Unveiling the SARS-CoV-2 Spike Protein: A Comparative Analysis of Vaccine Development Approaches and Glycosylation Implications

In December 2019, a mysterious pneumonia-causing sickness frightened the world. SARS-CoV-2 caused the acute respiratory illness. Since March 11, 2020, 220,563,227 COVID-19 cases and 4,565,483 deaths have been reported worldwide as of October 2021. SARS-CoV-2, like all coronavirus, appears to have crowns due to its S proteins and enters host cells using highly glycosylated spike (S) proteins. S1 and S2 are SARS-CoV-2 spike protein subunits. S2 controls transmembrane fusion, while S1 controls receptor binding. Antibody-mediated neutralization targets SARS-CoV-2 spike (S) proteins, which are essential for viral entry and fusion. This paper summarized how S protein was used in newly created and distributed SARS-CoV-2 vaccines and the implications for future advancements given the emergence of more lethal SARS-CoV-2 variants in this paper. It also discussed the role of S protein glycosylation in the viral entry and binding mechanism of SARS-CoV-2 and the implications for developing adaptive immunity and vaccines. The review was carried out through a deductive search strategy with keywords: COVID-19 vaccines, nCoV-2019 vaccines, coronavirus, COVID-19 vaccine development, S protein, and protein glycosylation using Google Scholar. The emergence of more transmissible and potentially more lethal SARS-CoV-2 variants, such as the Delta variant, highlights the need for continued research on vaccine development. Future research should focus on understanding the mechanism of the spike protein and how vaccines can effectively target the mutated regions. Continued monitoring and adaptation of vaccination strategies are essential to control the ongoing COVID-19 pandemic.