BackgroundEpstein-Barr virus (EBV) can cause cancer in people from around the world. There is no EBV vaccine available for use on a global scale. However, emerging evidence suggests that the epitope on the gp350/220 capsid protein may be developed into an EBV vaccine. Nevertheless, the production of small, single epitope is challenging of stability issues and possible alteration of peptide structure. In this study, a tandem epitope was developed consisting of three single epitopes, aimed to improve stability, antigenicity and preserve epitope structure.Materials and methodsA tandem epitope was designed using bioinformatics based on the epitope structure of the gp350/220 protein. The tandem epitope structure was analyzed using a protein folding method with Abalone software, which was further refined via YASARA force field and molecular repairing using a FoldX method. Immunogenicity was examined with Epitopia software, whereas allergen properties were tested using AlgPred. The pattern of the tandem epitope binding with anti-gp350/220 antibodies was performed using Z-dock and snugDock. The tandem epitope was then overproduced in E. coli strain BL21 as a host cell.ResultOur model demonstrated a successfully designed and overproduced tandem epitope. The tandem epitope demonstrated a similar structure compared with the epitope of whole protein gp350/220. Our epitope also demonstrated non-allergen and antigenicity properties, and possessed antibody binding patterns consistent with whole protein gp350/220.Conclusion and recommendationThese data suggest a novel tandem epitope composed of three similar epitopes demonstrates antigenicity, structure, and binding properties consistent with whole protein gp350/220. We also demonstrate successful production of the tandem epitope using E. coli strain BL21 as a host. Future in vivo experimental animal research is necessary to test the ability of this tandem epitope to stimulate antibody production.

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Glutathione (GSH) is an antioxidant that functions to protect cells from oxidative stress. It is used for medical purposes, as an additive in foods and cosmetics industry. The magnitude of these applications results in increased demand for glutathione every year, however, the cost of glutathione is high. The production of glutathione using an alternative source for the medium and the amino acids used in the media might be the solution for managing the high cost of glutathione production in yeast. This study uses an alternative media based on papaya and fish extract to reduce production costs. The fish extract contains glutamate, cysteine and glycine that can be utilised as a source of amino acid. This study suggested that media based on papaya extract could be employed to produce glutathione in yeast Saccharomyces cerevisiae. Moreover, administration of 5 mg/mL of fish extract could increase the glutathione production up to 36.36% as compared to a control. The optimum production of glutathione was obtained in a harvest time of 44 h culture. Therefore, further investigation by modifying the medium is warranted to produce glutathione in a cost friendly manner in the S. cerevisiae.