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Conformational flexibility and structural variability of SARS-CoV2 S protein.
Pramanick, Ishika; Sengupta, Nayanika; Mishra, Suman; Pandey, Suman; Girish, Nidhi; Das, Alakta; Dutta, Somnath.
  • Pramanick I; Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
  • Sengupta N; Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
  • Mishra S; Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
  • Pandey S; Mynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
  • Girish N; Mynvax Private Limited, ES12, Entrepreneurship Centre, SID, Indian Institute of Science, Bengaluru, India.
  • Das A; Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
  • Dutta S; Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India. Electronic address: somnath@iisc.ac.in.
Structure ; 29(8): 834-845.e5, 2021 08 05.
Article in English | MEDLINE | ID: covidwho-1208677
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / SARS-CoV-2 Topics: Vaccines Limits: Humans Language: English Journal: Structure Journal subject: Molecular Biology / Biochemistry / Biotechnology Year: 2021 Document Type: Article Affiliation country: J.str.2021.04.006

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Spike Glycoprotein, Coronavirus / SARS-CoV-2 Topics: Vaccines Limits: Humans Language: English Journal: Structure Journal subject: Molecular Biology / Biochemistry / Biotechnology Year: 2021 Document Type: Article Affiliation country: J.str.2021.04.006