β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis

Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation...

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Autores principales:	Anna I. Sulatskaya, Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail V. Belousov, Kirill S. Antonets, Maksim I. Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya V. Stepanenko, Anton A. Nizhnikov
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	amyloid β-barrel proteins amyloid fibrils amyloidosis amyloid aggregation protein aggregation Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/78f9cf2fea8f4c84a87ffd2143a1f795
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spelling	oai:doaj.org-article:78f9cf2fea8f4c84a87ffd2143a1f7952021-11-11T16:48:16Zβ-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis10.3390/ijms2221113161422-00671661-6596https://doaj.org/article/78f9cf2fea8f4c84a87ffd2143a1f7952021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11316https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which the amyloid state is native was also discovered. In particular, several prokaryotic and eukaryotic proteins with β-barrel domains were demonstrated to form amyloids in vivo, where they participate in interspecies interactions and nutrient storage, respectively. According to recent observations, despite the variety of primary structures of amyloid-forming proteins, most of them can adopt a conformational state with the β-barrel topology. This state can be intermediate on the pathway of fibrillogenesis (“on-pathway state”), or can be formed as a result of an alternative assembly of partially unfolded monomers (“off-pathway state”). The β-barrel oligomers formed by amyloid proteins possess toxicity, and are likely to be involved in the development of amyloidoses, thus representing promising targets for potential therapy of these incurable diseases. Considering rapidly growing discoveries of the amyloid-forming β-barrels, we may suggest that their real number and diversity of functions are significantly higher than identified to date, and represent only “the tip of the iceberg”. Here, we summarize the data on the amyloid-forming β-barrel proteins, their physicochemical properties, and their biological functions, and discuss probable means and consequences of the amyloidogenesis of these proteins, along with structural relationships between these two widespread types of β-folds.Anna I. SulatskayaAnastasiia O. KosolapovaAlexander G. BobylevMikhail V. BelousovKirill S. AntonetsMaksim I. SulatskyIrina M. KuznetsovaKonstantin K. TuroverovOlesya V. StepanenkoAnton A. NizhnikovMDPI AGarticleamyloidβ-barrel proteinsamyloid fibrilsamyloidosisamyloid aggregationprotein aggregationBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11316, p 11316 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	amyloid β-barrel proteins amyloid fibrils amyloidosis amyloid aggregation protein aggregation Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	amyloid β-barrel proteins amyloid fibrils amyloidosis amyloid aggregation protein aggregation Biology (General) QH301-705.5 Chemistry QD1-999 Anna I. Sulatskaya Anastasiia O. Kosolapova Alexander G. Bobylev Mikhail V. Belousov Kirill S. Antonets Maksim I. Sulatsky Irina M. Kuznetsova Konstantin K. Turoverov Olesya V. Stepanenko Anton A. Nizhnikov β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
description	Insoluble protein aggregates with fibrillar morphology called amyloids and β-barrel proteins both share a β-sheet-rich structure. Correctly folded β-barrel proteins can not only function in monomeric (dimeric) form, but also tend to interact with one another—followed, in several cases, by formation of higher order oligomers or even aggregates. In recent years, findings proving that β-barrel proteins can adopt cross-β amyloid folds have emerged. Different β-barrel proteins were shown to form amyloid fibrils in vitro. The formation of functional amyloids in vivo by β-barrel proteins for which the amyloid state is native was also discovered. In particular, several prokaryotic and eukaryotic proteins with β-barrel domains were demonstrated to form amyloids in vivo, where they participate in interspecies interactions and nutrient storage, respectively. According to recent observations, despite the variety of primary structures of amyloid-forming proteins, most of them can adopt a conformational state with the β-barrel topology. This state can be intermediate on the pathway of fibrillogenesis (“on-pathway state”), or can be formed as a result of an alternative assembly of partially unfolded monomers (“off-pathway state”). The β-barrel oligomers formed by amyloid proteins possess toxicity, and are likely to be involved in the development of amyloidoses, thus representing promising targets for potential therapy of these incurable diseases. Considering rapidly growing discoveries of the amyloid-forming β-barrels, we may suggest that their real number and diversity of functions are significantly higher than identified to date, and represent only “the tip of the iceberg”. Here, we summarize the data on the amyloid-forming β-barrel proteins, their physicochemical properties, and their biological functions, and discuss probable means and consequences of the amyloidogenesis of these proteins, along with structural relationships between these two widespread types of β-folds.
format	article
author	Anna I. Sulatskaya Anastasiia O. Kosolapova Alexander G. Bobylev Mikhail V. Belousov Kirill S. Antonets Maksim I. Sulatsky Irina M. Kuznetsova Konstantin K. Turoverov Olesya V. Stepanenko Anton A. Nizhnikov
author_facet	Anna I. Sulatskaya Anastasiia O. Kosolapova Alexander G. Bobylev Mikhail V. Belousov Kirill S. Antonets Maksim I. Sulatsky Irina M. Kuznetsova Konstantin K. Turoverov Olesya V. Stepanenko Anton A. Nizhnikov
author_sort	Anna I. Sulatskaya
title	β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
title_short	β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
title_full	β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
title_fullStr	β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
title_full_unstemmed	β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis
title_sort	β-barrels and amyloids: structural transitions, biological functions, and pathogenesis
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/78f9cf2fea8f4c84a87ffd2143a1f795
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β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis

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