Search

Your search keyword '"Nonno, Romolo"' showing total 13 results
Start Over Author "Nonno, Romolo" Journal plos pathogens
13 results on '"Nonno, Romolo"'

1. A single amino acid residue in bank vole prion protein drives permissiveness to Nor98/atypical scrapie and the emergence of multiple strain variants

Author

Pirisinu, Laura, primary, Di Bari, Michele Angelo, additional, D’Agostino, Claudia, additional, Vanni, Ilaria, additional, Riccardi, Geraldina, additional, Marcon, Stefano, additional, Vaccari, Gabriele, additional, Chiappini, Barbara, additional, Benestad, Sylvie L., additional, Agrimi, Umberto, additional, and Nonno, Romolo, additional

Published
2022
Full Text
View/download PDF

2. Adaptive selection of a prion strain conformer corresponding to established North American CWD during propagation of novel emergent Norwegian strains in mice expressing elk or deer prion protein

Author

Bian, Jifeng, primary, Kim, Sehun, additional, Kane, Sarah J., additional, Crowell, Jenna, additional, Sun, Julianna L., additional, Christiansen, Jeffrey, additional, Saijo, Eri, additional, Moreno, Julie A., additional, DiLisio, James, additional, Burnett, Emily, additional, Pritzkow, Sandra, additional, Gorski, Damian, additional, Soto, Claudio, additional, Kreeger, Terry J., additional, Balachandran, Aru, additional, Mitchell, Gordon, additional, Miller, Michael W., additional, Nonno, Romolo, additional, Vikøren, Turid, additional, Våge, Jørn, additional, Madslien, Knut, additional, Tran, Linh, additional, Vuong, Tram Thu, additional, Benestad, Sylvie L., additional, and Telling, Glenn C., additional

Published
2021
Full Text
View/download PDF

3. Development of a new largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies

Author

Eraña, Hasier, primary, Charco, Jorge M., additional, Di Bari, Michele A., additional, Díaz-Domínguez, Carlos M., additional, López-Moreno, Rafael, additional, Vidal, Enric, additional, González-Miranda, Ezequiel, additional, Pérez-Castro, Miguel A., additional, García-Martínez, Sandra, additional, Bravo, Susana, additional, Fernández-Borges, Natalia, additional, Geijo, Mariví, additional, D’Agostino, Claudia, additional, Garrido, Joseba, additional, Bian, Jifeng, additional, König, Anna, additional, Uluca-Yazgi, Boran, additional, Sabate, Raimon, additional, Khaychuk, Vadim, additional, Vanni, Ilaria, additional, Telling, Glenn C., additional, Heise, Henrike, additional, Nonno, Romolo, additional, Requena, Jesús R., additional, and Castilla, Joaquín, additional

Published
2019
Full Text
View/download PDF

4. Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis

Author

Sevillano, Alejandro M., primary, Fernández-Borges, Natalia, additional, Younas, Neelam, additional, Wang, Fei, additional, R. Elezgarai, Saioa, additional, Bravo, Susana, additional, Vázquez-Fernández, Ester, additional, Rosa, Isaac, additional, Eraña, Hasier, additional, Gil, David, additional, Veiga, Sonia, additional, Vidal, Enric, additional, Erickson-Beltran, Melissa L., additional, Guitián, Esteban, additional, Silva, Christopher J., additional, Nonno, Romolo, additional, Ma, Jiyan, additional, Castilla, Joaquín, additional, and R. Requena, Jesús, additional

Published
2018
Full Text
View/download PDF

5. Isolation of a Defective Prion Mutant from Natural Scrapie

Author

Vanni, Ilaria, primary, Migliore, Sergio, additional, Cosseddu, Gian Mario, additional, Di Bari, Michele Angelo, additional, Pirisinu, Laura, additional, D’Agostino, Claudia, additional, Riccardi, Geraldina, additional, Agrimi, Umberto, additional, and Nonno, Romolo, additional

Published
2016
Full Text
View/download PDF

6. Recombinant PrPSc shares structural features with brain-derived PrPSc: Insights from limited proteolysis.

Author

Sevillano, Alejandro M., Fernández-Borges, Natalia, Younas, Neelam, Wang, Fei, R. Elezgarai, Saioa, Bravo, Susana, Vázquez-Fernández, Ester, Rosa, Isaac, Eraña, Hasier, Gil, David, Veiga, Sonia, Vidal, Enric, Erickson-Beltran, Melissa L., Guitián, Esteban, Silva, Christopher J., Nonno, Romolo, Ma, Jiyan, Castilla, Joaquín, and R. Requena, Jesús

Subjects
PROTEOLYSIS, MOLECULAR structure of amyloids, PRIONS, EPITOPES, MASS spectrometry
Abstract

Very solid evidence suggests that the core of full length PrPSc is a 4-rung β-solenoid, and that individual PrPSc subunits stack to form amyloid fibers. We recently used limited proteolysis to map the β-strands and connecting loops that make up the PrPSc solenoid. Using high resolution SDS-PAGE followed by epitope analysis, and mass spectrometry, we identified positions ~116/118, 133–134, 141, 152–153, 162, 169 and 179 (murine numbering) as Proteinase K (PK) cleavage sites in PrPSc. Such sites likely define loops and/or borders of β-strands, helping us to predict the threading of the β-solenoid. We have now extended this approach to recombinant PrPSc (recPrPSc). The term recPrPSc refers to bona fide recombinant prions prepared by PMCA, exhibiting infectivity with attack rates of ~100%. Limited proteolysis of mouse and bank vole recPrPSc species yielded N-terminally truncated PK-resistant fragments similar to those seen in brain-derived PrPSc, albeit with varying relative yields. Along with these fragments, doubly N- and C-terminally truncated fragments, in particular ~89/97-152, were detected in some recPrPSc preparations; similar fragments are characteristic of atypical strains of brain-derived PrPSc. Our results suggest a shared architecture of recPrPSc and brain PrPSc prions. The observed differences, in particular the distinct yields of specific PK-resistant fragments, are likely due to differences in threading which result in the specific biochemical characteristics of recPrPSc. Furthermore, recombinant PrPSc offers exciting opportunities for structural studies unachievable with brain-derived PrPSc. [ABSTRACT FROM AUTHOR]

Published
2018
Full Text
View/download PDF

9. Chronic Wasting Disease in Bank Voles: Characterisation of the Shortest Incubation Time Model for Prion Diseases

Author

Di Bari, Michele Angelo, primary, Nonno, Romolo, additional, Castilla, Joaquín, additional, D'Agostino, Claudia, additional, Pirisinu, Laura, additional, Riccardi, Geraldina, additional, Conte, Michela, additional, Richt, Juergen, additional, Kunkle, Robert, additional, Langeveld, Jan, additional, Vaccari, Gabriele, additional, and Agrimi, Umberto, additional

Published
2013
Full Text
View/download PDF

11. Prion Protein Amino Acid Determinants of Differential Susceptibility and Molecular Feature of Prion Strains in Mice and Voles

Author

Agrimi, Umberto, primary, Nonno, Romolo, additional, Dell'Omo, Giacomo, additional, Di Bari, Michele Angelo, additional, Conte, Michela, additional, Chiappini, Barbara, additional, Esposito, Elena, additional, Di Guardo, Giovanni, additional, Windl, Otto, additional, Vaccari, Gabriele, additional, and Lipp, Hans-Peter, additional

Published
2008
Full Text
View/download PDF

12. Efficient Transmission and Characterization of Creutzfeldt–Jakob Disease Strains in Bank Voles

Author

Nonno, Romolo, primary, Bari, Michele A. Di, additional, Cardone, Franco, additional, Vaccari, Gabriele, additional, Fazzi, Paola, additional, Dell'Omo, Giacomo, additional, Cartoni, Claudia, additional, Ingrosso, Loredana, additional, Boyle, Aileen, additional, Galeno, Roberta, additional, Sbriccoli, Marco, additional, Lipp, Hans-Peter, additional, Bruce, Moira, additional, Pocchiari, Maurizio, additional, and Agrimi, Umberto, additional

Published
2006
Full Text
View/download PDF

13. Ultra-Efficient PrPSc Amplification Highlights Potentialities and Pitfalls of PMCA Technology.

Author

Cosseddu, Gian Mario, Nonno, Romolo, Vaccari, Gabriele, Bucalossi, Cecilia, Fernandez-Borges, Natalia, Di Bari, Michele Angelo, Castilla, Joaquin, and Agrimi, Umberto

Subjects
*PRIONS, *PROTEIN folding, *CHRONIC wasting disease, *GENE amplification, *VOLES, *REPRODUCTION
Abstract

In order to investigate the potential of voles to reproduce in vitro the efficiency of prion replication previously observed in vivo, we seeded protein misfolding cyclic amplification (PMCA) reactions with either rodent-adapted Transmissible Spongiform Encephalopathy (TSE) strains or natural TSE isolates. Vole brain homogenates were shown to be a powerful substrate for both homologous or heterologous PMCA, sustaining the efficient amplification of prions from all the prion sources tested. However, after a few serial automated PMCA (saPMCA) rounds, we also observed the appearance of PK- resistant PrPSc in samples containing exclusively unseeded substrate (negative controls), suggesting the possible spontaneous generation of infectious prions during PMCA reactions. As we could not definitively rule out cross-contamination through a posteriori biochemical and biological analyses of de novo generated prions, we decided to replicate the experiments in a different laboratory. Under rigorous prion-free conditions, we did not observe de novo appearance of PrPSc in unseeded samples of M109M and I109I vole substrates, even after many consecutive rounds of saPMCA and working in different PMCA settings. Furthermore, when positive and negative samples were processed together, the appearance of spurious PrPSc in unseeded negative controls suggested that the most likely explanation for the appearance of de novo PrPSc was the occurrence of cross-contamination during saPMCA. Careful analysis of the PMCA process allowed us to identify critical points which are potentially responsible for contamination events. Appropriate technical improvements made it possible to overcome PMCA pitfalls, allowing PrPSc to be reliably amplified up to extremely low dilutions of infected brain homogenate without any false positive results even after many consecutive rounds. Our findings underline the potential drawback of ultrasensitive in vitro prion replication and warn on cautious interpretation when assessing the spontaneous appearance of prions in vitro. [ABSTRACT FROM AUTHOR]

Published
2011
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results