Journal
INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS
Volume 27, Issue 2, Pages 1149-1166Publisher
SPRINGER
DOI: 10.1007/s10989-020-10157-w
Keywords
Helicobacter pylori; B-cell; T-cell; In-silico; Novel vaccine; Molecular dynamics simulation
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Helicobacter pylori is a highly potential pathogen colonizing in the human stomach, which poses serious health threats worldwide. Developing a novel vaccine construct using B-cell derived T-cell epitopes from four target antigenic proteins shows potential for inducing immune response. Additionally, protein-protein docking and molecular dynamics simulation studies suggest stable and proper binding interaction between Toll like receptor 5 and the vaccine candidate, indicating potential efficacy in combating H. pylori infection.
Helicobacter pylori is a highly potential pathogen to colonize in the human stomach. This bacterial strain is now alarming serious health concern all over the world. Combating through available drugs is a difficult task due to lack of appropriate common targets against genetically diverse strains. Therefore, the developments of effective targets vaccines require alternative strategies to eliminate the H. pylori infection. In this study, we developed a novel vaccine construct using B-cell derived T-cell epitopes from four target antigenic proteins (HpaA, FlaA, FlaB and Omp18), and found the induction of possible immune response using advanced immunoinformatics approaches. In order to boost immune system, we tagged adjuvant (50S ribosomal protein L7/L12) with a suitable linker at the N-terminus side of vaccine sequence. Protein-protein docking between human Toll like receptor 5 (TLR5) and vaccine construct help to predict the way of inductive signaling that leads to immune-response. The calculated negative score (- 151.4, + / - 8.7) of molecular docking complex signify the best binding interface. Molecular dynamics simulation studies confirmed the proper docking between TLR5 and vaccine candidate. Moreover, Normal mode analysis (NMA) calculates the molecular motion of the docking complex. The low eigenvalue (2.935e(-05)) indicates the stable and flexible molecular motion in the binding interaction side. Finally, in-silico cloning of vaccine candidate was performed using expression vector pET28b (+) with the optimized restriction sites.
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