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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doaj-f9968bff96fd4106b07e0a94f4004c472020-11-25T03:50:53ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-10-01217410741010.3390/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 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Tomas Sneideris Mantas Ziaunys Brett K.-Y. Chu Rita P.-Y. Chen Vytautas Smirnovas |
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 |
author_facet |
Tomas Sneideris Mantas Ziaunys Brett K.-Y. Chu Rita P.-Y. Chen Vytautas Smirnovas |
author_sort |
Tomas Sneideris |
title |
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_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_sort |
self-replication of prion protein fragment 89-230 amyloid fibrils accelerated by prion protein fragment 107-143 aggregates |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2020-10-01 |
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. |
topic |
amyloid prion aggregation self-replication |
url |
https://www.mdpi.com/1422-0067/21/19/7410 |
work_keys_str_mv |
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