The @entity375 @entity375 harbors several prions that constitute powerful models to investigate the mechanisms of epigenetic structural inheritance. [ @entity14807 ] is undoubtedly the best-known @entity375 prion and results from the conversion of the translation termination factor @entity16578 into self-perpetuating protein aggregates. Structurally different conformers of @entity16578 aggregates can lead to [PSI(+)] strains with weak or strong prion phenotypes. @entity375 prions are faithfully transmitted from mother to daughter cells during cell division, upon cytoplasmic mixing during mating, or when @entity16578 fibrils made in test tubes are introduced into spheroplasts. Virtually all living cells in the three domains of life, Bacteria, Archaea, and Eukarya, secrete small membrane vesicles in the extracellular space. These extracellular vesicles (EV) have gained increasing interest as vehicles for the intercellular transfer of signaling molecules, nucleic acids, and pathogenic factors, as well as prion-like protein aggregates associated with @entity179 . To begin to explore the question of whether EV could represent a natural mean for @entity375 prion transmission from cell to cell, we purified these extracellular vesicles and assessed whether they contained @entity16578 . Here, we show that @entity16578 is secreted within EV released in the extracellular medium of @entity375 cultures. We demonstrate that @entity16578 within EV isolated from strong and weak [PSI(+)] cells is in an infectious prion conformation. Among the possible implications of our work is the possibility of previously unsuspected EV-mediated horizontal cell-to-cell transfer of fungal prions. IMPORTANCE: Most living cells in the three domains of life, Bacteria, Archaea, and Eukarya, secrete small membrane vesicles in the extracellular space. These extracellular vesicles (EV) were long viewed as "trash cans" by which cells disposed of unwanted macromolecules. EV gained renewed interest as their roles as vehicles for the cell-to-cell transfer of nucleic acids, signaling molecules, and pathogenic factors were recently uncovered. Of particular interest is their proposed role in the prion-like propagation of toxic protein aggregates in @entity179 . @entity375 naturally harbor prion proteins that are excellent models to investigate the mechanisms of formation, propagation, and elimination of self-perpetuating protein aggregates. Here we show for the first time that a @entity375 prion is secreted within EV in its infectious aggregated state. A major implication of our work is the possibility of EV-mediated horizontal spread of fungal prions.

XXXX in Its Soluble and Prion States Is Packaged inside Extracellular Vesicles.

@entity16578 :: ('851752(Tax:4932)', 'Gene') :: ['Sup35p'] @entity375 :: ('4932', 'Species') :: ['Yeasts', 'yeast', 'Saccharomyces cerevisiae', 'Yeast'] @entity179 :: ('MESH:D019636', 'Disease') :: ['neurodegenerative diseases'] @entity14807 :: ('CHEBI:74981', 'Chemical') :: ['PSI(+)']
@entity16578 :: (851752(Tax:4932),Gene) :: ['Sup35p']
