In Silico Analysis of Potential Outer Membrane Beta-Barrel Proteins in Aeromonas hydrophila Pangenome

• Published in: International journal of peptide research and therapeutics Vol. 27; no. 4; pp. 2381 - 2389
• Main Authors: Awan, Furqan, Ali, Muhammad Muddassir, Dong, Yuhao, Yu, Yong, Zeng, Zhenling, Liu, Yongjie
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01-12-2021; Springer Nature B.V
• Subjects: Aeromonas hydrophila; Amino acid substitution; Animal Anatomy; Antigenicity; Binding sites; Biochemistry; Biomedical and Life Sciences; Epitopes; Genomes; Histology; Life Sciences; Lymphocytes B; Membrane proteins; Molecular Medicine; Morphology; Outer membrane proteins; Pharmaceutical Sciences/Technology; Pharmacology/Toxicology; Polymer Sciences; Proteins; Vaccine development; Vaccines; Virulence; In silico; Beta barrel; Pangenome; Outer membrane protein
• ISSN: 1573-3149; 1573-3904
• DOI: 10.1007/s10989-021-10259-z

Outer membrane proteins (OMPs) of
Aeromonas hydrophila
have a variety of functional roles in virulence and pathogenesis and represent promising targets for vaccine development. The main objective of this study was to develop an in-silico model of beta-barrel OMP present among the valid
A. hydrophila
pangenomes (n = 22). With a program named the β-barrel Outer Membrane Protein Predictor (BOMP), total beta-barrel OMPs (n = 3127) were predicted across 22 genomes with the estimated median number of 64 per genome. In pangenome analysis, only 32 OMPs were found to be conserved. These beta-barrel OMPs also showed variations among source of isolation, COG and KEGG classes. Among 32 conserved OMPs, a highly antigenic protein was identified by utilizing Vaxijen. With B cell epitope predictions, two fragments of amino acid sequences i.e. GLTLGAQFTGNNDPQNADRSN (21 mer) and FKPSLAYLRTDVKDNARGI DDTATEY (26 mer) bearing B-cell binding sites were selected. Further, an epitope (12 amino acids: GLTLGAQFTGNN) that complexes to maximum MHC alleles with a higher antigenicity was determined. The analysis of evolutionary forces on the identified OMP sequence and epitope indicated that none of basic amino acid sites has shown significantly different substitution ratios. This conserved protein and epitope will be helpful in developing a vaccine that may be effective against all the
A. hydrophila
strains. Also, this study provides a theoretical basis for vaccine design against other pathogenic bacteria.