Related Experiment Video
Updated: Aug 24, 2026

Assessing Transmissible Spongiform Encephalopathy Species Barriers with an In Vitro Prion Protein Conversion Assay
Published on: March 10, 2015
Compartmentalization of prion isoforms within the reproductive tract of the ram
Heath Ecroyd1, Pierre Sarradin, Jean-Louis Dacheux
1Gamètes Males et Fertilité, UMR 6175 INRA-CNRS-Université de Tours-Haras Nationaux, Station de Physiologie de la Reproduction et des Comportements, 37380 Nouzilly, France.
Abstract:
Cellular prion protein (Prp(C)) is a glycoprotein usually associated with membranes via its glycosylphosphatidylinositol (GPI) anchor. The trans-conformational form of this protein (Prp(SC)) is the suggested agent responsible for transmissible neurodegenerative spongiform encephalopathies. This protein has been shown on sperm and in the reproductive fluids of males. Antibodies directed against the C-terminal sequence near the GPI-anchor site, an N-terminal sequence, and against the whole protein showed that the Prp isoforms were compartmentalized within the reproductive tract of the ram. Immunoblotting with the three antibodies showed that the complete protein and both N- and C-terminally truncated and glycosylated isoforms are present within cauda epididymal fluid and seminal plasma. Moreover, we demonstrate that in these fluids, the Prp(C) isoforms are both in a soluble state as well as associated with small membranous vesicles (epididymosomes). We also report that only one major glycosylated 25 kDa C-terminally truncated Prp(C) isoform is associated with sperm from the testis, cauda epididymis, and semen, and this form is also present in the sperm cytoplasmic droplets that are released during maturation. In sperm, this C-terminal truncated form was found to be associated with membrane lipid rafts present in the mature sperm, suggesting a role for it in the terminal stages of sperm maturation.
Insights
Cellular prion protein (Prp(C)) is found in male reproductive fluids and on sperm. A specific truncated form associates with sperm during maturation, potentially playing a role in sperm development.
Area of Science:
- Reproductive Biology
- Neuroscience
- Biochemistry
Background:
- Cellular prion protein (Prp(C)) is a membrane-associated glycoprotein.
- Its pathogenic form (Prp(SC)) causes transmissible neurodegenerative spongiform encephalopathies.
- Prp(C) has been detected in male reproductive systems.
Purpose of the Study:
- To investigate the presence and localization of Prp(C) isoforms within the ram reproductive tract.
- To determine the association of Prp(C) with sperm during maturation.
- To explore the potential role of Prp(C) in sperm function.
Main Methods:
- Immunoblotting using antibodies against different Prp(C) sequences.
- Analysis of cauda epididymal fluid, seminal plasma, and sperm from different reproductive tract sections.
- Investigation of Prp(C) association with sperm cytoplasmic droplets and lipid rafts.
Main Results:
- Prp(C) isoforms, including full-length and truncated forms, are present in ram cauda epididymal fluid and seminal plasma.
- These isoforms exist in both soluble and vesicle-associated forms (epididymosomes).
- A specific 25 kDa C-terminally truncated Prp(C) isoform is consistently found on sperm from testis to semen, and in cytoplasmic droplets.
Conclusions:
- Prp(C) isoforms are compartmentalized within the male reproductive tract.
- A specific truncated Prp(C) isoform is associated with sperm throughout maturation.
- This association with sperm lipid rafts suggests a role in terminal sperm maturation stages.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Eukaryotic Compartmentalizations
For example, lysosomes in the animal cells...
Subviral Agents
Leaky Scanning

