Tubulovesicular structures are not labeled using antibodies to prion protein (PrP) with the immunogold electron microscopy techniques |
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Authors: | P P Liberski M Jeffrey C Goodsir |
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Institution: | (1) Laboratory of Electron Microscopy and Neuropathology, Laboratories of Tumor Biology, Chair of Oncology, Medical Academy Lodz, Paderewski Street 4, PL-93 509 Lodz, Poland Tel.: 48-42-81-11-17; Fax: 48-42-32-23-47, PL;(2) Central Veterinary Laboratory, Lasswade Veterinary Laboratory, Bush Estate, Penicuik, Edinburgh, Scotland, GB |
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Abstract: | Tubulovesicular structures (TVS) are disease-specific, intraneuronal particles found by thin-section electron microscopy
in all of the transmissible spongiform encephalopathies. We used immunogold (both 10 nm immunogold and 1 nm immunogold silver
enhanced) methods for ultrastructural localization of prion protein (PrP). In all scrapie models examined (263 K and 22CH
in hamsters and 87V and ME7 in mice), TVS-containing processes were readily detected but neither these processes nor TVS themselves
were decorated with gold particles. Even when amyloid plaques were observed in a close contact with TVS-containing neuronal
processes, the processes remained unstained, while the plaques were decorated with gold particles. TVS located in areas adjacent
to plaques in the 87V model and in areas of diffuse PrP immunolabelling in ME7 were also unlabelled with anti-PrP sera. Using
immunogold techniques we were unable to label TVS with anti-PrP antibodies. As these technique proved to be sensitive enough
to immunolabel not only amyloid plaques but also pre-amyloid accumulations of PrP, we strongly believe that the absence of
staining reflects the structure of TVS and that they are not composed of PrP. That TVS are PrP negative may have several important
implications for hypotheses about their nature. Principally, it does not support the suggestion that TVS are cross-sections
of “thick tubules” visualized by touch-preparations of scrapie-affected mouse and hamster brains. If PrP is the infectious
agent, as suggested by the prion hypothesis, the absence of stainable PrP in TVS would indicate that these are not the ultrastructural
correlate of the agent. If, however, TVS turn out to be more than merely a useful ultrastructural marker for the whole group
of transmissible spongiform encephalopathies, it may suggest that PrP and the agent are two separate entities.
Received: 11 March 1996 / Revised: 9 May 1996 / Accepted: 26 September 1996 |
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Keywords: | Tubulovesicular structures Prion protein Transmissible spongiform encephalopathy Immunogold electron microscopy |
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