期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 22, 期 10, 页码 -出版社
MDPI
DOI: 10.3390/ijms22105127
关键词
functional amyloids; curli; aggregation; biofilm; ATR-FTIR; FT-Raman
资金
- National Science Centre, Poland [2019/35/B/NZ2/03997, 2017/26/D/ST5/00341]
- National Centre for Research and Development, Poland [POWR.03.02.00-00-I003/16]
- Wroclaw Center of Biotechnology program The Leading National Research Center (KNOW) for years 2014-2018
The study found that the self-aggregation properties of CsgA repeat fragments differ between Salmonella enterica and Escherichia coli, with Salmonella enterica showing easier and more durable formation of amyloid structures.
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.
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