Search published articles
Showing 2 results for Rbd
Majid Sadeghizadeh, Narges Moazzezi Tehrankhah,
Volume 15, Issue 3 (6-2024)
Abstract
The countries’ social and economic conditions have been threatened by corona epidemic and a large number of people’s death in the world. SARS-CoV-2 virus, a form of corona virus family, is responsible for corona disease and its spread in the present century. The study of the receptor binding region (RBD) in the spike protein is very important for scientists because the new corona virus uses its surface spike protein for binding to the ACE2 surface protein and entering its genetic material to the host cells. By this protein and its receptor binding region inhibition, the prevention of virus entrance to the cell is possible. The virus’s genes can be multiplied by cloning and its protein can be purified. The usage of antiviral peptides as the most practical methods and binding inhibitory peptides of RBD to the ACE2 receptor for SARS-CoV-2 treatment, are of great interest to scientists. In the present research, RBD cloning in PET28a expression vector, RBD protein expression and GFP/RBD fusion protein were performed in prokaryotic host. Due to this protein’s insolubility in the prokaryotic host, column refolding was performed with urea gradient with a nickel-agarose column and the synthesized protein was confirmed through western blot technique. Three nominated peptides from articles used to compare their binding to RBD using bioinformatics and their tendency to bind to each other was investigated by molecular docking. The mentioned peptides can be used in this virus infection treatment due to their binding potential to RBD, if their interaction is proven.
Volume 23, Issue 1 (1-2020)
Abstract
Aims: No definitive treatment or effective vaccine has been suggested against the East Respiratory Syndrome Coronavirus (MERS-CoV) virus which indicates the growing importance of the study of this virus. Amongst all MERS proteins, glycoprotein S has always been the main candidate for vaccine research against this virus, due to its function and structure. The aim of the present study was to investigate the structural, functional, and immunological properties of S protein using bioinformatics software that paves the way for designing an effective vaccine against this virus.
Materials & Methods: 35 glycoprotein S sequences of MERS were obtained from Genbank and amino acid changes were investigated. In addition, sequences were analyzed by various software for post-translational changes. Five types of software were used to evaluate the immunologic and allergenic properties. Finally, different structural aspects of this protein were predicted by SOPMA software.
Findings: The highest prevalence substitutions were found in amino acids of 95, 123, and 696 and the results indicate that there are four B-cell epitopes in glycoprotein S, and this protein has been affected by post-translational changes, including glycosylation and phosphorylation. This protein has no allergenic properties and the majority of its structure contains Alpha helix.
Conclusion: Glycoprotein S, especially in the RBD region of S1, has a high potential to induce the host immune system and the other features mentioned protein make it appropriate for the production of recombinant protein, including stability in host cells. Therefore, the use of glycoprotein S, especially S1, is recommended as a suitable candidate for vaccine design.
