Comprehensive Structural and Molecular Comparison of Spike Proteins of SARS CoV 2, SARS CoV and MERS CoV, and Their Interactions with ACE2
The severe acute respiratory syndrome coronavirus 2 (SARS CoV 2) has recently emerged in China and caused a disease called coronavirus disease 2019 (COVID 19) The virus quickly spread around the world, causing a sustained global outbreak. Although SARS CoV 2, and other coronaviruses, SARS CoV and Middle East respiratory syndrome CoV (MERS CoV) are highly similar genetically and at the protein production level, there are significant differences between them. Research has shown that the structural spike (S) protein plays an important role in the evolution and transmission of SARS CoV 2. So far, studies have shown that various genes encoding primarily for elements of S protein undergo frequent mutation. We have performed an in depth review of the literature covering the structural and mutational aspects of S protein in the context of SARS CoV 2, and compared them with those of SARS CoV and MERS CoV. Our analytical approach consisted in an initial genome and transcriptome analysis, followed by primary, secondary and tertiary protein structure analysis. Additionally, we investigated the potential effects of these differences on the S protein binding and interactions to angiotensin converting enzyme 2 (ACE2) and we established, after extensive analysis of previous research articles, that SARS CoV 2 and SARS CoV use different ends/regions in S protein receptor binding motif (RBM) and different types of interactions for their chief binding with ACE2. These differences may have significant implications on pathogenesis, entry and ability to infect intermediate hosts for these coronaviruses. This review comprehensively addresses in detail the variations in S protein, its receptor binding characteristics and detailed structural interactions, the process of cleavage involved in priming, as well as other differences between coronaviruses.
Cells