SARS-CoV-1 and SARS-CoV-2 spike proteins utilize different mechanisms to bind to ACE2 ACE2 Angiotensin Coronavirus COVID MERSCoV SARSCoV2 FrontMicrobiol UTEP HowardU
By Nidhi Saha, BDSDec 11 2022Reviewed by Benedette Cuffari, M.Sc. A recent study published in the journal Frontiers in Molecular Biosciences applied computational approaches to study the binding mechanisms of the severe acute respiratory syndrome coronavirus 2 and SARS-CoV spike proteins to the human angiotensin-converting enzyme 2 receptor.
In addition to SARS-CoV-2, other viruses that belong to the Coronaviridae family include the Middle East respiratory syndrome coronavirus and SARS-CoV, both of which led to epidemics in 2012 and 2003, respectively. These coronaviruses consist of four primary structural proteins, of which include the S, envelope , membrane , and nucleocapsid proteins.
The gross structure of both the SARS-CoV and SARS-CoV-2 S protein RBDs were found to be very similar. However, certain differences in several loops were identified and can be attributed to the high loop flexibility and differences in the amino acids that comprise these viral proteins. Both SARS-CoV-2 and SARS-CoV complex structures exhibited similar in the field lines. Field lines connecting ACE2 and both S proteins had high densities surrounding the surfaces, thus indicating strong attractive forces between the ACE2 protein and the S protein RBD of both viruses.
A comparison of the electrostatic forces of both the SARS-CoV-2 and SARS-CoV RBDs revealed that the SARS-CoV-2 RBD exhibits a greater net force as compared to that of SARS-CoV-2 alone. This may be attributed to differences in the charge distributions between these two binding domains. Despite a weaker attractive force, the increased flexibility of the SARS-CoV-2 RBD likely allows for it to open and subsequently bind to ACE2 with greater ease.
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