Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2.

ABSTRACT: SARS-CoV-2 infects cells by attachment to its receptor-the angiotensin converting enzyme 2 (ACE2). Regardless of the wealth of structural data, little is known about the physicochemical mechanism of interactions of the viral spike (S) protein with ACE2 and how this mechanism has evolved during the pandemic. Here, we applied experimental and computational approaches to characterize the molecular interaction of S proteins from SARS-CoV-2 variants of concern (VOC). Data on kinetics, activation-, and equilibrium thermodynamics of binding of the receptor binding domain (RBD) from VOC with ACE2 as well as data from computational protein electrostatics revealed a profound remodeling of the physicochemical characteristics of the interaction during the evolution. Thus, as compared to RBDs from Wuha

SUBMITTER: Planchais C 

PROVIDER: S-EPMC9597384 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature