The prion protein is a cell surface glycoprotein whose physiological role remains elusive, while its implication in transmissible spongiform encephalopathies (TSEs) has been demonstrated. Multiple interactions between the prion protein and viruses have been described: viruses can act as co-factors in TSEs and life cycles of different viruses have been found to be controlled by prion modulation. We present data showing that human Adenovirus 5 induces prion expression. Inactivated Adenovirus did not alter prion transcription, while variants encoding for early products did, suggesting that the prion is stimulated by an early adenoviral function. Down-regulation of the prion through RNA interference showed that the prion controls adenovirus replication and expression. These data suggest that the prion protein could play a role in the defense strategy mounted by the host during viral infection, in a cell autonomous manner. These results have implications for the study of the prion protein and of associated TSEs.

Prion expression is activated by Adenovirus 5 infection and affects the adenoviral cycle in human cells / Caruso, P; Burla, R.; Piersanti, S; Cherubini, G; Remoli, C; Martina, Y; Saggio, I. - In: VIROLOGY. - ISSN 0042-6822. - STAMPA. - 385:2(2009), pp. 343-350. [10.1016/j.virol.2008.12.005]

Prion expression is activated by Adenovirus 5 infection and affects the adenoviral cycle in human cells

R. BURLA;PIERSANTI S;REMOLI C;MARTINA Y;SAGGIO I
2009

Abstract

The prion protein is a cell surface glycoprotein whose physiological role remains elusive, while its implication in transmissible spongiform encephalopathies (TSEs) has been demonstrated. Multiple interactions between the prion protein and viruses have been described: viruses can act as co-factors in TSEs and life cycles of different viruses have been found to be controlled by prion modulation. We present data showing that human Adenovirus 5 induces prion expression. Inactivated Adenovirus did not alter prion transcription, while variants encoding for early products did, suggesting that the prion is stimulated by an early adenoviral function. Down-regulation of the prion through RNA interference showed that the prion controls adenovirus replication and expression. These data suggest that the prion protein could play a role in the defense strategy mounted by the host during viral infection, in a cell autonomous manner. These results have implications for the study of the prion protein and of associated TSEs.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11573/344879
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