Abstract
Salmonella OmpC sequence analysis by Clustal revealed a unique amino acid residue (TSNGSNPST) in positions from 268 to 276. This region has seemingly been deleted in the Escherichia coli OmpC protein which is conserved in Salmonella and not present in Escherichia coli. In this study, the structure visualization and homology with the already existing 3D structure of S. Typhi osmoporin (OmpC) (3UU2) was carried out to get structural insight of the unique amino acid hits identified. The ability of the peptide (commercially synthesized) for their antigenicity using rabbit S. Typhi antisera and immunogenicity study with mice immunized with the OVA-conjugated peptide is also discussed. This study extends new possibilities of exploring the unique conserved amino acid patch as possible target for antibody detection, which may be Salmonella specific and also with a chance to induce memory response against the surface epitope possibly acting as a vaccine.
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Acknowledgements
The first author likes to extend his warm gratitude towards CSIR, Government of India for providing the Senior Research Fellowship stipend during the course of the study. The authors thank Prof. M.A. Vijayalakshmi, Director, Centre for Bioseparation Technology, VIT, Vellore, for providing the support and facilities. The authors also thank the Department of Science and Technology, Government of India, and VIT, Vellore for providing the facilities.
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Padmanabhan, V., Kumar, S. & Jayaprakash, N.S. Structural Characterization of a Unique Peptide in Porin: An Approach Towards Specific Detection of Salmonella enterica Serovar Typhi. Int J Pept Res Ther 25, 1651–1657 (2019). https://doi.org/10.1007/s10989-019-09807-5
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DOI: https://doi.org/10.1007/s10989-019-09807-5