Mass photometry reveals SARS-CoV-2 spike stabilisation to impede ACE2 binding through altered conformational dynamics.

Burnap, Sean A; Struwe, Weston B

Burnap, Sean A; Struwe, Weston B.

Burnap SA; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3TA, UK. weston.struwe@chem.ox.ac.uk.
Struwe WB; The Kavli Institute for Nanoscience Discovery, Dorothy Crowfoot Hodgkin Building, South Parks Road, OX1 3QU, UK.

Chem Commun (Camb) ; 58(93): 12939-12942, 2022 Nov 22.

Article in English | MEDLINE | ID: covidwho-2096844

ABSTRACT

ABSTRACT

Here we show using mass photometry how proline substitutions, commonly used for SARS-CoV-2 spike stabilisation in vaccine design, directly affects ACE2 receptor interactions via dynamics of open and closed states. Conformational changes and ACE2 binding were influenced by spike variant and temperature, but independent of site-specific N-glycosylation.

Subject(s)

COVID-19; SARS-CoV-2; Humans; Angiotensin-Converting Enzyme 2; Spike Glycoprotein, Coronavirus/chemistry; Peptidyl-Dipeptidase A/metabolism; Receptors, Virus/chemistry; Receptors, Virus/metabolism; Protein Binding; Photometry; Molecular Dynamics Simulation; Binding Sites

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Topics: Vaccines / Variants Limits: Humans Language: English Journal: Chem Commun (Camb) Journal subject: Chemistry Year: 2022 Document Type: Article Affiliation country: D2cc04711j

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