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ISSN (Print): 1872-2083
ISSN (Online): 2212-4012

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Research Article

Designing an Outer Membrane Protein (Omp-W) Based Vaccine for Immunization against Vibrio and Salmonella: An in silico Approach

Author(s): Sadra S. Tehrani, Abolfazl Jahangiri, Mortaza Taheri-Anganeh, Hossein Maghsoudi, Saeed Khalili, Saeed E. Fana, Mahmood Maniati and Jafar Amani*

Volume 14, Issue 4, 2020

Page: [312 - 324] Pages: 13

DOI: 10.2174/1874609813666200929113341

Price: $65

Abstract

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 that has immune cells recognizing epitopes and is considered as an antigen. The construct can be overexpressed in an E. coli.

Conclusion: The multi-epitope vaccine is a suitable stimulator for the immune system and would be a candidate for experimental research. Recent patents describe numerous inventions related to the clinical facets of vaccine peptide against human infectious disease.

Keywords: Bioinformatics, immune response, O-mpW, salmonella infections, vaccination, vibrio cholera.

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[1]
WHO Surveillance and outbreak management of water-related infectious diseases associated with water-supply systems 2019. Available from: https://www.euro.who.int/en/publications/abstracts/surveillance-and-outbreak-management-of-water-related-infectious-diseases-associated-with-water-supply-systems-2019
[2]
Zhang X, Lin H, Wang X, Austin B. Significance of Vibrio species in the marine organic carbon cycle-a review Sci China Earth Sci 2018; 61(10): 1357-68.
[http://dx.doi.org/10.1007/s11430-017-9229-x]
[3]
Le Roux F, Wegner KM, Baker-Austin C, Vezzulli L, Osorio CR, Amaro C, et al. The emergence of Vibrio pathogens in Europe: ecology, evolution, and pathogenesis (Paris, 11-12th March 2015). Front Microbiol 2015; 6: 830.
[PMID: 26322036]
[4]
De Vita D, Angeli A, Pandolfi F, Bortolami M, Costi R, Di Santo R, et al. Inhibition of the α-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties. J Enzyme Inhib Med Chem 2017; 32(1): 798-804.
[http://dx.doi.org/10.1080/14756366.2017.1327522] [PMID: 28569564]
[5]
Swayne DE, Boulianne M, Logue CM, McDougald LR, Nair V, Suarez DL, et al. Diseases of poultry. Hoboken, New Jersey: Wiley 2020; pp. 717-53.
[http://dx.doi.org/10.1002/9781119371199.ch16]
[6]
Li W, Wen L, Li C, Chen R, Ye Z, Zhao J, et al. Contribution of the outer membrane protein OmpW in Escherichia coli to complement resistance from binding to factor H. Microb Pathog 2016; 98: 57-62.
[http://dx.doi.org/10.1016/j.micpath.2016.06.024] [PMID: 27364548]
[7]
Fu X, Zhang J, Li T, Zhang M, Li J, Kan B. The outer membrane protein OmpW enhanced V. cholerae growth in hypersaline conditions by transporting carnitine. Front Microbiol 2018; 8: 2703.
[http://dx.doi.org/10.3389/fmicb.2017.02703] [PMID: 29403450]
[8]
Vakili A, Mousavi Gargari SL, Nazarian S, Amani J. Designing and expression of recombinant chimeric protein containing CtxB and OmpW from Vibrio cholerae and evaluation of its immunogenicity. Iran J Immunol 2018; 15(3): 207-20.
[PMID: 30246696]
[9]
Tabrizi NM, Amani J, Ebrahimzadeh M, Nazarian S, Kazemi R, Almasian P. Preparation and evaluation of chitosan nanoparticles containing CtxB antigen against Vibrio cholera. Microb Pathog 2018; 124: 170-7.
[http://dx.doi.org/10.1016/j.micpath.2018.08.037] [PMID: 30138759]
[10]
Cho Y, Park S, Barate AK, Truong QL, Han JH, Jung CH, et al. Proteomic analysis of outer membrane proteins in Salmonella enterica Enteritidis. J Microbiol Biotechnol 2015; 25(2): 288-95.
[http://dx.doi.org/10.4014/jmb.1410.10052] [PMID: 25418479]
[11]
Morales EH, Calderón IL, Collao B, Gil F, Porwollik S, McClelland M, et al. Hypochlorous acid and hydrogen peroxide-induced negative regulation of Salmonella enterica serovar Typhimurium ompW by the response regulator ArcA. BMC Microbiol 2012; 12(1): 63.
[http://dx.doi.org/10.1186/1471-2180-12-63] [PMID: 22545862]
[12]
Fasihi-Ramandi M, Ghobadi-Ghadikolaee H, Ahmadi-Renani S, Taheri RA, Ahmadi K. Vibrio cholerae lipopolysaccharide loaded chitosan nanoparticle could save life by induction of specific immunoglobulin isotype. Artif Cells Nanomed Biotechnol 2018; 46(1): 56-61.
[http://dx.doi.org/10.1080/21691401.2017.1290646] [PMID: 28278575]
[13]
Yadav SK, Meena JK, Sharma M, Dixit A. Recombinant outer membrane protein C of Aeromonas hydrophila elicits mixed immune response and generates agglutinating antibodies. Immunol Res 2016; 64(4): 1087-99.
[http://dx.doi.org/10.1007/s12026-016-8807-9] [PMID: 27328672]
[14]
Farhadi T, Nezafat N, Ghasemi Y, Karimi Z, Hemmati S, Erfani N. Designing of complex multi-epitope peptide vaccine based on omps of Klebsiella pneumoniae: an in silico approach. Int J Pept Res Ther 2015; 21(3): 325-41.
[http://dx.doi.org/10.1007/s10989-015-9461-0]
[15]
Rauta PR, Ashe S, Nayak D, Nayak B. In silico identification of outer membrane protein (Omp) and subunit vaccine design against pathogenic Vibrio cholerae. Comput Biol Chem 2016; 65: 61-8.
[http://dx.doi.org/10.1016/j.compbiolchem.2016.10.004] [PMID: 27769003]
[16]
Taheri-Anganeh M, Khatami SH, Jamali Z, Savardashtaki A, Ghasemi Y, Mostafavi-Pour Z. In silico analysis of suitable signal peptides for secretion of a recombinant alcohol dehydrogenase with a key role in atorvastatin enzymatic synthesis. Mol Biol Res Commun 2019; 8(1): 17-26.
[PMID: 31528640]
[17]
Khatami SH, Taheri-Anganeh M, Arianfar F, Savardashtaki A, Sarkari B, Ghasemi Y, et al. Analyzing signal peptides for secretory production of recombinant diagnostic antigen B8/1 from Echinococcus granulosus: an in silico Approach. Mol Biol Res Commun 2020; 9(1): 1-10.
[PMID: 32582787]
[18]
Abdollahi S, Morowvat M, Savardashtaki A, Irajie C, Najafipour S, Zarei M, et al. Amino acids sequence based analysis of arginine deiminase from different prokaryotic organisms: an in silico approach. Recent Pat Biotechnol 2020; 14(3): 235-46.
[http://dx.doi.org/10.2174/1872208314666200324114441] [PMID: 32208128]
[19]
Zarei M, Nezafat N, Morowvat MH, Ektefaie M, Ghasemi Y. In silico analysis of different signal peptides for secretory production of arginine deiminase in Escherichia coli. Recent Pat Biotechnol 2019; 13(3): 217-27.
[http://dx.doi.org/10.2174/1872208313666190101114602] [PMID: 30621572]
[20]
Mousavi P, Mostafavi-Pour Z, Morowvat MH, Nezafat N, Zamani M, Berenjian A, et al. In silico analysis of several signal peptides for the excretory production of reteplase in Escherichia coli. Curr Proteomics 2017; 14(4): 326-35.
[http://dx.doi.org/10.2174/1570164614666170809144446]
[21]
Yousefi T, Mir SM, Asadi J, Tourani M, Karimian A, Maniati M, et al. In silico analysis of non-synonymous single nucleotide polymorphism in a human KLK-2 gene associated with prostate cancer. Meta Gene 2019; 211: 00578.
[http://dx.doi.org/10.1016/j.mgene.2019.100578]
[22]
Jamali Z, Taheri-Anganeh M, Entezam M. Prediction of potential deleterious nonsynonymous single nucleotide polymorphisms of HIF1A gene: a computational approach. Comput Biol Chem 2020; 88: 107354.
[http://dx.doi.org/10.1016/j.compbiolchem.2020.107354] [PMID: 32801061]
[23]
Taheri-Anganeh M, Amiri A, Movahedpour A, Khatami SH, Ghasemi Y, Savardashtaki A, et al. In silico Evaluation of PLAC1-fliC as a chimeric vaccine against breast cancer. Iran Biomed J 2020; 24(3): 173-82.
[http://dx.doi.org/10.29252/ibj.24.3.173] [PMID: 31952435]
[24]
Jalali SA, Parmiani G. Pre-clinical and clinical aspects of peptide-based vaccine against human solid tumors. Recent Pat Biotechnol 2011; 5(2): 108-17.
[http://dx.doi.org/10.2174/187220811796365716] [PMID: 21707528]
[25]
Pundir S, Martin MJ, O’Donovan C. UniProt protein knowledgebase Protein Bioinformatics. Heidelberg: Springer 2017; pp. 41-55.
[http://dx.doi.org/10.1007/978-1-4939-6783-4_2]
[26]
Tsirigos KD, Elofsson A, Bagos PG. PRED-TMBB2: improved topology prediction and detection of beta-barrel outer membrane proteins. Bioinformatics 2016; 32(17): i665-71.
[http://dx.doi.org/10.1093/bioinformatics/btw444] [PMID: 27587687]
[27]
Tourani M, Karkhah A, Najafi A. Development of an epitope-based vaccine inhibiting immune cells rolling and migration against atherosclerosis using in silico approaches. Comput Biol Chem 2017; 70: 156-63.
[http://dx.doi.org/10.1016/j.compbiolchem.2017.08.016] [PMID: 28886485]
[28]
Bianchini G, Gianni L. The immune system and response to HER2-targeted treatment in breast cancer. Lancet Oncol 2014; 15(2): e58-68.
[http://dx.doi.org/10.1016/S1470-2045(13)70477-7] [PMID: 24480556]
[29]
Zaharieva N, Dimitrov I, Flower D, Doytchinova I. Immunogenicity prediction by VaxiJen: a ten year overview. J Proteomics Bioinform 2017; 10: 298-310.
[30]
Yu DS, Lee DH, Kim SK, Lee CH, Song JY, Kong EB, et al. Algorithm for predicting functionally equivalent proteins from BLAST and HMMER searches. J Microbiol Biotechnol 2012; 22(8): 1054-8.
[http://dx.doi.org/10.4014/jmb.1203.03050] [PMID: 22713980]
[31]
Vita R, Overton JA, Greenbaum JA, et al. The immune epitope database (IEDB) 3.0. Nucleic Acids Res 2015; 43(Database issue): D405-12.
[http://dx.doi.org/10.1093/nar/gku938] [PMID: 25300482]
[32]
Zamani M, Nezafat N, Negahdaripour M, Dabbagh F, Ghasemi Y. In silico evaluation of different signal peptides for the secretory production of human growth hormone in E. coli. Int J Pept Res 2015; 21(3): 261-8.
[http://dx.doi.org/10.1007/s10989-015-9454-z]
[33]
MacRaild CA, Richards JS, Anders RF, Norton RS. Antibody recognition of disordered antigens. Structure 2016; 24(1): 148-57.
[http://dx.doi.org/10.1016/j.str.2015.10.028] [PMID: 26712277]
[34]
Pan Q, Wang H, Ouyang W, Wang X, Bi Z, Xia X, et al. Immunogenicity of adenovirus-derived porcine parvovirus-like particles displaying B and T cell epitopes of foot-and-mouth disease. Vaccine 2016; 34(4): 578-85.
[http://dx.doi.org/10.1016/j.vaccine.2015.11.003] [PMID: 26685093]
[35]
Mohammad N, Karsabet MT, Amani J, Ardjmand A, Zadeh MR, Gholi MK, et al. In silico design of a chimeric protein containing antigenic fragments of Helicobacter pylori; a bioinformatic approach. Open Microbiol J 2016; 10: 97-112.
[http://dx.doi.org/10.2174/1874285801610010097] [PMID: 27335622]
[36]
Capasso C, Whalley T, Marwah V, Serafin A, Fusciello M, Feola S, et al. In silico design of a chimeric protein containing antigenic fragments of Helicobacter pylori; a bioinformatic approach. Open Microbiol J 2017; 10: 97.
[37]
Harris JB. Cholera: immunity and prospects in vaccine development. J Infect 2018; 218(suppl_3): S141-6.
[38]
Mayer A, Balasubramanian V, Mora T, Walczak AM. How a well-adapted immune system is organized. Proc Natl Acad Sci USA 2015; 112(19): 5950-5.
[http://dx.doi.org/10.1073/pnas.1421827112] [PMID: 25918407]
[39]
Gutjahr A, Tiraby G, Perouzel E, Verrier B, Paul S. Triggering intracellular receptors for vaccine adjuvantation. Trends Immunol 2016; 37(9): 573-87.
[http://dx.doi.org/10.1016/j.it.2016.07.001] [PMID: 27474233]
[40]
Pham OH, McSorley SJ. Protective host immune responses to Salmonella infection. Future Microbiol 2015; 10(1): 101-10.
[http://dx.doi.org/10.2217/fmb.14.98] [PMID: 25598340]
[41]
Sun H, Kamanova J, Lara-Tejero M, Galán JE. Salmonella stimulates pro-inflammatory signalling through p21-activated kinases bypassing innate immune receptors. Nat Microbiol 2018; 3(10): 1122-30.
[http://dx.doi.org/10.1038/s41564-018-0246-z] [PMID: 30224799]

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