Design, expression, and purification of a multi-epitope vaccine against Helicobacter Pylori based on Melittin as an adjuvant

Jafari, Elham; Mahmoodi, Shirin

doi:10.1016/j.micpath.2021.104970

Cited by 17 publications

(12 citation statements)

References 51 publications

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“…In the second step, the presence of a signal peptide was predicted using SignalP online tool in all proteins but not in MSP4, MSP6, Ralp1, RESA, Rh5, and Ron2. Signal peptides destine a protein towards a secretory route and for different functions including secretory-excretory antigen, structural molecule, and/or as a virulence factor [ 74 – 76 ]. Based on deep TMHMM tool, only AMA1 and RESA had a single transmembrane domain.…”

Section: Discussionmentioning

confidence: 99%

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Computational Clues of Immunogenic Hotspots in Plasmodium falciparum Erythrocytic Stage Vaccine Candidate Antigens: In Silico Approach

Azimi-Resketi

Heydaryan

Kumar

et al. 2022

BioMed Research International

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Malaria is the most pernicious parasitic infection, and Plasmodium falciparum is the most virulent species with substantial morbidity and mortality worldwide. The present in silico investigation was performed to reveal the biophysical characteristics and immunogenic epitopes of the 14 blood-stage proteins of the P. falciparum using comprehensive immunoinformatics approaches. For this aim, various web servers were employed to predict subcellular localization, antigenicity, allergenicity, solubility, physicochemical properties, posttranslational modification sites (PTMs), the presence of signal peptide, and transmembrane domains. Moreover, structural analysis for secondary and 3D model predictions were performed for all and stable proteins, respectively. Finally, human helper T lymphocyte (HTL) epitopes were predicted using HLA reference set of IEDB server and screened in terms of antigenicity, allergenicity, and IFN-γ induction as well as population coverage. Also, a multiserver B-cell epitope prediction was done with subsequent screening for antigenicity, allergenicity, and solubility. Altogether, these proteins showed appropriate antigenicity, abundant PTMs, and many B-cell and HTL epitopes, which could be directed for future vaccination studies in the context of multiepitope vaccine design.

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Section: Discussionmentioning

confidence: 99%

“…molecule, and/or as a virulence factor[74][75][76]. Based on deep TMHMM tool, only AMA1 and RESA had a single transmembrane domain.…”

mentioning

confidence: 99%

Computational Clues of Immunogenic Hotspots in Plasmodium falciparum Erythrocytic Stage Vaccine Candidate Antigens: In Silico Approach

Azimi-Resketi

Heydaryan

Kumar

et al. 2022

BioMed Research International

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“…A multi-epitope-based vaccine construct consists of different types of epitopes, rather than a single epitope. The vaccine construct is designed by linking screened epitopes with each other through specific linkers, i.e., GPGPG linkers for the purpose of overcoming the limitations of single-peptide-based vaccines that are unable to generate effective immune responses against variants of the same pathogen [97]. Another linker, i.e., EAAAK, is used to link the adjuvant CTBS, to enhance the immune efficacy of the vaccine construct [98].…”

Section: Multi-epitope Vaccine Construction and Processingmentioning

confidence: 99%

Designing a Recombinant Vaccine against Providencia rettgeri Using Immunoinformatics Approach

et al. 2022

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Antibiotic resistance (AR) is the resistance mechanism pattern in bacteria that evolves over some time, thus protecting the bacteria against antibiotics. AR is due to bacterial evolution to make itself fit to changing environmental conditions in a quest for survival of the fittest. AR has emerged due to the misuse and overuse of antimicrobial drugs, and few antibiotics are now left to deal with these superbug infections. To combat AR, vaccination is an effective method, used either therapeutically or prophylactically. In the current study, an in silico approach was applied for the design of multi-epitope-based vaccines against Providencia rettgeri, a major cause of traveler’s diarrhea. A total of six proteins: fimbrial protein, flagellar hook protein (FlgE), flagellar basal body L-ring protein (FlgH), flagellar hook-basal body complex protein (FliE), flagellar basal body P-ring formation protein (FlgA), and Gram-negative pili assembly chaperone domain proteins, were considered as vaccine targets and were utilized for B- and T-cell epitope prediction. The predicted epitopes were assessed for allergenicity, antigenicity, virulence, toxicity, and solubility. Moreover, filtered epitopes were utilized in multi-epitope vaccine construction. The predicted epitopes were joined with each other through specific GPGPG linkers and were joined with cholera toxin B subunit adjuvant via another EAAAK linker in order to enhance the efficacy of the designed vaccine. Docking studies of the designed vaccine construct were performed with MHC-I (PDB ID: 1I1Y), MHC-II (1KG0), and TLR-4 (4G8A). Findings of the docking study were validated through molecular dynamic simulations, which confirmed that the designed vaccine showed strong interactions with the immune receptors, and that the epitopes were exposed to the host immune system for proper recognition and processing. Additionally, binding free energies were estimated, which highlighted both electrostatic energy and van der Waals forces to make the complexes stable. Briefly, findings of the current study are promising and may help experimental vaccinologists to formulate a novel multi-epitope vaccine against P. rettgeri.

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“…The immune effects of MEL make it an effective adjuvant for vaccines. Owing to its ability to increase IFN-γ and IL-1β and decrease IL-10, MEL was selected as suitable adjuvant candidate for Helicobacter pylori intranasal vaccine development [ 150 ]. After deletion of the last four residues of the C-terminal region, with the aim of lowering the interactions with the cell membranes, the derived MEL peptide was linked to epitopes as an adjuvant.…”

Section: Nano Drug Delivery System With Melittin As a Functional Moleculementioning

confidence: 99%

Melittin-Based Nano-Delivery Systems for Cancer Therapy

et al. 2022

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Melittin (MEL) is a 26-amino acid polypeptide with a variety of pharmacological and toxicological effects, which include strong surface activity on cell lipid membranes, hemolytic activity, and potential anti-tumor properties. However, the clinical application of melittin is restricted due to its severe hemolytic activity. Different nanocarrier systems have been developed to achieve stable loading, side effects shielding, and tumor-targeted delivery, such as liposomes, cationic polymers, lipodisks, etc. In addition, MEL can be modified on nano drugs as a non-selective cytolytic peptide to enhance cellular uptake and endosomal/lysosomal escape. In this review, we discuss recent advances in MEL’s nano-delivery systems and MEL-modified nano drug carriers for cancer therapy.

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Design, expression, and purification of a multi-epitope vaccine against Helicobacter Pylori based on Melittin as an adjuvant

Cited by 17 publications

References 51 publications

Computational Clues of Immunogenic Hotspots in Plasmodium falciparum Erythrocytic Stage Vaccine Candidate Antigens: In Silico Approach

Computational Clues of Immunogenic Hotspots in Plasmodium falciparum Erythrocytic Stage Vaccine Candidate Antigens: In Silico Approach

Designing a Recombinant Vaccine against Providencia rettgeri Using Immunoinformatics Approach

Melittin-Based Nano-Delivery Systems for Cancer Therapy

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