TAILIEUCHUNG - Báo cáo khoa học: Vaccination with prion peptide-displaying papillomavirus-like particles induces autoantibodies to normal prion protein that interfere with pathologic prion protein production in infected cells

Prion diseases are fatal neurodegenerative disorders caused by proteina-ceous infectious pathogens termed prions (PrP Sc ). To date, there is no pro-phylaxis or therapy available for these transmissible encephalopathies. Passive immunization with monclonal antibodies recognizing the normal host-encoded prion protein (PrP C ) has been reported to abolish PrP Sc infec-tivity and to delay onset of disease. | ỊFEBS Journal Vaccination with prion peptide-displaying papillomavirus-like particles induces autoantibodies to normal prion protein that interfere with pathologic prion protein production in infected cells Ạ I occ a n H f a I I a nH IQ 11 r a 1 a Ki no r ilnK2 rinrian A in or3 4 Qannrl Qhaíti-I oramat1 rìĩo or l lai iroi 3 4 - l cooal KJia n al Ivllouiya uauillc xJIICII LsOllal I V V II ntei uaeeu ul laitlixeiai Hal Lzl clcl IVI auicl Hermann M. Schatzl2 and Reinhard Kirnbauer1 1 Laboratory of ViralOncology DIAID Department of Dermatology MedicalUniversity Vienna Austria 2 Institute of Virology TechnicalUniversity of Munich Germany 3 Laboratory of Experimentaland ClinicalImmunology DIAID Department of Dermatology MedicalUniversity Vienna Austria 4 Center of Molecular Medicine Austrian Academy of Sciences Vienna Austria Keywords immunotherapy papillomavirus-like particles prion Correspondence R. Kirnbauer Laboratory of ViralOncology DIAID Department of Dermatology Medical University Vienna Wahringer Gurtel 18 20 A-1090 Vienna Austria Fax 43 1 4030224 Tel 43 1 40400-7768 E-mail Received 29 September 2006 revised 21 December 2006 accepted 31 January 2007 doi Prion diseases are fatal neurodegenerative disorders caused by proteinaceous infectious pathogens termed prions PrPSc . To date there is no prophylaxis or therapy available for these transmissible encephalopathies. Passive immunization with monclonal antibodies recognizing the normal host-encoded prion protein PrPC has been reported to abolish PrPSc infectivity and to delay onset of disease. Because of established immunologic tolerance against the widely expressed PrPC active immunization appears to be difficult to achieve. To overcome this limitation papillomavirus-like particles were generated that display a nine amino acid B-cell epitope DWEDRYYRE of the murine rat prion protein in an immunogenic capsid surface loop by insertion into the L1 .

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