Validation of a luminescence immunoassay for the detection of PrPSc in brain homogenate

Biffiger, Karin; Zwald, Daniel; Kaufmann, L; Briner, Alexandra; Nayki, Inci; Pürro, Mario; Böttcher, Sigrid; Struckmeyer, Thomas; Schaller, Olivier; Meyer, R.; Fatzer, R; Zurbriggen, A.; Stack, M.J.; Moser, Markus; Oesch, Bruno; Kübler, Eric

doi:10.1016/s0166-0934(01)00421-9

Cited by 41 publications

(23 citation statements)

References 5 publications

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“…This can be achieved by denaturation, especially when preceded by a partial proteolytic digest of the protein, as is commonly done in prion diagnostics. 21,20 The C1 antibody may prove to be an excellent tool to meet the increased demand of highly sensitive diagnostic BSE tests for the detection of small amounts of PrP Sc present in brain tissue or other peripheral tissues. Furthermore, it is a generally useful model system to study the extremely tight binding of peptides.…”

Section: Introductionmentioning

confidence: 99%

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural Interpretation

Luginbühl

Kanyo

Jones³

et al. 2006

Journal of Molecular Biology

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Section: Introductionmentioning

confidence: 99%

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural Interpretation

Luginbühl

Kanyo

Jones³

et al. 2006

Journal of Molecular Biology

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“…The whole unfixed transverse sections from cervical spinal cord, medulla oblongata, thalamus, and basal ganglia areas were homogenized with triangle tissue sections of approximately 0.5 g, containing mainly gray matter, obtained from the cerebellar and cerebral cortical areas. LIA a, 3 and Western blot b,10 tests were performed according to the manufacturer's instructions. The IHC was performed as described previously, 7 using the monoclonal antibody 6H4 c as the primary antibody.…”

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confidence: 99%

Comparison of Immunohistochemistry and Two Rapid Tests for Detection of Abnormal Prion Protein in Different Brain Regions of Sheep with Typical Scrapie

Bolea

Monleón

Schiller³

et al. 2005

J VET Diagn Invest

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Abstract.One of the ''gold standard'' techniques for postmortem confirmation of scrapie diagnosis in sheep and goats is immunohistochemical examination of brain tissue. Active surveillance for scrapie is mainly performed by rapid diagnostic tests on the basis of postmortem immunochemical detection of prion protein (PrP) in the obex tissue. The aim of this study was to determine the performance of 2 rapid tests, Prionics-Check LIA (a chemiluminescence sandwich enzyme-linked immunosorbent assay) and Prionics-Check Western blot for scrapie diagnosis when applied to brain areas other than the obex, in comparison with the recognized immunohistochemistry. Prion protein was detected in the obex, cervical spinal cord, and thalamus from all the scrapie-positive sheep by the 3 tests. Western blot and LIA were negative in other areas of the brain, although weak immunohistochemical staining was detected. The results show that the 2 rapid tests studied may detect PrP in brain areas other than the obex, although with a lower sensitivity than immunohistochemistry when there is minimal PrP deposition.

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“…Higher-throughput tests developed for bovine spongiform encephalopathy have been described. 1,2,7 These assays are based on the detection of the disease-associated isoform of PrP in detergent lysates of the brain, the tissue with the highest accumulation of the abnormal protein. in lymphoid tissues from infected animals.…”

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confidence: 99%

Abundant PrP^CWD in Tonsil from Mule Deer with Preclinical Chronic Wasting Disease

et al. 2003

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Abstract.A monoclonal antibody dot-blot assay was used to evaluate detergent lysates of tonsil tissue from mule deer to detect PrP CWD , the marker for the cervid transmissible spongiform encephalopathy chronic wasting disease (CWD). Samples of formalin-fixed brain and tonsil tissues from mule deer were examined for PrP CWD using immunohistochemistry (IHC) with Mab F99/97.6.1, the gold standard for diagnosis of preclinical CWD. The contralateral tonsil from each of the 143 deer was prepared for confirmatory IHC and as a 10% (wt/vol) detergent lysate without purification or enrichment steps for monoclonal antibody dot-blot assay. PrP CWD was detected by dot-blot assay in 49 of 50 samples considered positive by IHC. Forty-eight of the positive samples were evaluated with a quantitative dot-blot assay calibrated with recombinant PrP. Tonsillar PrP CWD concentrations ranged from 34 to 1,188 ng per 0.5 mg starting wet weight of tissue. The abundant PrP CWD in mule deer tonsil will facilitate development and validation of high-throughput screening tests for CWD in large populations of free-ranging deer.

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Validation of a luminescence immunoassay for the detection of PrPSc in brain homogenate

Cited by 41 publications

References 5 publications

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural Interpretation

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural Interpretation

Comparison of Immunohistochemistry and Two Rapid Tests for Detection of Abnormal Prion Protein in Different Brain Regions of Sheep with Typical Scrapie

Abundant PrP^CWD in Tonsil from Mule Deer with Preclinical Chronic Wasting Disease

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Validation of a luminescence immunoassay for the detection of PrPSc in brain homogenate

Cited by 41 publications

References 5 publications

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural Interpretation

Directed Evolution of an Anti-prion Protein scFv Fragment to an Affinity of 1 pM and its Structural Interpretation

Comparison of Immunohistochemistry and Two Rapid Tests for Detection of Abnormal Prion Protein in Different Brain Regions of Sheep with Typical Scrapie

Abundant PrPCWD in Tonsil from Mule Deer with Preclinical Chronic Wasting Disease

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Abundant PrP^CWD in Tonsil from Mule Deer with Preclinical Chronic Wasting Disease