Conformational flexibility and structural variability of SARS-CoV2 S protein

Pramanick, I and Sengupta, N and Mishra, S and Pandey, S and Girish, N and Das, A and Dutta, S (2021) Conformational flexibility and structural variability of SARS-CoV2 S protein. In: Structure, 29 (8). 834-845.e5.

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Abstract

Spike (S) glycoprotein of SARS-CoV2 exists chiefly in two conformations, open and closed. Most previous structural studies on S protein have been conducted at pH 8.0, but knowledge of the conformational propensities under both physiological and endosomal pH conditions is important to inform vaccine development. Our current study employed single-particle cryoelectron microscopy to visualize multiple states of open and closed conformations of S protein at physiological pH 7.4 and near-physiological pH 6.5 and pH 8.0. Propensities of open and closed conformations were found to differ with pH changes, whereby around 68 of S protein exists in open conformation at pH 7.4. Furthermore, we noticed a continuous movement in the N-terminal domain, receptor-binding domain (RBD), S2 domain, and stalk domain of S protein conformations at various pH values. Several key residues involving RBD-neutralizing epitopes are differentially exposed in each conformation. This study will assist in developing novel therapeutic measures against SARS-CoV2. © 2021 Elsevier Ltd

Item Type:	Journal Article
Publication:	Structure
Publisher:	Cell Press
Additional Information:	The copyright for this article belongs to Authors
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	25 Sep 2021 13:34
Last Modified:	25 Sep 2021 13:34
URI:	http://eprints.iisc.ac.in/id/eprint/69814

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