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Exploring the Potentials of Campylobacter spp. Chaperone Proteins in the Design of B and T Cell Multi-Epitope Subunit Vaccine: An Immunoinformatics approach | Abstract

Der Pharma Chemica
Journal for Medicinal Chemistry, Pharmaceutical Chemistry, Pharmaceutical Sciences and Computational Chemistry

ISSN: 0975-413X
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Abstract

Exploring the Potentials of Campylobacter spp. Chaperone Proteins in the Design of B and T Cell Multi-Epitope Subunit Vaccine: An Immunoinformatics approach

Author(s): Kaka MO*, Adeosun IJ, Olotu TM, Oyebamiji AK, Ajayeoba TA and Oyawoye OM

Campylobacter has been reported to be the cause of community-acquired infection and is often presented in immunocompromised individuals as acute gastrointestinal illness. It is also often transmitted through undercooked poultry products. Campylobacter also causes significant morbidity, leading to huge cases of disability but limited mortality (there can be about 75,000 annual fatal cases). Heat shock proteins are defined as a group of highly conserved and regulated proteins which are known to play vital roles in enabling diverse organisms cope with physiological stress. Thus, this study used an immunoinformatic approach to design a multi-epitope based vaccine that is targeted against Campylobacter spp. and related infections using Heat shock protein sequences. Designed subunit vaccine was evaluated for its antigenicity, immunogenicity, allergenicity and physicochemical parameters. A total of 7200 CTL epitopes (9-mer) were predicted using Net CTL 1.2 server, among them only 97 epitopes with high ranked binding affinity score were chosen as final CTL epitopes. Similarly, the HTL epitopes were identified using IEDB MHC-II prediction module based on the higher binding affinity with MHC- II, the mouse alleles used for the prediction were HLA-DRB1*01:01, HLA-DRB1*01:02, HLA-DRB1* 01:03, HLA-DRB1*01:04. A maximum immune response TLR-5 agonist (Accession number: P04949) was used as an adjuvant and CTL epitopes were combined together by EAAAK linker, intra-CTL and intra-HTL epitopes joint by AAY and GPGPG linker to make a final vaccine construct of 1723 amino acid residues designed using 97 CTL and 3 HTL epitopes Collectively, this research provides novel candidates for epitope-based peptide vaccine design against Campylobacter spp.


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