Mutational landscape and in silico structure models of SARS-CoV-2 spike receptor binding domain reveal key molecular determinants for virus-host interaction.

BMC Molecular and Cell Biology   (2022) 23:2|

Shijulal Nelson-Sathi , P. K. Umasankar, E. Sreekumar, R. Radhakrishnan Nair, Iype Joseph,Sai Ravi Chandra Nori, Jamiema Sara Philip, Roshny Prasad, K. V. Navyasree1, Shikha Ramesh, Heera Pillai,Sanu Ghosh, T. R. Santosh Kumar and M. Radhakrishna Pillai


SARS-CoV-2, the causative agent of COVID-19 pandemic is a RNA virus prone to mutations. Formation of a stable binding interface between the Receptor Binding Domain (RBD) of SARS-CoV-2 Spike (S) protein and Angiotensin-Converting Enzyme 2 (ACE2) of host is pivotal for viral entry. RBD has been shown to mutate frequently during pandemic. Although, a few mutations in RBD exhibit enhanced transmission rates leading to rise of new variants of concern, most RBD mutations show sustained ACE2 binding and virus infectivity. Yet, how all these mutations make the binding interface constantly favourable for virus remain enigmatic. This study aims to delineate molecular rearrangements in the binding interface of SARS-CoV-2 RBD mutants


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