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In silico structural and physicochemical characterization of fimbrial chaperones from Human and animal Pathogenic Escherichia coli
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| Author:
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VAJIHEH ESKANDARI
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| Abstract:
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Escherichia coli (E. coli) are considered as the most common causes of bacterial infections in humans and animals. Fimbriae are among the most important pathogenic factors in E.coli establishing bacterial pathogens on specific cells of the host.The production of animal bacterial fimbriae is also based on chaperone–usher (CU) secretion pathway like most human bacterial fimbriae. There are significant similarities between physicochemical properties and structural characterization of various chaperones among different strains of E.coli.
The present study was conducted to investigate common ligand binding sites of chaperones among different pathogens. For this purpose, the physicochemical properties of chaperones were calculated using expasy’s ProtParam tool. The 3D-structure of the proteins were predicted using Modeller 9 v 20 software. The interacting surface areas of the chaperones were determined using the PDBePISA and Meta-PPISP server. The ligand-binding pockets and residues were predicted by FTMap and COACH server. Phylogenetic trees were constructed based on the multiple alignments using Mega X software.
In conclusion, the results of this study may provide useful information for finding and/or designing inhibitors to block the chaperone binding pocket which could be introduced as common drug candidates against some pathogenic E.coli.
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| Keyword:
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Pathogenic Escherichia coli, Chaperone, Modeller and Ligand Binding Pocket.
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| EOI:
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-
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| DOI:
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https://doi.org/10.31838/ijpr/2019.11.04.0306
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| Download:
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Request For Article
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