ArticleAdvanced biomedical research2015
In silico design of fusion protein of FimH from uropathogenic Escherichia coli and MrpH from Proteus mirabilis against urinary tract infections.
Article in Advanced biomedical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Molecular docking and simulation analysis of the FimH protein with secondary metabolites from theBioinformation · 2022Article
- Fimbriae reprogram host gene expression - Divergent effects of P and type 1 fimbriae.PLoS pathogens · 2019Article
- Targeting Dynamical Binding Processes in the Design of Non-Antibiotic Anti-Adhesives by Molecular Simulation-The Example of FimH.Molecules (Basel, Switzerland) · 2018Review
- Genome sequencing and analysis of the first spontaneous Nanosilver resistant bacteriumAntimicrobial resistance and infection control · 2017Article
- Dimeric and Trimeric Fusion Proteins Generated with Fimbrial Adhesins of UropathogenicFrontiers in cellular and infection microbiology · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundUrinary tract infections (UTIs) caused by uropathogenic Escherichia coli (UPEC) and Proteus mirabilis are the most important pathogens causing UTIs. The FimH from type 1 pili of UPEC and the MrpH from P. mirabilis play critical roles in the UTI process and have presented as ideal vaccine candidates against UTIs. There is no effective vaccine against UTI and the development of an ideal UTI vaccine is required. MATERIALS AND
methodsIn this study, we planned to design a novel fusion protein of FimH from UPEC and MrpH from P. mirabilis. For this purpose, we modeled fusion protein forms computationally using the Iterative Threading Assembly Refinement (I-TASSER) server and evaluated their interactions with toll-like receptor 4 (TLR4). The best fusion protein was constructed using overlap extension polymerase chain reaction (OE-PCR) and the biological activity of fusion was evaluated by the induction of interleukin-8 (IL-8) in the HT-29 cell line.
resultsOur study indicated that based on the Protein Structure Analysis (ProSA)-web and the docking results, MrpH.FimH showed better results than did FimH.MrpH, and it was selected for construction. The results of bioassay on the HT-29 showed that FimH and MrpH.FimH induced significantly higher IL-8 responses than untreated cells or MrpH alone in the cell line tested.
conclusionsIn the present study, we designed and constructed the novel fusion protein MrpH.FimH from UPEC and P. mirabilis based on in silico methods. Our bioassay results indicate that the MrpH.FimH fusion protein is active and capable of inducing immune responses.
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