Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates
Prion protein amyloid aggregates are associated with infectious neurodegenerative diseases, known as transmissible spongiform encephalopathies. Self-replication of amyloid structures by refolding of native protein molecules is the probable mechanism of disease transmission. Amyloid fibril formation...
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MDPI AG
2020-10-01
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| Series: | International Journal of Molecular Sciences |
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| author | Tomas Sneideris Mantas Ziaunys Brett K.-Y. Chu Rita P.-Y. Chen Vytautas Smirnovas |
| author_facet | Tomas Sneideris Mantas Ziaunys Brett K.-Y. Chu Rita P.-Y. Chen Vytautas Smirnovas |
| author_sort | Tomas Sneideris |
| collection | DOAJ |
| description | Prion protein amyloid aggregates are associated with infectious neurodegenerative diseases, known as transmissible spongiform encephalopathies. Self-replication of amyloid structures by refolding of native protein molecules is the probable mechanism of disease transmission. Amyloid fibril formation and self-replication can be affected by many different factors, including other amyloid proteins and peptides. Mouse prion protein fragments 107-143 (PrP(107-143)) and 89-230 (PrP(89-230)) can form amyloid fibrils. <inline-formula><math display="inline"><semantics><mi mathvariant="sans-serif">β</mi></semantics></math></inline-formula>-sheet core in PrP(89-230) amyloid fibrils is limited to residues ∼160–220 with unstructured N-terminus. We employed chemical kinetics tools, atomic force microscopy and Fourier-transform infrared spectroscopy, to investigate the effects of mouse prion protein fragment 107-143 fibrils on the aggregation of PrP(89-230). The data suggest that amyloid aggregates of a short prion-derived peptide are not able to seed PrP(89-230) aggregation; however, they accelerate the self-replication of PrP(89-230) amyloid fibrils. We conclude that PrP(107-143) fibrils could facilitate the self-replication of PrP(89-230) amyloid fibrils in several possible ways, and that this process deserves more attention as it may play an important role in amyloid propagation. |
| first_indexed | 2024-03-10T15:48:20Z |
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| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T15:48:20Z |
| publishDate | 2020-10-01 |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-f9968bff96fd4106b07e0a94f4004c472023-11-20T16:20:47ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-10-012119741010.3390/ijms21197410Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 AggregatesTomas Sneideris0Mantas Ziaunys1Brett K.-Y. Chu2Rita P.-Y. Chen3Vytautas Smirnovas4Institute of Biothechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biothechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaInstitute of Biological Chemistry, Academia Sinica, Taipei 115, TaiwanInstitute of Biological Chemistry, Academia Sinica, Taipei 115, TaiwanInstitute of Biothechnology, Life Sciences Center, Vilnius University, LT-10257 Vilnius, LithuaniaPrion protein amyloid aggregates are associated with infectious neurodegenerative diseases, known as transmissible spongiform encephalopathies. Self-replication of amyloid structures by refolding of native protein molecules is the probable mechanism of disease transmission. Amyloid fibril formation and self-replication can be affected by many different factors, including other amyloid proteins and peptides. Mouse prion protein fragments 107-143 (PrP(107-143)) and 89-230 (PrP(89-230)) can form amyloid fibrils. <inline-formula><math display="inline"><semantics><mi mathvariant="sans-serif">β</mi></semantics></math></inline-formula>-sheet core in PrP(89-230) amyloid fibrils is limited to residues ∼160–220 with unstructured N-terminus. We employed chemical kinetics tools, atomic force microscopy and Fourier-transform infrared spectroscopy, to investigate the effects of mouse prion protein fragment 107-143 fibrils on the aggregation of PrP(89-230). The data suggest that amyloid aggregates of a short prion-derived peptide are not able to seed PrP(89-230) aggregation; however, they accelerate the self-replication of PrP(89-230) amyloid fibrils. We conclude that PrP(107-143) fibrils could facilitate the self-replication of PrP(89-230) amyloid fibrils in several possible ways, and that this process deserves more attention as it may play an important role in amyloid propagation.https://www.mdpi.com/1422-0067/21/19/7410amyloidprionaggregationself-replication |
| spellingShingle | Tomas Sneideris Mantas Ziaunys Brett K.-Y. Chu Rita P.-Y. Chen Vytautas Smirnovas Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates International Journal of Molecular Sciences amyloid prion aggregation self-replication |
| title | Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates |
| title_full | Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates |
| title_fullStr | Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates |
| title_full_unstemmed | Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates |
| title_short | Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates |
| title_sort | self replication of prion protein fragment 89 230 amyloid fibrils accelerated by prion protein fragment 107 143 aggregates |
| topic | amyloid prion aggregation self-replication |
| url | https://www.mdpi.com/1422-0067/21/19/7410 |
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