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Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii

Morganella morganii is one of the main etiological agents of hospital-acquired infections and no licensed vaccine is available against the pathogen. Herein, we designed a multi-epitope-based vaccine against M. morganii. Predicted proteins from fully sequenced genomes of the pathogen were subjected t...

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Autores principales: Ullah, Asad, Ahmad, Sajjad, Ismail, Saba, Afsheen, Zobia, Khurram, Muhammad, Tahir ul Qamar, Muhammad, AlSuhaymi, Naif, Alsugoor, Mahdi H., Allemailem, Khaled S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8535705/
https://www.ncbi.nlm.nih.gov/pubmed/34682706
http://dx.doi.org/10.3390/ijerph182010961
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author Ullah, Asad
Ahmad, Sajjad
Ismail, Saba
Afsheen, Zobia
Khurram, Muhammad
Tahir ul Qamar, Muhammad
AlSuhaymi, Naif
Alsugoor, Mahdi H.
Allemailem, Khaled S.
author_facet Ullah, Asad
Ahmad, Sajjad
Ismail, Saba
Afsheen, Zobia
Khurram, Muhammad
Tahir ul Qamar, Muhammad
AlSuhaymi, Naif
Alsugoor, Mahdi H.
Allemailem, Khaled S.
author_sort Ullah, Asad
collection PubMed
description Morganella morganii is one of the main etiological agents of hospital-acquired infections and no licensed vaccine is available against the pathogen. Herein, we designed a multi-epitope-based vaccine against M. morganii. Predicted proteins from fully sequenced genomes of the pathogen were subjected to a core sequences analysis, followed by the prioritization of non-redundant, host non-homologous and extracellular, outer membrane and periplasmic membrane virulent proteins as vaccine targets. Five proteins (TonB-dependent siderophore receptor, serralysin family metalloprotease, type 1 fimbrial protein, flagellar hook protein (FlgE), and pilus periplasmic chaperone) were shortlisted for the epitope prediction. The predicted epitopes were checked for antigenicity, toxicity, solubility, and binding affinity with the DRB*0101 allele. The selected epitopes were linked with each other through GPGPG linkers and were joined with the cholera toxin B subunit (CTBS) to boost immune responses. The tertiary structure of the vaccine was modeled and blindly docked with MHC-I, MHC-II, and Toll-like receptors 4 (TLR4). Molecular dynamic simulations of 250 nanoseconds affirmed that the designed vaccine showed stable conformation with the receptors. Further, intermolecular binding free energies demonstrated the domination of both the van der Waals and electrostatic energies. Overall, the results of the current study might help experimentalists to develop a novel vaccine against M. morganii.
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spelling pubmed-85357052021-10-23 Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii Ullah, Asad Ahmad, Sajjad Ismail, Saba Afsheen, Zobia Khurram, Muhammad Tahir ul Qamar, Muhammad AlSuhaymi, Naif Alsugoor, Mahdi H. Allemailem, Khaled S. Int J Environ Res Public Health Article Morganella morganii is one of the main etiological agents of hospital-acquired infections and no licensed vaccine is available against the pathogen. Herein, we designed a multi-epitope-based vaccine against M. morganii. Predicted proteins from fully sequenced genomes of the pathogen were subjected to a core sequences analysis, followed by the prioritization of non-redundant, host non-homologous and extracellular, outer membrane and periplasmic membrane virulent proteins as vaccine targets. Five proteins (TonB-dependent siderophore receptor, serralysin family metalloprotease, type 1 fimbrial protein, flagellar hook protein (FlgE), and pilus periplasmic chaperone) were shortlisted for the epitope prediction. The predicted epitopes were checked for antigenicity, toxicity, solubility, and binding affinity with the DRB*0101 allele. The selected epitopes were linked with each other through GPGPG linkers and were joined with the cholera toxin B subunit (CTBS) to boost immune responses. The tertiary structure of the vaccine was modeled and blindly docked with MHC-I, MHC-II, and Toll-like receptors 4 (TLR4). Molecular dynamic simulations of 250 nanoseconds affirmed that the designed vaccine showed stable conformation with the receptors. Further, intermolecular binding free energies demonstrated the domination of both the van der Waals and electrostatic energies. Overall, the results of the current study might help experimentalists to develop a novel vaccine against M. morganii. MDPI 2021-10-19 /pmc/articles/PMC8535705/ /pubmed/34682706 http://dx.doi.org/10.3390/ijerph182010961 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ullah, Asad
Ahmad, Sajjad
Ismail, Saba
Afsheen, Zobia
Khurram, Muhammad
Tahir ul Qamar, Muhammad
AlSuhaymi, Naif
Alsugoor, Mahdi H.
Allemailem, Khaled S.
Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii
title Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii
title_full Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii
title_fullStr Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii
title_full_unstemmed Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii
title_short Towards A Novel Multi-Epitopes Chimeric Vaccine for Simulating Strong Immune Responses and Protection against Morganella morganii
title_sort towards a novel multi-epitopes chimeric vaccine for simulating strong immune responses and protection against morganella morganii
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8535705/
https://www.ncbi.nlm.nih.gov/pubmed/34682706
http://dx.doi.org/10.3390/ijerph182010961
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