Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc
Prion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrPC). The prion protein is a membrane glycoprotein that consists of two...
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| Format: | Article |
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PeerJ Inc.
2015-03-01
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| Series: | PeerJ |
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| Online Access: | https://peerj.com/articles/811.pdf |
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| author | Alessandro Didonna Anja Colja Venturini Katrina Hartman Tanja Vranac Vladka Čurin Šerbec Giuseppe Legname |
| author_facet | Alessandro Didonna Anja Colja Venturini Katrina Hartman Tanja Vranac Vladka Čurin Šerbec Giuseppe Legname |
| author_sort | Alessandro Didonna |
| collection | DOAJ |
| description | Prion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrPC). The prion protein is a membrane glycoprotein that consists of two domains: a globular, structured C-terminus and an unstructured N-terminus. The N-terminal part of the protein is involved in different functions in both health and disease. In the present work we discuss the production and biochemical characterization of a panel of four monoclonal antibodies (mAbs) against the distal N-terminus of PrPC using a well-established methodology based on the immunization of Prnp0/0 mice. Additionally, we show their ability to block prion (PrPSc) replication at nanomolar concentrations in a cell culture model of prion infection. These mAbs represent a promising tool for prion diagnostics and for studying the physiological role of the N-terminal domain of PrPC. |
| first_indexed | 2024-03-09T06:25:47Z |
| format | Article |
| id | doaj.art-4ff3d64b5efc45999357885f609e61d6 |
| institution | Directory Open Access Journal |
| issn | 2167-8359 |
| language | English |
| last_indexed | 2024-03-09T06:25:47Z |
| publishDate | 2015-03-01 |
| publisher | PeerJ Inc. |
| record_format | Article |
| series | PeerJ |
| spelling | doaj.art-4ff3d64b5efc45999357885f609e61d62023-12-03T11:19:44ZengPeerJ Inc.PeerJ2167-83592015-03-013e81110.7717/peerj.811811Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPcAlessandro Didonna0Anja Colja Venturini1Katrina Hartman2Tanja Vranac3Vladka Čurin Šerbec4Giuseppe Legname5Department of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), Trieste, ItalyDepartment for Production of Diagnostic Reagents and Research, Blood Transfusion Centre of Slovenia, Ljubljana, SloveniaDepartment for Production of Diagnostic Reagents and Research, Blood Transfusion Centre of Slovenia, Ljubljana, SloveniaDepartment for Production of Diagnostic Reagents and Research, Blood Transfusion Centre of Slovenia, Ljubljana, SloveniaDepartment for Production of Diagnostic Reagents and Research, Blood Transfusion Centre of Slovenia, Ljubljana, SloveniaDepartment of Neuroscience, Scuola Internazionale Superiore di Studi Avanzati (SISSA), Trieste, ItalyPrion diseases are a group of fatal neurodegenerative disorders that affect humans and animals. They are characterized by the accumulation in the central nervous system of a pathological form of the host-encoded prion protein (PrPC). The prion protein is a membrane glycoprotein that consists of two domains: a globular, structured C-terminus and an unstructured N-terminus. The N-terminal part of the protein is involved in different functions in both health and disease. In the present work we discuss the production and biochemical characterization of a panel of four monoclonal antibodies (mAbs) against the distal N-terminus of PrPC using a well-established methodology based on the immunization of Prnp0/0 mice. Additionally, we show their ability to block prion (PrPSc) replication at nanomolar concentrations in a cell culture model of prion infection. These mAbs represent a promising tool for prion diagnostics and for studying the physiological role of the N-terminal domain of PrPC.https://peerj.com/articles/811.pdfPrion proteinMonoclonal antibodiesHistopathologyPrion inhibition |
| spellingShingle | Alessandro Didonna Anja Colja Venturini Katrina Hartman Tanja Vranac Vladka Čurin Šerbec Giuseppe Legname Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc PeerJ Prion protein Monoclonal antibodies Histopathology Prion inhibition |
| title | Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc |
| title_full | Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc |
| title_fullStr | Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc |
| title_full_unstemmed | Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc |
| title_short | Characterization of four new monoclonal antibodies against the distal N-terminal region of PrPc |
| title_sort | characterization of four new monoclonal antibodies against the distal n terminal region of prpc |
| topic | Prion protein Monoclonal antibodies Histopathology Prion inhibition |
| url | https://peerj.com/articles/811.pdf |
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