What question did this study set out to answer?

To directly track the generation and pathological behavior of conformation-specific beta-sheet-rich prion protein in scrapie-infected cells using a novel human antibody.

February 23, 2012Journal of Biological ChemistryOpen Access

Direct Evidence of Generation and Accumulation of β-Sheet-rich Prion Protein in Scrapie-infected Neuroblastoma Cells with Human IgG1 Antibody Specific for β-Form Prion Protein

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Authors

TKToshiya Kubota YHYuta Hamazoe SHShuhei Hashiguchi

Discussion

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Overview

In vitro study demonstrates accumulation of toxic beta-sheet prion aggregates in infected neuroblastoma cells, indicating that end-stage aggregates drive apoptosis rather than prion propagation.

Key Points

To directly track the generation and pathological behavior of conformation-specific beta-sheet-rich prion protein in scrapie-infected cells using a novel human antibody.
Generated a human IgG1 antibody (PRB7) specific to beta-form prion protein using recombinant full-length protein and a single-chain Fv phage display library.
Cultured scrapie-infected mouse neuroblastoma (ScN2a) cells with PRB7 IgG or the N-terminal-binding SAF32 antibody, monitoring granule formation by confocal laser microscopy.
Assayed the generation of proteinase K-resistant prion protein and progression to apoptotic cell death.
ScN2a cells cultured with PRB7 IgG formed cytoplasmic granules that condensed into large aggregates over time, culminating in apoptotic cell death.
Confocal imaging showed SAF32 recognized distinct granules separate from PRB7-bound aggregates.
Accumulation of proteinase K-resistant prion protein was strongly suppressed by SAF32 but completely unaffected by PRB7 IgG.

Cite This Study

Kubota et al. (2012) studied this question.

synapsesocial.com/papers/6a77f781576efb0ddaf7c7ef https://doi.org/10.1074/jbc.m111.318352

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February 23, 2012Journal of Biological ChemistryOpen Access

Direct Evidence of Generation and Accumulation of β-Sheet-rich Prion Protein in Scrapie-infected Neuroblastoma Cells with Human IgG1 Antibody Specific for β-Form Prion Protein

View Full Paper

Ask AI

Bookmark

Authors

TKToshiya Kubota YHYuta Hamazoe SHShuhei Hashiguchi

Discussion

Member takes

Overview

In vitro study demonstrates accumulation of toxic beta-sheet prion aggregates in infected neuroblastoma cells, indicating that end-stage aggregates drive apoptosis rather than prion propagation.

Key Points

To directly track the generation and pathological behavior of conformation-specific beta-sheet-rich prion protein in scrapie-infected cells using a novel human antibody.
Generated a human IgG1 antibody (PRB7) specific to beta-form prion protein using recombinant full-length protein and a single-chain Fv phage display library.
Cultured scrapie-infected mouse neuroblastoma (ScN2a) cells with PRB7 IgG or the N-terminal-binding SAF32 antibody, monitoring granule formation by confocal laser microscopy.
Assayed the generation of proteinase K-resistant prion protein and progression to apoptotic cell death.
ScN2a cells cultured with PRB7 IgG formed cytoplasmic granules that condensed into large aggregates over time, culminating in apoptotic cell death.
Confocal imaging showed SAF32 recognized distinct granules separate from PRB7-bound aggregates.
Accumulation of proteinase K-resistant prion protein was strongly suppressed by SAF32 but completely unaffected by PRB7 IgG.

Cite This Study

Kubota et al. (2012) studied this question.

synapsesocial.com/papers/6a77f781576efb0ddaf7c7ef https://doi.org/10.1074/jbc.m111.318352

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