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Energetics of Spike Protein Opening of SARS-CoV-1 and SARS-CoV-2 and Its Variants of Concern: Implications in Host Receptor Scanning and Transmission.
Singh, Jasdeep; Vashishtha, Shubham; Rahman, Syed Asad; Ehtesham, Nasreen Zafar; Alam, Anwar; Kundu, Bishwajit; Dobrindt, Ulrich.
Afiliación
  • Singh J; Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology-Delhi, Hauz Khas, New Delhi 110016, India.
  • Vashishtha S; Kusuma School of Biological Sciences, Indian Institute of Technology-Delhi, Hauz Khas, New Delhi 110016, India.
  • Rahman SA; BioInception Pvt. Ltd., Future Business Centre, Kings Hedges Road, Cambridge CB4 2HY, U.K.
  • Ehtesham NZ; ICMR National Institute of Pathology, Safdarjung Hospital Campus, New Delhi 110029, India.
  • Alam A; ICMR National Institute of Pathology, Safdarjung Hospital Campus, New Delhi 110029, India.
  • Kundu B; Kusuma School of Biological Sciences, Indian Institute of Technology-Delhi, Hauz Khas, New Delhi 110016, India.
  • Dobrindt U; Institute of Hygiene, University of Münster, Münster 48149, Germany.
Biochemistry ; 61(20): 2188-2197, 2022 10 18.
Article en En | MEDLINE | ID: mdl-36166360
The receptor binding domain(s) (RBD) of spike (S) proteins of SARS-CoV-1 and SARS-CoV-2 (severe acute respiratory syndrome coronavirus) undergoes closed to open transition to engage with host ACE2 receptors. In this study, using multi atomistic (equilibrium) and targeted (non-equilibrium) molecular dynamics simulations, we have compared energetics of RBD opening pathways in full-length (modeled from cryo-EM structures) S proteins of SARS-CoV-1 and SARS-CoV-2. Our data indicate that amino acid variations at the RBD interaction interface can culminate into distinct free energy landscapes of RBD opening in these S proteins. We further report that mutations in the S protein of SARS-CoV-2 variants of concern can reduce the protein-protein interaction affinity of RBD(s) with its neighboring domains and could favor its opening to access ACE2 receptors. The findings can also aid in predicting the impact of future mutations on the rate of S protein opening for rapid host receptor scanning.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glicoproteína de la Espiga del Coronavirus / SARS-CoV-2 Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochemistry Año: 2022 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Glicoproteína de la Espiga del Coronavirus / SARS-CoV-2 Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Revista: Biochemistry Año: 2022 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos