uniqKey="Surewicz W" first="W. K." last="Surewicz">W. K. Surewicz</name><name sortKey="Wang, J" sort="Wang, J" uniqKey="Wang J" first="J." last="Wang">J. Wang</name><name sortKey="Xiao, X" sort="Xiao, X" uniqKey="Xiao X" first="X." last="Xiao">X. Xiao</name><name sortKey="Zou, W Q" sort="Zou, W Q" uniqKey="Zou W" first="W. Q." last="Zou">W. Q. Zou</name><name sortKey="Zou, W Q" sort="Zou, W Q" uniqKey="Zou W" first="W. Q." last="Zou">W. Q. Zou</name></country><country name="Canada"><noRegion><name sortKey="Guo, J P" sort="Guo, J P" uniqKey="Guo J" first="J.-P." last="Guo">J.-P. Guo</name></noRegion><name sortKey="Cashman, N R" sort="Cashman, N R" uniqKey="Cashman N" first="N. R." last="Cashman">N. R. Cashman</name><name sortKey="Mcgeer, P L" sort="Mcgeer, P L" uniqKey="Mcgeer P" first="P. L." last="Mcgeer">P. L. Mcgeer</name></country><country name="Royaume-Uni"><noRegion><name sortKey="Mcgeehan, J" sort="Mcgeehan, J" uniqKey="Mcgeehan J" first="J." last="Mcgeehan">J. Mcgeehan</name></noRegion><name sortKey="Kneale, G" sort="Kneale, G" uniqKey="Kneale G" first="G." last="Kneale">G. Kneale</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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