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- Title
Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein of Salmonella enterica and Escherichia coli.
- Authors
Szulc, Natalia; Gąsior-Głogowska, Marlena; Wojciechowski, Jakub W.; Szefczyk, Monika; Żak, Andrzej M.; Burdukiewicz, Michał; Kotulska, Malgorzata; Smirnovas, Vytautas; Turoverov, Konstantin K.
- Abstract
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.
- Subjects
ESCHERICHIA coli; BACTERIAL proteins; AMINO acid residues; SALMONELLA enterica; AMYLOID; TRANSMISSION electron microscopy
- Publication
International Journal of Molecular Sciences, 2021, Vol 22, Issue 10, p5127
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms22105127