Study of Structural and Immunological Properties of Glycoprotein S of the East Respiratory Syndrome Coronavirus (MERS-CoV)

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.

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.

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.

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.