Prion protein resides in membrane microclusters of the immunological synapse during lymphocyte activation.

Expression of prion protein (PrP) has been reported for a variety of cell types including neuronal cells, haematopoietic stem cells, antigen-presenting cells, as well as lymphocytes. However, besides this widespread occurrence little is known about the physiological roles exhibited by this enigmatic protein. In this study, the contribution of PrP to the classical T-lymphocyte activation process was characterized by clustering the T-cell receptor component CD3epsilon as well as PrP with soluble and surface-immobilized antibodies, respectively.

The physiological functions of prion protein.

Prion proteins are mentioned predominantly as unprecedented infectious pathogens in the context of transmissible spongiform encephalopathies. Since prions are devoid of nucleic acids, disease transmission must be mediated by an entirely novel mechanism. The general accepted theory proposes the conversion of cellular prion protein (PrP(C)) into the pathological isoform solely through conformational changes.