Structure Evaluation of IroN for Designing a Vaccine against Escherichia Coli, an In Silico Approach
Authors
Abstract:
Introduction: Some strains of Escherichia Coli, including intestinal pathogenic strains, commensal strains, and extra intestinal pathogenic E. coli (ExPEC) have a significant impact on human health status. A standard vaccine designed based on conserved epitopes can stimulate a protective immune response against these pathogens. Additionally, enhanced expression at the infection site as a pathogenesis factor in disease is crucial for an ideal vaccine candidate. The IroN protein plays a role in severe infections of E. coli. Hence, this protein will assist in developing the novel and more efficient treatments for E. coli related infections. A better understanding of protein tertiary structure can help to percept their functions and also their interactions with other molecules. There is a growing interest in using bioinformatics tool to make accurate predictions about the functional, immunological, and biochemical features of target antigens. Method: Herein, we aimed to predict the structure of the IroN protein upon its folding and determine their immunological properties. Results: In the present study, using bioinformatics analyses, we identified the highly antigenic regions of IroN protein. Our designed vaccine candidate had the highest immunological properties and folded into a typical beta-barrel structure. Conclusion: The approach of assigning structural and immunological properties of the target antigen to design the vaccine candidate could be deployed as an efficient strategy to circumvent the challenges ahead of empirical methods without dealing with ethical concerns of animal usage and human participants. Although the obtained results are promising, further experimental studies could bring about more insights on the efficiency of the designed vaccine.
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Journal title
volume 7 issue 4
pages 93- 106
publication date 2019-10
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