The emergence of a rapidly spreading and highly infectious COVID-19 outbreak by a novel coronavirus, Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), has caused a global pandemic with unprecedented, social and economic dimensions. Therefore, the development of effective strategies is urgent to control COVID-19 outbreak. According to the recent investigations, cell entry of coronaviruses relies on binding of the viral spike glycoprotein to the host cellular receptors. Therefore, in the present study aimed to predict immunogenic epitopes in silico by analyzed spike protein. In parallel, by screening the immunogenic SARS-CoV-2 spike derived epitopes provided in the literature, we chose a set of epitopes believed to induce immunogenic response. Next, we provided the selected epitopes from both approaches, we performed immunoinformatic analysis that map identically to antigen regions and have antigenic properties. Finally, by suggesting a screened set of epitopes, we designed a novel virus-like particle (VLP) vaccine, optimized to be produced in plants by using molecular farming biotechnology techniques. We anticipate our assay to be a starting point for guiding experimental efforts toward the development of a vaccine against SARS-CoV-2.

Highlights Virus-like particles -based vaccines have attracted great interest as the next generation of vaccines due to their safety profile, efficacy, shorter production times, and ability to induce both cellular and humoral immunity. The production of HBc-based virus-like particles in plants would thus greatly increase the efficiency of vaccine production. This review investigates the application of plant-based HBc VLP as a platform for vaccine production.

In contrast to conventional antibiotics, which microorganisms can readily evade, it is nearly impossible for a microbial strain that is sensitive to antimicrobial proteins to convert to a resistant strain. Therefore, antimicrobial proteins and peptides that are promising alternative candidates for the control of bacterial infections are under investigation. The MAP30 protein of Momordica charantia is a valuable type I ribosome-inactivating protein (RIP) with anti-HIV and anti-tumor activities. Whereas the antimicrobial activity of some type I RIPs has been confirmed, less attention has been paid to the antimicrobial activity of MAP30 produced in a stable, easily handled, and extremely cost-effective protein-expression system. rMAP30-KDEL was expressed in Nicotiana tobacum hairy roots, and its effect on different microorganisms was investigated. Analysis of the extracted total proteins of transgenic hairy roots showed that rMAP30-KDEL was expressed effectively and that this protein exhibited significant antibacterial activity in a dose-dependent manner. rMAP30-KDEL also possessed thermal and pH stability. Bioinformatic analysis of MAP30 and other RIPs regarding their conserved motifs, amino-acid contents, charge, aliphatic index, GRAVY value, and secondary structures demonstrated that these factors accounted for their thermophilicity. Therefore, RIPs such as MAP30 and its derived peptides might have promising applications as food preservatives, and their analysis might provide useful insights into designing clinically applicable antibiotic agents.

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