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Human FDC express PrPc in vivo and in vitro
C Thielen1, N Antoine, F Mélot
1Institute of Human Histology, University of Liège, Belgium. Caroline.Thielen@ulg.ac.be
Abstract:
Prion diseases are fatal neurodegenerative disorders caused by accumulation of abnormal prion protein (protease-resistant prion, PrPres). PrPres accumulation is also detected in lymphoid organs after peripheral infection. Several studies suggest that follicular dendritic cells (FDC) could be the site of PrPres retention and amplification. Here we show that human follicular dendritic cells can express normal cellular prion protein (PrPc) both in situ and in vitro. When tonsillar cryosections were treated with anti-PrP antibody, the label was found on some very delicate cell extensions inside the lymphoid follicles, especially in the germinal centres. These extensions react with DRC1 antibody, used frequently to label FDC. Other structures labelled with anti-PrP antibody were the keratinocytes. To confirm the ability of FDC to synthesise PrPc, we isolated FDC by a non-enzymatic procedure and cultured them. By cytochemistry and flow cytometry it was clearly shown that FDC do produce PrPc.
Insights
Human follicular dendritic cells (FDC) express normal prion protein (PrPc), potentially explaining prion retention in lymphoid organs. This finding offers new insights into prion disease pathogenesis and spread.
Area of Science:
- Neuroscience
- Immunology
- Cell Biology
Background:
- Prion diseases are fatal neurodegenerative disorders.
- Abnormal prion protein (PrPres) accumulation occurs in lymphoid organs after peripheral infection.
- Follicular dendritic cells (FDC) are implicated in PrPres retention and amplification.
Purpose of the Study:
- To investigate whether human follicular dendritic cells (FDC) express the normal cellular prion protein (PrPc).
- To determine if FDC can synthesize PrPc in vitro.
Main Methods:
- Immunohistochemical staining of tonsillar cryosections with anti-PrP and DRC1 antibodies.
- Isolation and in vitro culture of human FDC using a non-enzymatic procedure.
- Cytochemistry and flow cytometry analysis of cultured FDC for PrPc expression.
Main Results:
- Anti-PrP antibody labeling was observed on cell extensions within lymphoid follicles, co-localizing with FDC markers (DRC1).
- Human FDC, both in situ and in vitro, were shown to express PrPc.
- Keratinocytes also showed anti-PrP antibody labeling.
Conclusions:
- Human FDC express and likely synthesize normal cellular prion protein (PrPc).
- This expression suggests FDC play a role in the initial retention and amplification of prions in lymphoid tissues.
- Findings contribute to understanding prion disease pathogenesis and potential transmission routes.
