Toward molecular dissection of PrPC-PrPSc interactions.

Toward molecular dissection of PrPC-PrPSc interactions. Research Abstract Details 

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Toward molecular dissection of PrPC-PrPSc interactions. Abstract Text:

Laura Solforosi,Anne Bellon,Monica Schaller,Justin T Cruite,Gil C Abalos,R Anthony Williamson,

Direct interaction between endogenous cellular prion protein (PrP(C)) and misfolded, disease-associated (PrP(Sc)) conformers is a key event in prion propagation, which precedes templated conversion of PrP(C) into nascent PrP(Sc) and prion infectivity. Although almost none of the molecular details of this pivotal process are understood, the persistence of individual prion strains suggests that assembly of the prion replicative complex is mechanistically precise. To systematically map defined regions of PrP(C) sequence that bind tightly to PrP(Sc), we have generated a comprehensive panel of over 45 motif-grafted antibodies containing overlapping peptide grafts collectively spanning PrP residues 19-231. Grafted antibody binding experiments, performed under stringent conditions, clearly identified only three distinct and independent high affinity PrP(Sc) recognition motifs. The first of these binding motifs lies at the very N-terminal region of the mature PrP molecule within PrP-(23-33); the second motif lies within PrP-(98-110); and the third is contained within PrP-(136-158). Mutational analyses of these PrP(Sc)-binding regions revealed that reactivity of the 23-33 and 98-110 segments are largely dependent upon the presence of multiple positively charged amino acid residues. These studies yield new insight into critical peptidic components composing one side of the prion replicative interface.

Toward molecular dissection of PrPC-PrPSc interactions. Publishing Authors By Initials

L Solforosi,A Bellon,M Schaller,JT Cruite,GC Abalos,RA Williamson,

For similar protein interaction mapping research abstracts see: protein interaction mapping research

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Toward molecular dissection of PrPC-PrPSc interactions. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: The Journal of biological chemistry

VOLUME: 282

Page Numbers: 7465-71

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 10

MONTH: 01

YEAR: 2007

Toward molecular dissection of PrPC-PrPSc interactions. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

Toward molecular dissection of PrPC-PrPSc interactions. Keywords Mesh Terms:

KEYWORDS: Protein Interaction Mapping

MESH TERMS: methods

Chemical & Substance for Abstract: Toward molecular dissection of PrPC-PrPSc interactions. Information

Substance Name: PrPSc Proteins

Registry Number: 0

Grant and Affiliation Information for Toward molecular dissection of PrPC-PrPSc interactions.

AFFILIATION: Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.

Country: United States

AGENCY: United States NIA

GRANT: AG004243

ACRONYM: AG

MEDLINETA: J Biol Chem

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