Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach

Aeromonas hydrophila, a gram-negative bacterium, is a major pathogen responsible for various diseases in mammals, reptiles, amphibians, fish, and humans. Targeting the specific toxin aerolysin in A. hydrophila is crucial to address antibiotic resistance and the lack of adequate and protective vaccin...

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Main Authors: Rozi, ., Tyasningsih, Wiwiek, Rahmahani, Jola, Aksono, Eduardus Bimo, Yunus, Muchammad, Al Arif, Mohammad Anam, Kuncorojati, Suryo, Kusdarwati, Rahayu, Sari, Putri Desi Wulan, Azmai, Mohammad Noor Amal, Salleh, Annas, Khanand, Nadeem, Suwarno, .
Format: Article
Language:English
Published: Faculty of Fisheries and Marine Universitas Airlangga 2024
Online Access:http://psasir.upm.edu.my/id/eprint/114778/
http://psasir.upm.edu.my/id/eprint/114778/1/114778.pdf
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author Rozi, .
Tyasningsih, Wiwiek
Rahmahani, Jola
Aksono, Eduardus Bimo
Yunus, Muchammad
Al Arif, Mohammad Anam
Kuncorojati, Suryo
Kusdarwati, Rahayu
Sari, Putri Desi Wulan
Azmai, Mohammad Noor Amal
Salleh, Annas
Khanand, Nadeem
Suwarno, .
author_facet Rozi, .
Tyasningsih, Wiwiek
Rahmahani, Jola
Aksono, Eduardus Bimo
Yunus, Muchammad
Al Arif, Mohammad Anam
Kuncorojati, Suryo
Kusdarwati, Rahayu
Sari, Putri Desi Wulan
Azmai, Mohammad Noor Amal
Salleh, Annas
Khanand, Nadeem
Suwarno, .
author_sort Rozi, .
building UPM Institutional Repository
collection Online Access
description Aeromonas hydrophila, a gram-negative bacterium, is a major pathogen responsible for various diseases in mammals, reptiles, amphibians, fish, and humans. Targeting the specific toxin aerolysin in A. hydrophila is crucial to address antibiotic resistance and the lack of adequate and protective vaccines against this intracellular and extracellular pathogen. This study aimed to identify a multi-epitope vaccine (MEV) candidate targeting the aerolysin toxin to combat the disease effectively. Standard biochemical characterization methods, detection of PCR, and sequencing of the 16S rRNA, rpoB, and aerA genes identified the isolate AHSA1 as A. hydrophila isolated from O. goramy. Subsequently, we identified B and T cell epitopes on the aerolysin protein and predicted MHC-I and MHC-II epitopes. The epitopes were then evaluated for toxicity, antigenicity, allergenicity, and solubility. The vaccine design integrated multi-epitope constructs, utilizing specialized linkers (GPGPG and EAAAK) to connect epitope peptides with the cholera toxin B subunit as an adjuvant, thereby enhancing immunogenicity. Ramachandran plots showed that 85.25% of the residues were in the most favorable regions, followed by additionally allowed regions (10.80%), generously allowed regions (1.30%), and disallowed regions (2.65%), confirming the feasibility of the modeled vaccine design. Based on docking simulations, the MEV had strong binding energies with TLR-4 (-1081.4 kcal/mol), TLR-9 (-723.2 kcal/mol), MHC-I (-866.2 kcal/ mol), and MHC-II (-9043.3 kcal/mol). Based on computational modeling, we expect the aerolysin MEV candidate to activate diverse immune mechanisms, stimulate robust responses against A. hydrophila, and maintain safety. The significant solubility, absence of toxicity and allergic response contribute to the potential clinical utility of this vaccine candidate.
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spelling upm-1147782025-01-31T02:54:34Z http://psasir.upm.edu.my/id/eprint/114778/ Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach Rozi, . Tyasningsih, Wiwiek Rahmahani, Jola Aksono, Eduardus Bimo Yunus, Muchammad Al Arif, Mohammad Anam Kuncorojati, Suryo Kusdarwati, Rahayu Sari, Putri Desi Wulan Azmai, Mohammad Noor Amal Salleh, Annas Khanand, Nadeem Suwarno, . Aeromonas hydrophila, a gram-negative bacterium, is a major pathogen responsible for various diseases in mammals, reptiles, amphibians, fish, and humans. Targeting the specific toxin aerolysin in A. hydrophila is crucial to address antibiotic resistance and the lack of adequate and protective vaccines against this intracellular and extracellular pathogen. This study aimed to identify a multi-epitope vaccine (MEV) candidate targeting the aerolysin toxin to combat the disease effectively. Standard biochemical characterization methods, detection of PCR, and sequencing of the 16S rRNA, rpoB, and aerA genes identified the isolate AHSA1 as A. hydrophila isolated from O. goramy. Subsequently, we identified B and T cell epitopes on the aerolysin protein and predicted MHC-I and MHC-II epitopes. The epitopes were then evaluated for toxicity, antigenicity, allergenicity, and solubility. The vaccine design integrated multi-epitope constructs, utilizing specialized linkers (GPGPG and EAAAK) to connect epitope peptides with the cholera toxin B subunit as an adjuvant, thereby enhancing immunogenicity. Ramachandran plots showed that 85.25% of the residues were in the most favorable regions, followed by additionally allowed regions (10.80%), generously allowed regions (1.30%), and disallowed regions (2.65%), confirming the feasibility of the modeled vaccine design. Based on docking simulations, the MEV had strong binding energies with TLR-4 (-1081.4 kcal/mol), TLR-9 (-723.2 kcal/mol), MHC-I (-866.2 kcal/ mol), and MHC-II (-9043.3 kcal/mol). Based on computational modeling, we expect the aerolysin MEV candidate to activate diverse immune mechanisms, stimulate robust responses against A. hydrophila, and maintain safety. The significant solubility, absence of toxicity and allergic response contribute to the potential clinical utility of this vaccine candidate. Faculty of Fisheries and Marine Universitas Airlangga 2024-10-23 Article PeerReviewed text en cc_by_nc_sa_4 http://psasir.upm.edu.my/id/eprint/114778/1/114778.pdf Rozi, . and Tyasningsih, Wiwiek and Rahmahani, Jola and Aksono, Eduardus Bimo and Yunus, Muchammad and Al Arif, Mohammad Anam and Kuncorojati, Suryo and Kusdarwati, Rahayu and Sari, Putri Desi Wulan and Azmai, Mohammad Noor Amal and Salleh, Annas and Khanand, Nadeem and Suwarno, . (2024) Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach. Jurnal Ilmiah Perikanan dan Kelautan, 16 (2). pp. 298-321. ISSN 2085-5842; eISSN: 2528-0759 https://e-journal.unair.ac.id/JIPK/article/view/62035 10.20473/jipk.v16i2.62035
spellingShingle Rozi, .
Tyasningsih, Wiwiek
Rahmahani, Jola
Aksono, Eduardus Bimo
Yunus, Muchammad
Al Arif, Mohammad Anam
Kuncorojati, Suryo
Kusdarwati, Rahayu
Sari, Putri Desi Wulan
Azmai, Mohammad Noor Amal
Salleh, Annas
Khanand, Nadeem
Suwarno, .
Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach
title Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach
title_full Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach
title_fullStr Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach
title_full_unstemmed Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach
title_short Designing a novel Aerolysin-based multiepitope vaccine against Aeromonas hydrophila isolated from Osphronemus goramy using reverse vaccinology: an in silico approach
title_sort designing a novel aerolysin-based multiepitope vaccine against aeromonas hydrophila isolated from osphronemus goramy using reverse vaccinology: an in silico approach
url http://psasir.upm.edu.my/id/eprint/114778/
http://psasir.upm.edu.my/id/eprint/114778/
http://psasir.upm.edu.my/id/eprint/114778/
http://psasir.upm.edu.my/id/eprint/114778/1/114778.pdf