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

Sulatskaya, Anna I.; Kosolapova, Anastasiia O.; Bobylev, Alexander G.; Belousov, Mikhail V.; Antonets, Kirill S.; Sulatsky, Maksim I.; Kuznetsova, Irina M.; Turoverov, Konstantin K.; Stepanenko, Olesya V.; Nizhnikov, Anton A.

doi:10.3390/ijms222111316

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

by

Anna I. Sulatskaya

^1,2

,

Anastasiia O. Kosolapova

^1,3

,

Alexander G. Bobylev

⁴

,

Mikhail V. Belousov

^1,3

,

Kirill S. Antonets

^1,3

,

Maksim I. Sulatsky

⁵

,

Irina M. Kuznetsova

²

,

Konstantin K. Turoverov

²

,

Olesya V. Stepanenko

²

and

Anton A. Nizhnikov

^1,3,*

¹

Laboratory for Proteomics of Supra-Organismal Systems, All-Russia Research Institute for Agricultural Microbiology, 3 Podbelskogo Sh., Pushkin, 196608 St. Petersburg, Russia

²

Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia

³

Faculty of Biology, St. Petersburg State University, 7/9 Universitetskaya Emb., 199034 St. Petersburg, Russia

⁴

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 3 Institutskaya St., 142290 Moscow, Russia

⁵

Laboratory of Cell Morphology, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Av., 194064 St. Petersburg, Russia

^*

Author to whom correspondence should be addressed.

Int. J. Mol. Sci. 2021, 22(21), 11316; https://doi.org/10.3390/ijms222111316

Submission received: 28 September 2021 / Revised: 15 October 2021 / Accepted: 18 October 2021 / Published: 20 October 2021

(This article belongs to the Special Issue Protein-Based Infection, Inheritance, and Memory)

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Abstract

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.

Keywords: amyloid; β-barrel proteins; amyloid fibrils; amyloidosis; amyloid aggregation; protein aggregation

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MDPI and ACS Style

Sulatskaya, A.I.; Kosolapova, A.O.; Bobylev, A.G.; Belousov, M.V.; Antonets, K.S.; Sulatsky, M.I.; Kuznetsova, I.M.; Turoverov, K.K.; Stepanenko, O.V.; Nizhnikov, A.A. β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis. Int. J. Mol. Sci. 2021, 22, 11316. https://doi.org/10.3390/ijms222111316

AMA Style

Sulatskaya AI, Kosolapova AO, Bobylev AG, Belousov MV, Antonets KS, Sulatsky MI, Kuznetsova IM, Turoverov KK, Stepanenko OV, Nizhnikov AA. β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis. International Journal of Molecular Sciences. 2021; 22(21):11316. https://doi.org/10.3390/ijms222111316

Chicago/Turabian Style

Sulatskaya, Anna I., Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail V. Belousov, Kirill S. Antonets, Maksim I. Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya V. Stepanenko, and Anton A. Nizhnikov. 2021. "β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis" International Journal of Molecular Sciences 22, no. 21: 11316. https://doi.org/10.3390/ijms222111316

APA Style

Sulatskaya, A. I., Kosolapova, A. O., Bobylev, A. G., Belousov, M. V., Antonets, K. S., Sulatsky, M. I., Kuznetsova, I. M., Turoverov, K. K., Stepanenko, O. V., & Nizhnikov, A. A. (2021). β-Barrels and Amyloids: Structural Transitions, Biological Functions, and Pathogenesis. International Journal of Molecular Sciences, 22(21), 11316. https://doi.org/10.3390/ijms222111316

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

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