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Article

Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli

1
Department of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland
2
LPCT, CNRS, Université de Lorraine, F-54000 Nancy, France
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Department of Bioorganic Chemistry, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland
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Electron Microscopy Laboratory, Faculty of Mechanical Engineering, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wrocław, Poland
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Clinical Research Centre, Medical University of Białystok, Jana Kilińskiego 1, 15-089 Białystok, Poland
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Institute of Biochemistry and Biophysics, Polish Academy Sciences, 02-106 Warsaw, Poland
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Faculty of Natural Sciences, Brandenburg University of Technology Cottbus-Senftenberg, 01968 Senftenberg, Germany
*
Authors to whom correspondence should be addressed.
Academic Editors: Vytautas Smirnovas and Konstantin K. Turoverov
Int. J. Mol. Sci. 2021, 22(10), 5127; https://doi.org/10.3390/ijms22105127
Received: 9 April 2021 / Revised: 22 April 2021 / Accepted: 7 May 2021 / Published: 12 May 2021
(This article belongs to the Special Issue The Role of Environment in Amyloid Aggregation)
CsgA is an aggregating protein from bacterial biofilms, representing a class of functional amyloids. Its amyloid propensity is defined by five fragments (R1–R5) of the sequence, representing non-perfect repeats. Gate-keeper amino acid residues, specific to each fragment, define the fragment’s propensity for self-aggregation and aggregating characteristics of the whole protein. We study the self-aggregation and secondary structures of the repeat fragments of Salmonella enterica and Escherichia coli and comparatively analyze their potential effects on these proteins in a bacterial biofilm. Using bioinformatics predictors, ATR-FTIR and FT-Raman spectroscopy techniques, circular dichroism, and transmission electron microscopy, we confirmed self-aggregation of R1, R3, R5 fragments, as previously reported for Escherichia coli, however, with different temporal characteristics for each species. We also observed aggregation propensities of R4 fragment of Salmonella enterica that is different than that of Escherichia coli. Our studies showed that amyloid structures of CsgA repeats are more easily formed and more durable in Salmonella enterica than those in Escherichia coli. View Full-Text
Keywords: functional amyloids; curli; aggregation; biofilm; ATR-FTIR; FT-Raman functional amyloids; curli; aggregation; biofilm; ATR-FTIR; FT-Raman
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MDPI and ACS Style

Szulc, N.; Gąsior-Głogowska, M.; Wojciechowski, J.W.; Szefczyk, M.; Żak, A.M.; Burdukiewicz, M.; Kotulska, M. Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli. Int. J. Mol. Sci. 2021, 22, 5127. https://doi.org/10.3390/ijms22105127

AMA Style

Szulc N, Gąsior-Głogowska M, Wojciechowski JW, Szefczyk M, Żak AM, Burdukiewicz M, Kotulska M. Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli. International Journal of Molecular Sciences. 2021; 22(10):5127. https://doi.org/10.3390/ijms22105127

Chicago/Turabian Style

Szulc, Natalia; Gąsior-Głogowska, Marlena; Wojciechowski, Jakub W.; Szefczyk, Monika; Żak, Andrzej M.; Burdukiewicz, Michał; Kotulska, Malgorzata. 2021. "Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli" Int. J. Mol. Sci. 22, no. 10: 5127. https://doi.org/10.3390/ijms22105127

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