Background:
Cholera triggered by Vibrio cholerae remains the main reason for
morbidity and mortality all over the world. In addition, salmonellosis is regarded as an infectious
disease that makes it essential for the identification and detection of Salmonella.
With a beta-barrel structure consisting of eight non-parallel beta strands, OmpW family is
widely distributed among gram-negative bacteria. Moreover, OmpW isolated from
S. typhimurium and Vibrio cholerae can be used in vaccine design.
Methods:
Topology prediction was determined. T-cell and B-cell epitopes were selected
from exposed areas, and sequence conservancy was evaluated. The remaining loops and
inaccessible residues were removed to prepare OmpW-1. High antigenicity peptides were
detected to replace inappropriate residues to obtain OmpW-2. Physicochemical properties
were assessed, and antigenicity, hydrophobicity, flexibility, and accessibility were compared
to the native Omp-W structure. Low score areas were removed from the designed
structure for preparing the OmpW-3. To construct OmpW-4, TTFrC was used as T-CD4+
cell-stimulating factor and CTB as adjuvant to the end of the C-terminal of this sequence,
which can increase the antigenicity and sequence density. The sequences were re-analyzed
to delete the unfavorable residues. Besides, the solubility of the mature OmpW and the designed
structure were predicted while overexpressed in E. coli.
Results:
The designed vaccine is a stable protein which has immune cells recognizing epitopes and is considered as an
antigen. The construct can be overexpressed in a E. coli.
Conclusion:
The multi-epitope vaccine is a suitable stimulator for immune system and would be a candidate for
experimental research. Recent patents describing numerous inventions related to the clinical facets of vaccine peptide
against human infectious disease.
Improved topology prediction using the terminal hydrophobic helices rule